Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,5-dinitrophenyl-beta-D-xylobioside + H2O
?
-
-
-
?
2-chloro-4-nitrophenyl beta-D-xylobioside + H2O
?
-
-
-
-
?
2-nitrophenyl xylopyranoside + H2O
2-nitrophenol + xylopyranose
-
-
-
-
?
4-deoxy-hexenuronosylxylan + H2O
?
-
-
-
-
?
4-methoxyphenol + H2O
?
weak transxylosylation activity
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
?
-
-
-
-
?
4-methylumbelliferyl-beta-xylobiose + H2O
?
-
enzyme cleaves at the second glycosidic bond adjacent to the aglycon
-
-
?
4-methylumbelliferyl-beta-xylotriose + H2O
?
-
highly preferred substrate, enzyme cleaves at the second glycosidic bond adjacent to the aglycon
-
-
?
4-methylumbelliferyl-xylobiose + H2O
?
-
hydrolysis at the glycosidic linkage
-
-
?
4-methylumbelliferyl-xylotriose + H2O
?
-
hydrolysis at the glycosidic linkage
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] + H2O
?
4-nitrophenyl 4-O-beta-D-xylopyranosyl-beta-D-xylopyranoside + H2O
4-nitrophenol + 4-O-beta-D-xylopyranosyl-beta-D-xylopyranose
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinopyranose
-
-
-
-
?
4-nitrophenyl arabinofuranoside + H2O
4-nitrophenol + arabinofuranose
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
4-nitrophenyl beta-D-xylobioside + H2O
?
-
-
-
?
4-nitrophenyl beta-D-xylopyranose + H2O
4-nitrophenol + D-xylopyranose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside
4-nitrophenol + beta-D-xylopyranose
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
4-nitrophenyl beta-D-xylose + H2O
4-nitrophenol + D-xylose
-
-
-
?
4-nitrophenyl beta-D-xylotrioside + H2O
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
4-nitrophenyl xylopyranoside + H2O
4-nitrophenol + xylopyranose
4-nitrophenyl-4-O-beta-D-xylopyranosyl-beta-D-xylopyranose + H2O
?
-
-
-
-
?
4-O methyl-glucuronoxylan + H2O
?
moderate activity
-
-
?
4-O-methyl glucuronoxylan + H2O
?
-
-
-
-
?
4-O-methyl-beta-D-glucuronopyranosyl-1,2-(beta-1,4-xylan) + H2O
?
4-O-methyl-beta-D-glucuronoxylan + H2O
?
4-O-methyl-D-glucurono-D-xylan + H2O
?
4-O-methyl-D-glucurono-D-xylan + H2O
xylo-oligosaccharides + ?
4-O-methyl-D-glucuronoxylan + H2O
?
4-O-methyl-D-glucuronoxylan + H2O
xylose + xylobiose + ?
-
from beechwood
main products, also release of acidic xylooligosaccharides
-
?
4-O-methyl-glucuronoxylan + H2O
?
-
-
-
-
?
4-O-methylglucurono-D-xylan + H2O
?
acetylhemicellulose + H2O
hemicellulose + acetate
aldotetraouronic acid + H2O
D-xylose + ?
-
-
produced only by XynC, from the reducing end of substrate
-
?
amylopectin + H2O
?
-
-
-
-
?
arabinoxylan + H2O
arabinose + xylose + xylobiose
-
-
-
-
?
arabinoxylan + H2O
D-xylose + ?
-
wheat arabinoxylan substrates with different arabinose to xylose ratio
-
-
?
arabinoxylan + H2O
xylo-oligosaccharide + ?
arabinoxylan + H2O
xylo-oligosaccharides + ?
arabinoxylan + H2O
xylobiose + xylotriose + xylotetraose + ?
the enzyme is most active on xylans with high content of arabinose (rye arabinoxylan and wheat arabinoxylan) than on xylans with low content of arabinose (oat spelts xylan, birchwood xylan and beechwood xylan). It releases xylooligosaccharides but not xylose, indicating that XynA is an endoxylanase
-
-
?
arabinoxylan xylan + H2O
?
-
-
-
?
ascorbic acid + H2O
?
weak transxylosylation activity
-
-
?
azure cross link xylan
?
-
-
-
?
azurin-cross-linked arabinoxylan + H2O
?
azurin-cross-linked xylan + H2O
?
azurin-labelled birchwood xylan + H2O
?
azurine cross-linked arabinoxylan xylan + H2O
?
-
-
-
?
bagasse + H2O
xylo-oligosaccharides + ?
barley beta-glucan + H2O
?
beech wood xylan + H2O
xylobiose + ?
MK331807
hydrolysis of beechwood xylan in endo-action mode releasing xylobiose as its main end product
-
-
?
beechwood 4-O-methyl-D-glucuronoxylan + H2O
xylose + xylobiose + ?
beechwood glucuronoxylan + H2O
?
beechwood glucuronoxylan + H2O
aldotetraouronic acid + xylose
-
-
-
-
?
beechwood xylan + H2O
xylo-oligosaccharides
beechwood xylan + H2O
xylo-oligosaccharides + ?
beechwood xylan + H2O
xylobiose + ?
beechwood xylan + H2O
xylobiose + xylopentaose + ?
beechwood xylan + H2O
xylobiose + xylose + ?
best substrate
-
-
?
beechwood xylan + H2O
xylobiose + xylotriose
beechwood xylan + H2O
xylohexaose + ?
beechwood xylan + H2O
xylooligosaccharides + ?
-
-
-
?
beechwood xylan + H2O
xylose + ?
beechwood xylan + H2O
xylose + xylo-oligosaccharides
beechwood xylan + H2O
xylose + xylobiose + ?
beechwood xylan + H2O
xylose + xylobiose + xylopentaose + ?
-
-
-
?
beechwood xylan + H2O
xylose + xylobiose + xylotetraose
best substrate
-
-
?
beechwood xylan + H2O
xylose + xylotriose + xylobiose
beechwood xylan + H2O
xylotriose + xylotetraose + xylopentaose + ?
-
about 19.9% xylobiose, 33.6% xylotetraose, 40.6% xylopentaose plus some xylose and xylobiose
-
?
beta-1,4-D-glucan + H2O
?
beta-1,4-xylan + H2O
D-xylose + 1,4-beta-D-xylobiose + 1,4-beta-D-xylotriose + 1,4-beta-D-xylotetraose
from birchwood or oat spelt
from oat spelt xylan results 7.46% xylose, 28.36% xylobiose, 25.37% xylotriose, and 38.81% xylotetraose
-
?
beta-1,4-xylan + H2O
D-xylose + beta-1,4-xylobiose + ?
-
hydrolysis products comprise 20.1% xylose and 79.9% xylobiose
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharide + ?
beta-1,4-xylan + H2O
xylo-oligosaccharides
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
beta-1,4-xylan + H2O
xylooligosaccharides
beta-1,4-xylan + H2O
xylose + ?
beta-1,4-xylan + H2O
xylotriose + xylobiose + ?
-
from oat spelt, birchwood, or beechwood, specificity, overview
as the main degradation products of Xyn2
-
?
beta-1,4-xylan + H2O
xylotriose + xylotetraose + xylopentaose + xylopentaose + xylohexaose + xyloheptaose
beta-1,4-xylohexaose + H2O
?
-
-
-
?
beta-1,4-xylopentaose + H2O
?
-
-
-
?
beta-1,4-xylotetraose + H2O
?
-
-
-
?
birch wood xylan + H2O
D-xylose + ?
birch wood xylan + H2O
D-xylose + xylobiose + ?
birch wood xylan + H2O
xylobiose + xylotriose + xylose + ?
birch wood xylan + H2O
xylobiose + xylotriose + xylotetraose + ?
-
major products
-
?
birch wood xylan + H2O
xylose + xylobiose + ?
birch wood xylan + H2O
xylotriose + ?
birchwood xylan + H2O
D-xylose + ?
birchwood xylan + H2O
D-xylose + L-arabinose + xylobiose + ?
birchwood xylan + H2O
D-xylose + xylobiose + ?
birchwood xylan + H2O
D-xylose + xylobiose + xylotriose + ?
-
main hydrolysis product of xylan is xylobiose (more than 75%)
-
-
?
birchwood xylan + H2O
D-xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose
birchwood xylan + H2O
xylo-oligosaccharides
birchwood xylan + H2O
xylo-oligosaccharides + ?
birchwood xylan + H2O
xylobiose + ?
birchwood xylan + H2O
xylobiose + xylose + ?
-
-
xylobiose, 74% of products, plus 21% xylose
-
?
birchwood xylan + H2O
xylobiose + xylotetraose + ?
-
slightly lower activity than with beechwood xylan
-
-
?
birchwood xylan + H2O
xylobiose + xylotriose + ?
birchwood xylan + H2O
xylohexaose + ?
birchwood xylan + H2O
xylooligosaccharides
birchwood xylan + H2O
xylose + ?
birchwood xylan + H2O
xylose + xylo-oligosaccharides
birchwood xylan + H2O
xylose + xylobiose + ?
birchwood xylan + H2O
xylotetraose + xylotriose + xylobiose + xylose
-
hydrolysis product composition is 1.4% xylose, 37.1% xylobiose, 58.9% xylotriose and 2.6% xylotetraose
-
?
caffeic acid + H2O
?
weak transxylosylation activity
-
-
?
canola meal + H2O
xylo-glucuronic acid + xylobiose
-
main products
-
?
carboxylmethyl cellulose + H2O
?
carboxymethyl cellulose + H2O
?
carboxymethylcellulose + H2O
?
carboxymethylcellulose + H2O
cellobiose + cellooligomers
catechin + H2O
?
strong transxylosylation activity
-
-
?
catechol + H2O
?
strong transxylosylation activity
-
-
?
cell wall fragment + H2O
?
Xyn10A containing three SLH domains at its C-terminus can bind to cell wall fragments significantly (32%)
-
-
?
corn cob + H2O
?
-
56% of the activity with wheat bran
-
-
?
corncob + H2O
xylo-oligosaccharides + ?
corncob xylan + H2O
xylo-oligosaccharides + ?
corncob xylan + H2O
xylobiose + xylotriose + ?
corncob xylan + H2O
xylobiose + xylotriose + xylopentose + xylohexaose
cotton stalk + H2O
?
-
8.5% of the activity with wheat bran
-
-
?
delignified bagasse + H2O
?
-
-
-
-
?
DOPA + H2O
?
weak transxylosylation activity
-
-
?
dopamine + H2O
?
weak transxylosylation activity
-
-
?
fructose + H2O
?
weak transxylosylation activity
-
-
?
gallic acid + H2O
?
strong transxylosylation activity
-
-
?
glucuronoxylan + H2O
aldotetrauronic acid
-
-
-
-
?
glucuronoxylan + H2O
MeGlcA-alpha(1-2)-Xyl-beta(1-4)-Xyl-beta(1-4)-Xyl + ?
-
-
shortest acidic fragment
-
?
hydroquinone + H2O
?
strong transxylosylation activity
-
-
?
insoluble birchwood xylan + H2O
xylo-oligosaccharides + ?
insoluble oat spelt xylan + H2O
?
insoluble wheat arabinoxylan + H2O
?
-
-
-
?
insoluble xylan + H2O
?
-
-
-
?
kraft pulp
?
-
reduction of kappa number and increase in viscosity
-
-
?
larch xylan + H2O
?
-
-
-
-
?
larchwood xylan + H2O
?
-
-
-
-
?
larchwood xylan + H2O
xylobiose + xylotriose + ?
low-viscosity wheat arabinoxylan + H2O
?
mannitol + H2O
?
weak transxylosylation activity
-
-
?
marine beta-1,3-beta-1,4-xylan + H2O
?
-
-
-
?
medium viscosity wheat arabinoxylan + H2O
?
mixed-linkage (beta-1,3,beta-1,4) xylan + H2O
?
maximal activity against mixed-linkage polymeric xylans
-
-
?
mustard bran + H2O
xylo-glucuronic acid + xylobiose
-
main products
-
?
nutrient broth + H2O
?
strong transxylosylation activity
-
-
?
O-acetyl-4-O-glucuronoxylan + H2O
?
-
-
-
-
?
O-acetyl-4-O-methyl-D-glucuronoxylan + H2O
xylose + xylobiose
-
from beechwood
main products
-
?
O-acetyl-4-O-methyl-D-glucuronoxylan + H2O
xylose + xylobiose + ?
O-acetyl-4-O-methyl-glucuronoxylan + H2O
short-acetylated and non-acetylated fragments of 4-O-methyl-glucuronoxylan
-
-
-
-
?
oat bran + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
D-xylose + ?
oat spelt xylan + H2O
D-xylose + xylobiose + ?
oat spelt xylan + H2O
xylo-oligosaccharides
oat spelt xylan + H2O
xylo-oligosaccharides + ?
oat spelt xylan + H2O
xylobiose + ?
oat spelt xylan + H2O
xylobiose + D-xylose + xylotriose + ?
-
main hydrolysis product of xylan is xylobiose (more than 75%)
-
-
?
oat spelt xylan + H2O
xylobiose + xylotriose + ?
oat spelt xylan + H2O
xylose + ?
oat spelt xylan + H2O
xylose + xylobiose + xylopentaose + ?
-
-
-
?
oat spelt xylan + H2O
xylotriose + ?
oat spelts xylan + H2O
D-xylose + ?
oat speltxylan + H2O
xylose + xylo-oligosaccharides
oatspelt xylan + H2O
xylobiose + ?
p-nitrophenyl beta-D-cellobioside + H2O
?
p-nitrophenyl beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
p-nitrophenyl beta-D-xylopyranoside
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranoside
-
weak substrate for isoforms xynA, xynC, no substrate for xynB
-
-
?
p-nitrophenyl-beta-D-glucoside + H2O
?
-
hydrolysis with xylanase I, no activity with xylanase II
-
-
?
p-nitrophenyl-beta-D-xylobioside + H2O
?
phloroglucinol + H2O
?
weak transxylosylation activity
-
-
?
poplar stem + H2O
?
-
enzyme degrades approximately 45% of unsubstituted xylans in the cell wall from poplar stems
-
?
pustulan + H2O
?
-
slight activity with xylanase I, no activity with xylanase II
-
-
?
pyrogallol + H2O
?
strong transxylosylation activity
-
-
?
remazol brilliant blue xylan + H2O
?
Remazol brilliant blue-birchwood xylan + H2O
?
Remazol brilliant blue-carboxymethylcellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose + high-molecular-mass oligosaccharides
Remazol Brilliant Blue-Xylan + H2O
?
-
-
-
-
?
resorcinol + H2O
?
weak transxylosylation activity
-
-
?
rhodymenan + H2O
Xyl-beta(1-3)-Xyl-beta(1-4)-Xyl + ?
-
-
isomeric xylotriose
-
?
rhodymenan + H2O
xylose + xylobiose + ?
rhodymenan + H2O
xylose + xylobiose + xylotetraose + xylopentaose
-
from beechwood, a beta(1-4)-beta(1-3)-xylan
main products, isomeric oligosaccharides
-
?
rhodymenan + H2O
xylotriose + xylotetraose + ?
-
-
isoform XynB produces xylotriose, XynC produces xylotetraose
-
?
rice husk + H2O
?
-
-
-
-
?
rye flour xylan + H2O
xylo-oligosaccharides + ?
no exoxylanase activity on rye fluor xylan
-
-
?
sawdust + H2O
?
-
-
-
-
?
shorea leaf dust + H2O
?
-
-
-
-
?
sodium carboxymethyl cellulose + H2O
?
recombinant EGXA with a cellulose-binding domain binds to the cellulose with higher affinity than wild-type EGX, which lacks the cellulose-binding domain
-
-
?
soluble birchwood xylan + H2O
xylo-oligosaccharides + ?
soluble oat spelt xylan + H2O
?
soluble wheat arabinoxylan + H2O
?
steam-exploded aspenwood hemicellulose + H2O
?
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
sugar cane bagasse + H2O
?
sun flower stalk + H2O
?
-
11% of the activity with wheat bran
-
-
?
wheat arabinoxylan + H2O
?
wheat arabinoxylan + H2O
xylobiose
best substrate
-
-
?
wheat arabinoxylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
wheat arabinoxylan + H2O
xylose + ?
wheat bran + H2O
xylo-oligosaccharides + ?
wheat bran xylan + H2O
D-xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose
wheat flour xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
wheat soluble arabinoxylan + H2O
xylotriose + xylobiose
wheat straw + H2O
xylo-oligosaccharides + ?
wheat straw xylan + H2O
?
xylan + ?
xylose + ?
-
-
-
-
?
xylan + H2O
D-xylose + ?
-
from oat spelt
-
-
?
xylan + H2O
D-xylose + xylobiose + high-molecular-mass oligoxyloside
xylan + H2O
D-xylotriose + xylotetraose + ?
xylan + H2O
oligoxylosides
-
xylan from sweetgum, beech-, and birchwood, specific for xylan substrates wirth a preference for a low ratio of xylose to 4-O-methyl-D-glucuronic acid, requires 4-O-methyl-D-glucuronic acid residues for substrate recognition and/or cleavage of a beta-1,4-xylosidic bond, no clevagae of the internal xylan backbone between xylose residues
-
-
?
xylan + H2O
xylobiose + ?
xylan + H2O
xylobiose + D-xylose + ?
xylan + H2O
xylobiose + xylose + ?
xylan + H2O
xylobiose + xylotetraose + ?
xylan + H2O
xylobiose + xylotriose + ?
xylan + H2O
xylobiose + xylotriose + xylooligosaccharides
-
xylanase IA and xylanase IIIA are bothe specific for beta-1,4 xylose-rich polymer
-
-
?
xylan + H2O
xylobiose + xylotriose + xylotetraose
the hydrolysis products are mainly xylobiose (57.5% with immobilized enzyme, 36.1% with soluble enzyme) and xylotriose (38.4% with immobilized enzyme, 48.7% with soluble enzyme)
-
-
?
xylan + H2O
xylobiose + xylotriose + xylotetraose + ?
the enzyme is most active on xylans with high content of arabinose (rye arabinoxylan and wheat arabinoxylan) than on xylans with low content of arabinose (oat spelts xylan, birchwood xylan and beechwood xylan). It releases xylooligosaccharides but not xylose, indicating that XynA is an endoxylanase
-
-
?
xylan + H2O
xylobiose + xylotriose + xylotetraose + xylooligosaccharides
xylan + H2O
xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose + xyloheptaose + xylooctaose + xylononaose
xylan + H2O
xylooligosaccharides
xylan + H2O
xylooligosaccharides + ?
-
-
-
-
?
xylan + H2O
xylooligosaccharides + D-xylose + xylobiose
xylan + H2O
xylose + xylotriose + xylotetraose
xylan + H2O
xylotriose + ?
xylan + H2O
xylotriose + xylotetraose + ?
-
-
-
-
?
xylan + H2O
xylotriose + xylotetraose + larger xylooligosaccharides
-
oatspelt xylan is preferred substrate
-
-
?
xylan + H2O
xylotriose + xylotriose + ?
-
-
-
-
?
xylo-oligosaccharide + H2O
?
xylobiose + H2O
2 D-xylose
xyloglucan + H2O
?
-
low activity
-
-
?
xyloheptaose + H2O
xylobiose + xylotriose + xylotetraose
xyloheptaose + H2O
xylotriose + ?
-
-
-
-
?
xyloheptaose + H2O
xylotriose + xylotetraose + ?
xylohexaose + H2O
2 xylotriose
xylohexaose + H2O
D-xylose + ?
-
-
-
-
?
xylohexaose + H2O
xylobiose + D-xylose + ?
xylohexaose + H2O
xylobiose + xylotriose + xylotetraose
xylohexaose + H2O
xylopentaose + xylotetraose + xylotriose + xylobiose + xylose
-
hydrolysis product composition is 1.2% xylose, 29.8% xylobiose, 56.4% xylotriose, 10.9% xylotetraose and 1.7% xylopentaose
-
?
xylohexaose + H2O
xylose + ?
xylohexaose + H2O
xylose + xylobiose + xylotriose
-
-
-
?
xylohexaose + H2O
xylotriose + xylotriose
xylooctaose + H2O
xylobiose + xylotriose + xylotetraose
xylooligosaccharide + H2O
?
weak transxylosylation activity
-
-
?
xylooligosaccharide + H2O
D-xylotriose + xylotetraose
long-chain substrates, high activity
-
-
?
xylooligosaccharides + H2O
?
xylooligosaccharides + H2O
xylobiose + xylose
-
-
predominantly xylobiose
-
?
xylopentaose + H2O
5 D-xylose + ?
-
-
-
-
?
xylopentaose + H2O
xylobiose + D-xylose
-
-
-
?
xylopentaose + H2O
xylobiose + xylose
-
-
-
?
xylopentaose + H2O
xylobiose + xylotriose
xylopentaose + H2O
xylobiose + xylotriose + xylotetraose
xylopentaose + H2O
xylopentaose + xylotetraose + xylotriose + xylobiose + xylose
-
hydrolysis product composition is 1.2% xylose, 38.4% xylobiose, 49.1% xylotriose, 6.7% xylotetraose and 4.6% xylopentaose
-
?
xylopentaose + H2O
xylose + ?
xylopentaose + H2O
xylotriose + xylobiose
xylose + H2O
?
weak transxylosylation activity
-
-
?
xylotetraose + 3 H2O
4 xylose
-
-
-
?
xylotetraose + H2O
2 xylobiose
xylotetraose + H2O
D-xylose + ?
-
-
-
-
?
xylotetraose + H2O
xylobiose + xylobiose
-
-
xylotetraose is hydrolyzed mainly to two xylobioses, with only traceable amounts of xylotriose
-
?
xylotetraose + H2O
xylobiose + xylotriose
xylotetraose + H2O
xylotetraose + xylotriose + xylobiose + xylose
-
hydrolysis product composition is 1.9% xylose, 34.9% xylobiose, 49.2% xylotriose and 14.0% xylotetraose
-
?
xylotriose
xylobiose + xylotetraose
xylotriose + 2 H2O
3 xylose
-
-
-
?
xylotriose + H2O
xylobiose + ?
xylotriose + H2O
xylobiose + D-xylose
xylotriose + H2O
xylobiose + xylose
1,4-beta-D-xylan + H2O
additional information
-
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
enzyme production on ground straw as principal substrate is maximal within 7 days with 4% w/v straw
-
-
?
1,4-beta-D-xylan + H2O
?
-
enzyme production on ground straw as principal substrate is maximal within 7 days with 4% w/v straw
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
repressed by glucose, induced by oat spelt xylan, arabinoxylan, 4-O-methylglucurono-xylan, birchwood xylan and xylose
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
enzyme is secreted at high levels during growth on commercial xylan and on agricultural wastes
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
catabolite repression occurs when glucose, cellobiose, and other readily metabolizable substrates are added during growth on carboxymethylcellulose
-
-
?
1,4-beta-D-xylan + H2O
?
-
formation of the enzyme is induced by xylotriose and repressed by xylose
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
maximum enzyme production at the beginning of the exponential growth phase
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
from birchwood
-
-
?
1,4-beta-D-xylan + H2O
?
-
from birchwood
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
the enzyme is best synthesized at higher incubation temperatures 24-48 h after the maximum mycelial growth has occured
-
-
?
1,4-beta-D-xylan + H2O
?
-
the enzyme is best synthesized at higher incubation temperatures 24-48 h after the maximum mycelial growth has occured
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
inductively produced
-
-
?
1,4-beta-D-xylan + H2O
?
-
inductively produced in medium containing methyl beta-xyloside
-
-
?
1,4-beta-D-xylan + H2O
?
-
inductively produced
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
catabolite repression with glucose and other readily metabolizable substrates
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
1,4-beta-D-xylan + H2O
?
-
the enzyme induces ethylene biosynthesis
-
-
?
1,4-beta-D-xylan + H2O
?
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] + H2O
?
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] + H2O
?
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] + H2O
?
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
-
-
-
?
4-nitrophenyl arabinofuranoside + H2O
4-nitrophenol + arabinofuranose
-
Xyl2 and Xyl3 show arabinofuranosidase activity
-
-
?
4-nitrophenyl arabinofuranoside + H2O
4-nitrophenol + arabinofuranose
-
Xyl2 and Xyl3 show arabinofuranosidase activity
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
-
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside
4-nitrophenol + beta-D-xylopyranose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside
4-nitrophenol + beta-D-xylopyranose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
highest activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
highest activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
beta-xylosidase activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
only isozyme IIa shows beta-xylosidase activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
only isozyme IIa shows beta-xylosidase activity
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
no hydrolysis
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
no hydrolysis
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
no hydrolysis
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
no hydrolysis
-
-
?
4-nitrophenyl beta-D-xylotrioside + H2O
?
-
-
-
?
4-nitrophenyl beta-D-xylotrioside + H2O
?
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
Xyl2 and Xyl3 show cellulase activity
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
Xyl2 and Xyl3 show cellulase activity
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
high activity
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
high activity
-
-
?
4-nitrophenyl xylopyranoside + H2O
4-nitrophenol + xylopyranose
-
-
-
-
?
4-nitrophenyl xylopyranoside + H2O
4-nitrophenol + xylopyranose
-
Xyl2 and Xyl3 show xylosidase activity
-
-
?
4-O-methyl-beta-D-glucuronopyranosyl-1,2-(beta-1,4-xylan) + H2O
?
-
-
-
?
4-O-methyl-beta-D-glucuronopyranosyl-1,2-(beta-1,4-xylan) + H2O
?
-
-
-
?
4-O-methyl-beta-D-glucuronoxylan + H2O
?
-
-
-
-
?
4-O-methyl-beta-D-glucuronoxylan + H2O
?
soluble xylan, commercial substrate
-
-
?
4-O-methyl-D-glucurono-D-xylan + H2O
?
-
-
-
-
?
4-O-methyl-D-glucurono-D-xylan + H2O
?
-
-
-
-
?
4-O-methyl-D-glucurono-D-xylan + H2O
xylo-oligosaccharides + ?
substrate dyed with Remazol brilliant blue R
-
-
?
4-O-methyl-D-glucurono-D-xylan + H2O
xylo-oligosaccharides + ?
substrate dyed with Remazol brilliant blue R
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
-
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
-
-
-
-
?
4-O-methylglucurono-D-xylan + H2O
?
-
-
-
-
?
4-O-methylglucurono-D-xylan + H2O
?
-
-
-
-
?
4-O-methylglucurono-D-xylan + H2O
?
-
-
-
-
?
acetylhemicellulose + H2O
hemicellulose + acetate
-
high activity on sugar cane bagasse hemicellulose A and B
-
-
?
acetylhemicellulose + H2O
hemicellulose + acetate
-
high activity on sugar cane bagasse hemicellulose A and B
-
-
?
alpha-cellulose + H2O
?
high affinity, affinity is slightly greater for celluloses than for insoluble xylans and chitin
-
-
?
alpha-cellulose + H2O
?
high affinity, affinity is slightly greater for celluloses than for insoluble xylans and chitin
-
-
?
arabinan + H2O
?
-
from sugar beet, low activity
-
-
?
arabinan + H2O
?
hydrolysed at 53% compared to the hydrolysis of carboxymethylcellulose. The enzyme shows cellulase and xylanase activity
-
-
?
arabinan + H2O
?
hydrolysed at 53% compared to the hydrolysis of carboxymethylcellulose. The enzyme shows cellulase and xylanase activity
-
-
?
arabinogalactan + H2O
?
-
low activity
-
-
?
arabinogalactan + H2O
?
-
slight activity
-
-
?
arabinogalactan + H2O
?
-
-
-
-
?
arabinogalactan + H2O
?
-
-
-
-
?
arabinogalactan + H2O
?
-
-
-
-
?
arabinoxylan + H2O
?
-
from rye or wheat, low activity
-
-
?
arabinoxylan + H2O
?
-
the GHF 10 endoxylanase has a lower substrate specificity as compared to GHF 11 endoxylanases
-
-
?
arabinoxylan + H2O
?
-
-
-
-
?
arabinoxylan + H2O
?
-
39% arabinan, 62% xylan from wheat, substrate water activity (ratio of the equilibrium water vapor pressure over a material to that over pure water, roughly corresponding to the water content) range from 0.21-1.0, corresponding to 5-60% water content (dry basis)
oligosaccharides, xylobiose, xylotriose
-
?
arabinoxylan + H2O
?
-
a branched chain xylan
-
-
?
arabinoxylan + H2O
?
-
a branched chain xylan
-
-
?
arabinoxylan + H2O
?
-
-
-
-
?
arabinoxylan + H2O
?
-
-
-
?
arabinoxylan + H2O
?
-
-
-
-
?
arabinoxylan + H2O
?
-
the GHF 11 endoxylanase has a higher substrate specificity as compared to GHF 10 endoxylanases
-
-
?
arabinoxylan + H2O
?
-
-
-
-
?
arabinoxylan + H2O
?
-
from wheat or rye
-
-
?
arabinoxylan + H2O
?
-
GH 10 enzyme produces smaller oligosaccharides than GH 11. GH 10 xylanase hydrolyses arabinoxylan to give oligomers with substituted xylopyranose at the non-reducing end
-
-
?
arabinoxylan + H2O
?
-
GH 10 enzyme produces smaller oligosaccharides than GH 11. GH 11 produces oligosaccharides with unsubstituted xylopyranose at the reducing- and non-reducing ends
-
-
?
arabinoxylan + H2O
?
-
-
-
?
arabinoxylan + H2O
?
-
-
-
-
?
arabinoxylan + H2O
?
-
-
-
-
?
arabinoxylan + H2O
?
highest production of xylanase activity after approximately 3 days of incubation. Only the heavier protein band (42.8 kDa) binds to the substrate
-
-
?
arabinoxylan + H2O
?
highest production of xylanase activity after approximately 3 days of incubation. Only the heavier protein band (42.8 kDa) binds to the substrate
-
-
?
arabinoxylan + H2O
?
low to high viscosity arabinoxylans, and water-extractable wheat arabinoxylans with different ratio arabinose:xylose, overview
-
-
?
arabinoxylan + H2O
?
-
-
-
?
arabinoxylan + H2O
?
-
-
-
?
arabinoxylan + H2O
?
-
-
-
?
arabinoxylan + H2O
?
-
-
-
?
arabinoxylan + H2O
?
-
-
-
-
?
arabinoxylan + H2O
?
-
39% arabinan, 62% xylan from wheat, substrate water activity (ratio of the equilibrium water vapor pressure over a material to that over pure water, roughly corresponding to the water content) range from 0.21-1.0, corresponding to 5-60% water content (dry basis)
oligosaccharides, xylobiose, xylotriose
-
?
arabinoxylan + H2O
?
-
39% arabinan, 62% xylan from wheat, substrate water activity (ratio of the equilibrium water vapor pressure over a material to that over pure water, roughly corresponding to the water content) range from 0.21-1.0, corresponding to 5-60% water content (dry basis)
oligosaccharides, xylobiose, xylotriose
-
?
arabinoxylan + H2O
?
-
-
-
-
?
arabinoxylan + H2O
?
-
azurine-cross-linked arabinoxylan
-
-
?
arabinoxylan + H2O
xylo-oligosaccharide + ?
-
product analysis, overview
-
?
arabinoxylan + H2O
xylo-oligosaccharide + ?
higher activity with water-unextractable, than-extractable arabinoxylans, overview
product analysis, overview
-
?
arabinoxylan + H2O
xylo-oligosaccharides + ?
148% of the activity with oat spelt xylan
-
-
?
arabinoxylan + H2O
xylo-oligosaccharides + ?
148% of the activity with oat spelt xylan
-
-
?
avicel + H2O
?
-
10% activity as compared to beechwood xylan
-
-
?
avicel + H2O
?
high affinity
-
-
?
avicel + H2O
?
high affinity
-
-
?
avicel + H2O
?
-
weak reaction
-
-
?
avicel + H2O
?
-
weak reaction
-
-
?
avicel + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
azo-xylan + H2O
?
-
-
-
?
azo-xylan + H2O
?
-
-
-
?
azo-xylan + H2O
?
-
-
-
?
azurin-cross-linked arabinoxylan + H2O
?
-
-
-
?
azurin-cross-linked arabinoxylan + H2O
?
-
-
-
?
azurin-cross-linked xylan + H2O
?
-
-
-
?
azurin-cross-linked xylan + H2O
?
-
-
-
?
azurin-labelled birchwood xylan + H2O
?
-
-
-
-
?
azurin-labelled birchwood xylan + H2O
?
-
-
-
-
?
azurin-labelled birchwood xylan + H2O
?
-
-
-
-
?
bagasse + H2O
xylo-oligosaccharides + ?
Halalkalibacterium halodurans
-
-
-
?
bagasse + H2O
xylo-oligosaccharides + ?
Halalkalibacterium halodurans TSEV1
-
-
-
?
barley beta-glucan + H2O
?
minor activity
-
-
?
barley beta-glucan + H2O
?
minor activity
-
-
?
barley glucan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
barley glucan + H2O
?
-
the main end-products are monosaccharides, disaccharides, trisacchraides, and tetrasaccharides
-
?
beech wood xylan + H2O
?
-
-
-
-
?
beech wood xylan + H2O
?
-
-
-
-
?
beech wood xylan + H2O
?
-
-
-
-
?
beech wood xylan + H2O
?
-
-
-
-
?
beech wood xylan + H2O
?
-
-
-
-
?
beech wood xylan + H2O
?
-
-
-
-
?
beech wood xylan + H2O
?
strong transxylosylation activity
-
-
?
beech wood xylan + H2O
?
-
-
-
-
?
beech wood xylan + H2O
?
-
-
-
-
?
beech wood xylan + H2O
?
-
-
-
?
beech wood xylan + H2O
?
-
-
-
-
?
beechwood 4-O-methyl-D-glucuronoxylan + H2O
xylose + xylobiose + ?
-
-
-
-
?
beechwood 4-O-methyl-D-glucuronoxylan + H2O
xylose + xylobiose + ?
-
-
-
-
?
beechwood glucuronoxylan + H2O
?
-
-
products are acidic xylo-oligosaccharides having methyl glucuronic acid moiety penultimate to the reducing end of xylan
-
?
beechwood glucuronoxylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
-
best substrate, TLC analysis of CtXynGH30 hydrolysis products from beechwood xylan. CtXynGH30 shows the release of a series of higher xylooligosaccharides, overview
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
85% of the activity with oat spelt xylan
-
-
?
beechwood xylan + H2O
?
91% of the activity with xyloheptaose
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
low affinity of the enzyme towards this substrate
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
low affinity of the enzyme towards this substrate
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
136% of the activity with xyloheptaose
-
-
?
beechwood xylan + H2O
?
62.6% activity compared to rye arabinoxylan
-
-
?
beechwood xylan + H2O
?
Halalkalibacterium halodurans
-
95% activity compared to birchwood xylan
-
-
?
beechwood xylan + H2O
?
Halalkalibacterium halodurans S7
-
95% activity compared to birchwood xylan
-
-
?
beechwood xylan + H2O
?
best substrate
-
-
?
beechwood xylan + H2O
?
-
highest activity
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
161% of the activity with xyloheptaose
-
-
?
beechwood xylan + H2O
?
129% of the activity with birchwood xylan
-
-
?
beechwood xylan + H2O
?
129% of the activity with birchwood xylan
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
100% activity
-
-
?
beechwood xylan + H2O
?
hydrolysed at 84% compared to the hydrolysis of carboxymethylcellulose. The enzyme shows cellulase and xylanase activity
-
-
?
beechwood xylan + H2O
?
-
100% activity
-
-
?
beechwood xylan + H2O
?
hydrolysed at 84% compared to the hydrolysis of carboxymethylcellulose. The enzyme shows cellulase and xylanase activity
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
hydolysis is 93% in 4 h. Maximum values of xylooligosaccharides are found for beechwood at 20.6 mg/ml. Enzyme immobilized and stabilized on glyoxyl-agarose beads by multipoint covalent attachment, optimal modification consists of surface coating with a bilayer formed by a layer of derived dextran polymers and a layer of polyethylenimine
-
-
?
beechwood xylan + H2O
?
hydolysis is 93% in 4 h. Maximum values of xylooligosaccharides are found for beechwood at 20.6 mg/ml. Enzyme immobilized and stabilized on glyoxyl-agarose beads by multipoint covalent attachment, optimal modification consists of surface coating with a bilayer formed by a layer of derived dextran polymers and a layer of polyethylenimine
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
-
77% of the activtiy with oat spelt xylan
-
-
?
beechwood xylan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
beechwood xylan + H2O
?
-
77% of the activtiy with oat spelt xylan
-
-
?
beechwood xylan + H2O
?
-
2.2fold higher activity on carboxymethyl cellulose than on beechwood xylan
-
-
?
beechwood xylan + H2O
?
-
2.2fold higher activity on carboxymethyl cellulose than on beechwood xylan
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
?
beechwood xylan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
xylo-oligosaccharides
-
-
-
?
beechwood xylan + H2O
xylo-oligosaccharides
-
lower activity as compared to oat spelt xylan
-
-
?
beechwood xylan + H2O
xylo-oligosaccharides
-
lower activity as compared to oat spelt xylan
-
-
?
beechwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
beechwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
beechwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
-
?
beechwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
-
?
beechwood xylan + H2O
xylobiose + ?
best substrate
-
-
?
beechwood xylan + H2O
xylobiose + ?
best substrate
-
-
?
beechwood xylan + H2O
xylobiose + ?
-
-
products are xylobiose, an unknown oligosaccharide containing about five residues of xylose and a small amount of xylose
-
?
beechwood xylan + H2O
xylobiose + ?
-
-
products are xylobiose, an unknown oligosaccharide containing about five residues of xylose and a small amount of xylose
-
?
beechwood xylan + H2O
xylobiose + xylopentaose + ?
the endoxylanase hydrolyzes beechwood xylan to only yield xylobiose (X2) and xylopentaose
-
-
?
beechwood xylan + H2O
xylobiose + xylopentaose + ?
the endoxylanase hydrolyzes beechwood xylan to only yield xylobiose (X2) and xylopentaose
-
-
?
beechwood xylan + H2O
xylobiose + xylopentaose + ?
the endoxylanase hydrolyzes beechwood xylan to only yield xylobiose (X2) and xylopentaose
-
-
?
beechwood xylan + H2O
xylobiose + xylopentaose + ?
the endoxylanase hydrolyzes beechwood xylan to only yield xylobiose (X2) and xylopentaose
-
-
?
beechwood xylan + H2O
xylobiose + xylopentaose + ?
the endoxylanase hydrolyzes beechwood xylan to only yield xylobiose (X2) and xylopentaose
-
-
?
beechwood xylan + H2O
xylobiose + xylopentaose + ?
the endoxylanase hydrolyzes beechwood xylan to only yield xylobiose (X2) and xylopentaose
-
-
?
beechwood xylan + H2O
xylobiose + xylopentaose + ?
-
main products
-
?
beechwood xylan + H2O
xylobiose + xylopentaose + ?
-
main products
-
?
beechwood xylan + H2O
xylobiose + xylotriose
best substrate
-
-
?
beechwood xylan + H2O
xylobiose + xylotriose
-
-
-
?
beechwood xylan + H2O
xylobiose + xylotriose
-
-
-
?
beechwood xylan + H2O
xylobiose + xylotriose
-
-
-
?
beechwood xylan + H2O
xylobiose + xylotriose
-
-
-
?
beechwood xylan + H2O
xylobiose + xylotriose
-
-
-
?
beechwood xylan + H2O
xylobiose + xylotriose
-
-
-
?
beechwood xylan + H2O
xylobiose + xylotriose
-
end products are 71.2% xylobiose + 28.8% xylotriose
-
?
beechwood xylan + H2O
xylobiose + xylotriose
-
end products are 71.2% xylobiose + 28.8% xylotriose
-
?
beechwood xylan + H2O
xylohexaose + ?
-
and larger products
-
?
beechwood xylan + H2O
xylohexaose + ?
-
and larger products
-
?
beechwood xylan + H2O
xylose + ?
-
-
-
?
beechwood xylan + H2O
xylose + ?
-
-
-
?
beechwood xylan + H2O
xylose + xylo-oligosaccharides
-
-
-
?
beechwood xylan + H2O
xylose + xylo-oligosaccharides
-
-
-
?
beechwood xylan + H2O
xylose + xylobiose + ?
-
main products
-
?
beechwood xylan + H2O
xylose + xylobiose + ?
-
main products
-
?
beechwood xylan + H2O
xylose + xylotriose + xylobiose
-
best substrate
-
-
?
beechwood xylan + H2O
xylose + xylotriose + xylobiose
-
best substrate
-
-
?
beta-1,4-D-glucan + H2O
?
Thermochaetoides thermophila
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-1,4-D-glucan + H2O
?
Thermochaetoides thermophila CBS 144.50
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-1,4-D-glucan + H2O
?
Thermochaetoides thermophila DSM 1495
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-1,4-D-glucan + H2O
?
Thermochaetoides thermophila IMI 039719
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-1,4-D-xylan + H2O
?
Thermochaetoides thermophila
0.5% w/v xylan from beechwood
-
-
?
beta-1,4-D-xylan + H2O
?
Thermochaetoides thermophila
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-1,4-D-xylan + H2O
?
Thermochaetoides thermophila CBS 144.50
0.5% w/v xylan from beechwood
-
-
?
beta-1,4-D-xylan + H2O
?
Thermochaetoides thermophila CBS 144.50
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-1,4-D-xylan + H2O
?
Thermochaetoides thermophila DSM 1495
0.5% w/v xylan from beechwood
-
-
?
beta-1,4-D-xylan + H2O
?
Thermochaetoides thermophila DSM 1495
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-1,4-D-xylan + H2O
?
Thermochaetoides thermophila IMI 039719
0.5% w/v xylan from beechwood
-
-
?
beta-1,4-D-xylan + H2O
?
Thermochaetoides thermophila IMI 039719
bifunctional endoglucanase/xylanase enzyme
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
from birchwood
-
-
?
beta-1,4-xylan + H2O
?
insoluble xylan from birchwood, and soluble xylan
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
xylan from beechwood
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
from oat spelt, birchwood, or beechwood
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
from oat spelt, birchwood, or beechwood
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
oat spelt xylan, degradation into xylo-oligosaccharides of various lengths
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
from birchwood
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
from birchwood
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
from oat spelt, birchwood, or beechwood
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
from oat spelt, birchwood, or beechwood
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
from birchwood
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
from oat spelt
-
-
?
beta-1,4-xylan + H2O
?
beechwood xylan, birchwood xylan, 4-O-methyl-D-glucuronoxylan, and oat spelt xylan
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
from oalt spelt and birchwood
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
xylan from birchwood, beechwood, and oat spelt
-
-
?
beta-1,4-xylan + H2O
?
xylan from birchwood, beechwood, and oat spelt
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
water-soluble xylan
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
the enzyme cleaves the internal beta-1,4-bonds in the xylan backbone at non-modified residues, yielding different chain-length-substituted xylooligosaccharides
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
from oat spelt, birchwood, or beechwood in descending order
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
from oat spelt, birchwood, or beechwood in descending order
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
?
beta-1,4-xylan + H2O
?
-
best substrate is oat spelt xylan
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
B2CNY5
-
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
B2CNY5
from birchwood
-
-
?
beta-1,4-xylan + H2O
?
-
from oat spelt, birchwood, or beechwood
-
-
?
beta-1,4-xylan + H2O
?
B2CNY5
xylan from birchwood, beechwood, and oat spelt
-
-
?
beta-1,4-xylan + H2O
?
-
-
-
-
?
beta-1,4-xylan + H2O
?
B2CNY5
-
-
-
?
beta-1,4-xylan + H2O
?
B2CNY5
xylan from birchwood, beechwood, and oat spelt
-
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharide + ?
-
product analysis, overview
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharide + ?
from birchwood xylan and wheat bran
product analysis, overview
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharides
-
-
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharides
from birchwood
-
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharides
-
-
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharides
from birchwood
-
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharides
-
isozyme EX1 exhibits better affinity but lower hydrolytic efficiency than isozyme EX2 to xylans from beechwood, birchwood, and oat-spelt
product analysis by HPLC, overview
-
?
beta-1,4-xylan + H2O
xylo-oligosaccharides
-
isozyme EX1 exhibits better affinity but lower hydrolytic efficiency than isozyme EX2 to xylans from beechwood, birchwood, and oat-spelt
product analysis by HPLC, overview
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
-
the predominant products resulting from xylan and xylooligosaccharide hydrolysis are xylobiose and xylotriose. The enzyme can hydrolyze xylooligosaccharides larger than xylotriose
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
from birchwood
major products with equimolar ratio
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
from oat spelt or birchwood
the predominant products resulting from xylan and xylooligosaccharide hydrolysis are xylobiose and xylotriose. The enzyme can hydrolyze xylooligosaccharides larger than xylotriose
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
-
the predominant products resulting from xylan and xylooligosaccharide hydrolysis are xylobiose and xylotriose. The enzyme can hydrolyze xylooligosaccharides larger than xylotriose
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
from oat spelt or birchwood
the predominant products resulting from xylan and xylooligosaccharide hydrolysis are xylobiose and xylotriose. The enzyme can hydrolyze xylooligosaccharides larger than xylotriose
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
predominant products
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
from birchwood
predominant products
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
from birchwood or oat spelt
most predominant products. Hydrolysis products of oat spelt xylan is 2.3 mM xylobiose and 0.652 mM xylotriose, and of birchwood xylan 4.95 mM xylobiose and 1.57 mM xylotriose
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
from birchwood or oat spelt
most predominant products. Hydrolysis products of oat spelt xylan is 2.3 mM xylobiose and 0.652 mM xylotriose, and of birchwood xylan 4.95 mM xylobiose and 1.57 mM xylotriose
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
from birchwood
the main degradation products
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
from birchwood
the main degradation products
-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
-
from birchwood
the main degradation products
-
?
beta-1,4-xylan + H2O
xylooligosaccharides
-
-
-
-
?
beta-1,4-xylan + H2O
xylooligosaccharides
-
-
-
-
?
beta-1,4-xylan + H2O
xylose + ?
-
-
-
-
?
beta-1,4-xylan + H2O
xylose + ?
-
from birchwood
-
-
?
beta-1,4-xylan + H2O
xylose + ?
-
natural mutant XynBE18 can accommodate xylan and beta-1,3-1,4-glucan, but XynE2 is only accessible to xylan, the cleft of XynBE18 containing the active site is larger than that of XynE2
-
-
?
beta-1,4-xylan + H2O
xylose + ?
-
from birchwood and oat spelt
-
-
?
beta-1,4-xylan + H2O
xylotriose + xylotetraose + xylopentaose + xylopentaose + xylohexaose + xyloheptaose
-
PhX33 possesses three tryptophan and one carboxyl residues at the active site. The active site of PhX20 comprises one residue each of tryptophan, carboxyl and histidine
both the xylanases PhX33 and PhX20 produce only xylooligosaccharides with degree of polymerization 3-7 without formation of xylose and xylobiose. PhX33 hydrolyzes xylan to xylotriose, xylotetraose and xylopentaose and PhX20 gives xylotriose, xylotetraose, xylopentaose, xylohexaose, and xyloheptaose
-
?
beta-1,4-xylan + H2O
xylotriose + xylotetraose + xylopentaose + xylopentaose + xylohexaose + xyloheptaose
-
PhX33 possesses three tryptophan and one carboxyl residues at the active site. The active site of PhX20 comprises one residue each of tryptophan, carboxyl and histidine
both the xylanases PhX33 and PhX20 produce only xylooligosaccharides with degree of polymerization 3-7 without formation of xylose and xylobiose. PhX33 hydrolyzes xylan to xylotriose, xylotetraose and xylopentaose and PhX20 gives xylotriose, xylotetraose, xylopentaose, xylohexaose, and xyloheptaose
-
?
beta-glucan + H2O
?
-
barley beta-glucan
-
-
?
beta-glucan + H2O
?
-
barley beta-glucan
-
-
?
beta-glucan + H2O
?
-
barley beta-glucan
-
-
?
beta-glucan + H2O
?
-
-
-
-
?
birch wood xylan + H2O
?
-
best substrate, thin-layer chromatography determination of reaction products, the major products from oat spelt and birchwood xylan have retention factor values between those of xylose and xylopentaose
-
-
?
birch wood xylan + H2O
?
-
best substrate, thin-layer chromatography determination of reaction products, the major products from oat spelt and birchwood xylan have retention factor values between those of xylose and xylopentaose
-
-
?
birch wood xylan + H2O
?
-
-
-
-
?
birch wood xylan + H2O
?
-
-
-
-
?
birch wood xylan + H2O
?
-
-
-
?
birch wood xylan + H2O
?
-
best substrate
-
-
?
birch wood xylan + H2O
?
-
best substrate
-
-
?
birch wood xylan + H2O
?
-
best substrate
-
-
?
birch wood xylan + H2O
?
-
-
-
-
?
birch wood xylan + H2O
?
-
-
-
-
?
birch wood xylan + H2O
?
Halalkalibacterium halodurans
-
-
-
-
?
birch wood xylan + H2O
?
Halalkalibacterium halodurans TSPV1
-
-
-
-
?
birch wood xylan + H2O
?
-
-
-
?
birch wood xylan + H2O
?
-
-
-
?
birch wood xylan + H2O
?
-
-
-
?
birch wood xylan + H2O
?
-
-
-
?
birch wood xylan + H2O
?
-
-
-
?
birch wood xylan + H2O
?
-
-
-
-
?
birch wood xylan + H2O
?
-
-
-
-
?
birch wood xylan + H2O
?
-
-
-
?
birch wood xylan + H2O
?
-
-
-
-
?
birch wood xylan + H2O
?
-
-
-
-
?
birch wood xylan + H2O
?
-
-
-
?
birch wood xylan + H2O
D-xylose + ?
-
-
-
-
?
birch wood xylan + H2O
D-xylose + ?
-
-
-
-
?
birch wood xylan + H2O
D-xylose + xylobiose + ?
-
-
-
-
?
birch wood xylan + H2O
D-xylose + xylobiose + ?
-
-
-
-
?
birch wood xylan + H2O
D-xylose + xylobiose + ?
-
-
-
-
?
birch wood xylan + H2O
D-xylose + xylobiose + ?
-
-
-
-
?
birch wood xylan + H2O
D-xylose + xylobiose + ?
-
-
-
-
?
birch wood xylan + H2O
D-xylose + xylobiose + ?
-
low hydrolysis
-
-
?
birch wood xylan + H2O
D-xylose + xylobiose + ?
-
low hydrolysis
-
-
?
birch wood xylan + H2O
D-xylose + xylobiose + ?
-
low hydrolysis
-
-
?
birch wood xylan + H2O
D-xylose + xylobiose + ?
-
low hydrolysis
-
-
?
birch wood xylan + H2O
D-xylose + xylobiose + ?
-
low hydrolysis
-
-
?
birch wood xylan + H2O
xylobiose + xylotriose + xylose + ?
high activity
xylobiose is the major product with smaller amounts of xylotriose and xylose, TLC analysis
-
?
birch wood xylan + H2O
xylobiose + xylotriose + xylose + ?
high activity
xylobiose is the major product with smaller amounts of xylotriose and xylose, TLC analysis
-
?
birch wood xylan + H2O
xylose + xylobiose + ?
-
low hydrolysis
-
-
?
birch wood xylan + H2O
xylose + xylobiose + ?
-
low hydrolysis
-
-
?
birch wood xylan + H2O
xylotriose + ?
-
constitutes the majority of the hydrolyzed products from oat spelt and birchwood xylan
-
?
birch wood xylan + H2O
xylotriose + ?
-
constitutes the majority of the hydrolyzed products from oat spelt and birchwood xylan
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
high activity
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
64.6% of the activity with oat spelt xylan
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
X-I releases mainly xylotetraose and larger xylooligosaccharides, X-II liberates mainly xylotetraose, xylotriose, and xylobiose, whereas xylose is observed in smaller amounts
-
?
birchwood xylan + H2O
?
highest activity against birchwood xylan
-
-
?
birchwood xylan + H2O
?
-
-
X-I releases mainly xylotetraose and larger xylooligosaccharides, X-II liberates mainly xylotetraose, xylotriose, and xylobiose, whereas xylose is observed in smaller amounts
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
highest activity against birchwood xylan
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
32.4% activity compared to rye arabinoxylan
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
Halalkalibacterium halodurans
-
100% activity
-
-
?
birchwood xylan + H2O
?
Halalkalibacterium halodurans S7
-
100% activity
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
50% activity compared to beechwood xylan
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
73% of the activity with beechwood xylan
-
-
?
birchwood xylan + H2O
?
-
73% of the activity with beechwood xylan
-
-
?
birchwood xylan + H2O
?
high affinity, hydrolyzes birchwood xylan (hard wood) more effectively than oat spelt xylan (soft wood)
-
-
?
birchwood xylan + H2O
?
-
enzyme releases xylooligosaccharides of various length at the initial stage of xylan hydrolysis. After 2 h of incubation, the major products of hydrolysis are xylobiose, xylotriose, xylotetraose, and short-chain xylooligosaccharides
-
?
birchwood xylan + H2O
?
-
enzyme releases xylooligosaccharides of various length at the initial stage of xylan hydrolysis. After 2 h of incubation, the major products of hydrolysis are xylobiose, xylotriose, xylotetraose, and short-chain xylooligosaccharides
-
?
birchwood xylan + H2O
?
the absence of the xylan-binding domain results in a reduction of the enzymatic activity to one-second
-
-
?
birchwood xylan + H2O
?
the absence of the xylan-binding domain results in a reduction of the enzymatic activity to one-second
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
moderate activity
-
-
?
birchwood xylan + H2O
?
moderate activity
-
-
?
birchwood xylan + H2O
?
moderate activity
-
-
?
birchwood xylan + H2O
?
moderate activity
-
-
?
birchwood xylan + H2O
?
moderate activity
-
-
?
birchwood xylan + H2O
?
moderate activity
-
-
?
birchwood xylan + H2O
?
moderate activity
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
67% activity compared to beechwood xylan
-
-
?
birchwood xylan + H2O
?
hydrolysed at 73% compared to the hydrolysis of carboxymethylcellulose. The enzyme shows cellulase and xylanase activity
-
-
?
birchwood xylan + H2O
?
-
67% activity compared to beechwood xylan
-
-
?
birchwood xylan + H2O
?
hydrolysed at 73% compared to the hydrolysis of carboxymethylcellulose. The enzyme shows cellulase and xylanase activity
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
KU366607
-
-
-
?
birchwood xylan + H2O
?
-
84% of the activtiy with oat spelt xylan
-
-
?
birchwood xylan + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
birchwood xylan + H2O
?
-
84% of the activtiy with oat spelt xylan
-
-
?
birchwood xylan + H2O
?
KU366607
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
-
highest levels of both intracellular and extracellular xylanase activities in medium supplemented with xylan
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
?
LC132960
-
-
-
?
birchwood xylan + H2O
?
-
-
-
?
birchwood xylan + H2O
D-xylose + ?
Halalkalibacterium halodurans
-
-
-
-
?
birchwood xylan + H2O
D-xylose + ?
Halalkalibacterium halodurans PPKS-2
-
-
-
-
?
birchwood xylan + H2O
D-xylose + ?
-
-
-
-
?
birchwood xylan + H2O
D-xylose + ?
-
-
-
-
?
birchwood xylan + H2O
D-xylose + ?
-
-
-
-
?
birchwood xylan + H2O
D-xylose + L-arabinose + xylobiose + ?
-
-
-
?
birchwood xylan + H2O
D-xylose + L-arabinose + xylobiose + ?
-
-
-
?
birchwood xylan + H2O
D-xylose + xylobiose + ?
with soluble xylan after 12 h of incubation, about 15% (w/w) of the total reaction products is xylose, and 85% is xylobiose
-
-
?
birchwood xylan + H2O
D-xylose + xylobiose + ?
xylose and xylobiose are the predominant products
-
-
?
birchwood xylan + H2O
D-xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose
-
can be hydrolyzed by hybrid xylanase and its Aspergillus parent. Hydrolysis products by hybrid xylanase and its Aspergillus parent are D-xylose, xylobiose, xylotriose, xylotetraose and xylopentaose. Xylotriose is the main product released from birchwood xylan and wheat bran insoluble xylan by hybrid xylanase and its Aspergillus parent, respectively
-
-
?
birchwood xylan + H2O
D-xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose
-
can be hydrolyzed by hybrid xylanase and its Thermomonospora parent. Hydrolysis products by hybrid xylanase are D-xylose, xylobiose, xylotriose, xylotetraose and xylopentaose and by its Thermomonospora parent are D-xylose, xylobiose, xylotriose, xylotetraose, xylopentaose and xylohexaose. Xylotriose is the main product released from birchwood xylan and wheat bran insoluble xylan by hybrid xylanase. Xylobiose is the main product separately released from birchwood xylan and wheat bran insoluble xylan by the Thermomonospora parent
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides
-
lower activity as compared to oat spelt xylan
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides
-
lower activity as compared to oat spelt xylan
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides
-
-
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides
-
-
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
Halalkalibacterium halodurans
-
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
Halalkalibacterium halodurans TSEV1
-
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
110% of the activity with oat spelt xylan
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
110% of the activity with oat spelt xylan
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
-
initial product is D-xylose, after 10 min hydrolysis, xylo-oligosaccharides are obeserved
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
birchwood xylan + H2O
xylobiose + ?
-
-
-
?
birchwood xylan + H2O
xylobiose + ?
-
-
-
?
birchwood xylan + H2O
xylobiose + ?
-
-
-
-
?
birchwood xylan + H2O
xylobiose + ?
-
-
-
-
?
birchwood xylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
birchwood xylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
birchwood xylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
birchwood xylan + H2O
xylobiose + xylotriose + ?
temperature-dependent action mode producing xylobiose and xylotriose at 20°C, and exclusively xylobiose at 90°C
-
-
?
birchwood xylan + H2O
xylobiose + xylotriose + ?
temperature-dependent action mode producing xylobiose and xylotriose at 20°C, and exclusively xylobiose at 90°C
-
-
?
birchwood xylan + H2O
xylohexaose + ?
-
and larger products
-
?
birchwood xylan + H2O
xylohexaose + ?
-
and larger products
-
?
birchwood xylan + H2O
xylooligosaccharides
-
the endoxylanase produces only xylooligosaccharides from birchwood xylan
-
-
?
birchwood xylan + H2O
xylooligosaccharides
-
the endoxylanase produces only xylooligosaccharides from birchwood xylan
-
-
?
birchwood xylan + H2O
xylose + ?
-
-
-
?
birchwood xylan + H2O
xylose + ?
-
-
-
?
birchwood xylan + H2O
xylose + ?
-
-
-
-
?
birchwood xylan + H2O
xylose + ?
-
-
-
-
?
birchwood xylan + H2O
xylose + ?
-
-
-
-
?
birchwood xylan + H2O
xylose + xylo-oligosaccharides
-
-
-
?
birchwood xylan + H2O
xylose + xylo-oligosaccharides
-
-
-
?
birchwood xylan + H2O
xylose + xylobiose + ?
-
main products
-
?
birchwood xylan + H2O
xylose + xylobiose + ?
-
main products
-
?
carboxylmethyl cellulose + H2O
?
-
10% activity as compared to beechwood xylan
-
-
?
carboxylmethyl cellulose + H2O
?
minor activity
-
-
?
carboxylmethyl cellulose + H2O
?
minor activity
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila
bifunctional endoglucanase/xylanase enzyme
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila CBS 144.50
bifunctional endoglucanase/xylanase enzyme
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila DSM 1495
bifunctional endoglucanase/xylanase enzyme
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila IMI 039719
bifunctional endoglucanase/xylanase enzyme
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
2.2fold higher activity on carboxymethyl cellulose than on beechwood xylan
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
2.2fold higher activity on carboxymethyl cellulose than on beechwood xylan
-
-
?
carboxymethylcellulose + H2O
?
-
slight activity
-
-
?
carboxymethylcellulose + H2O
?
-
slight activity
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
no activity
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
very low activity
-
-
?
carboxymethylcellulose + H2O
?
-
very low activity
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
no activity
-
-
?
carboxymethylcellulose + H2O
?
-
low activity, 1.4% activity compared to xylan
-
-
?
carboxymethylcellulose + H2O
?
-
low activity, 1.4% activity compared to xylan
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
slight activity with xylanase I, no activity with xylanase II
-
-
?
carboxymethylcellulose + H2O
?
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellooligomers
endo-beta-1,4-glucanase activity. The enzyme shows cellulase and xylanase activity
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellooligomers
endo-beta-1,4-glucanase activity. The enzyme shows cellulase and xylanase activity
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
chitin + H2O
?
high affinity
-
-
?
chitin + H2O
?
high affinity
-
-
?
corn cobs + H2O
?
Halalkalibacterium halodurans
-
-
release of 11.8 mg reducing sugars per g of substrate
-
?
corn cobs + H2O
?
Halalkalibacterium halodurans TSPV1
-
-
release of 11.8 mg reducing sugars per g of substrate
-
?
corncob + H2O
?
-
higher titers of xylanases when powdered corncob is used as the substrate in comparison to that of birch wood xylan or oat spelt xylan
-
-
?
corncob + H2O
?
-
higher titers of xylanases when powdered corncob is used as the substrate in comparison to that of birch wood xylan or oat spelt xylan
-
-
?
corncob + H2O
xylo-oligosaccharides + ?
Halalkalibacterium halodurans
-
-
-
?
corncob + H2O
xylo-oligosaccharides + ?
Halalkalibacterium halodurans TSEV1
-
-
-
?
corncob xylan + H2O
?
-
-
-
?
corncob xylan + H2O
?
hydolysis is 100% in 1 h. Maximum values of xylooligosaccharides are found for beechwood at 30.4 mg/ml. Enzyme immobilized and stabilized on glyoxyl-agarose beads by multipoint covalent attachment, optimal modification consists of surface coating with a bilayer formed by a layer of derived dextran polymers and a layer of polyethylenimine
-
-
?
corncob xylan + H2O
?
hydolysis is 100% in 1 h. Maximum values of xylooligosaccharides are found for beechwood at 30.4 mg/ml. Enzyme immobilized and stabilized on glyoxyl-agarose beads by multipoint covalent attachment, optimal modification consists of surface coating with a bilayer formed by a layer of derived dextran polymers and a layer of polyethylenimine
-
-
?
corncob xylan + H2O
?
-
-
-
?
corncob xylan + H2O
xylo-oligosaccharides + ?
-
-
-
-
?
corncob xylan + H2O
xylo-oligosaccharides + ?
-
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + xylopentose + xylohexaose
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + xylopentose + xylohexaose
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + xylopentose + xylohexaose
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + xylopentose + xylohexaose
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + xylopentose + xylohexaose
-
-
-
?
corncob xylan + H2O
xylobiose + xylotriose + xylopentose + xylohexaose
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
galactomannan + H2O
?
-
from Konjac, low activity
-
-
?
galactomannan + H2O
?
-
from locust bean, low activity
-
-
?
gellan gum + H2O
?
-
low activity, 7.3% activity compared to xylan
-
-
?
gellan gum + H2O
?
-
low activity, 7.3% activity compared to xylan
-
-
?
glucomannan + H2O
?
-
slight activity
-
-
?
glucomannan + H2O
?
-
slight activity with xylanase I, no activity with xylanase II
-
-
?
glucose + H2O
?
weak transxylosylation activity
-
-
?
glucose + H2O
?
weak transxylosylation activity
-
-
?
glucuronoxylan + H2O
?
-
a branched chain xylan
-
-
?
glucuronoxylan + H2O
?
-
a branched chain xylan
-
-
?
glucuronoxylan + H2O
?
-
-
-
-
?
grape skin + H2O
?
-
-
-
-
?
grape skin + H2O
?
-
-
-
-
?
grass straw + H2O
?
-
-
-
-
?
grass straw + H2O
?
-
-
-
-
?
industrial pulp + H2O
?
Halalkalibacterium halodurans
-
-
release of 5.1 mg reducing sugars per g of substrate
-
?
industrial pulp + H2O
?
Halalkalibacterium halodurans TSPV1
-
-
release of 5.1 mg reducing sugars per g of substrate
-
?
insoluble birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
-
?
insoluble birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
-
?
insoluble oat spelt xylan + H2O
?
-
best substrate
-
-
?
insoluble oat spelt xylan + H2O
?
-
best substrate
-
-
?
insoluble oat spelt xylan + H2O
?
LC132960
-
-
-
?
insoluble oat spelt xylan + H2O
?
-
-
-
?
jute dust + H2O
?
-
pretreated with boiling sodium hydroxide solution for 1 h, followed by washing. Xylanase from Thermomyces lanuginosus produces a softer and mechanically stronger final product than that from Thermomyces aurantiacus when applied to low-quality jute fiber
-
-
?
jute dust + H2O
?
-
pretreated with boiling sodium hydroxide solution for 1 h, followed by washing. Xylanase from Thermomyces lanuginosus produces a softer and mechanically stronger final product than that from Thermomyces aurantiacus when applied to low-quality jute fiber
-
-
?
jute stalk + H2O
?
-
-
-
-
?
jute stalk + H2O
?
-
-
-
-
?
kraft pulp + H2O
?
-
-
-
-
?
kraft pulp + H2O
?
-
-
-
-
?
lactose + H2O
?
strong transxylosylation activity
-
-
?
lactose + H2O
?
strong transxylosylation activity
-
-
?
laminarin + H2O
?
-
weak activity
-
-
?
laminarin + H2O
?
-
no activity
-
-
?
laminarin + H2O
?
-
no activity
-
-
?
laminarin + H2O
?
-
no activity
-
-
?
laminarin + H2O
?
-
no activity
-
-
?
laminarin + H2O
?
-
low activity, 3.4% activity compared to xylan
-
-
?
laminarin + H2O
?
-
low activity, 3.4% activity compared to xylan
-
-
?
laminarin + H2O
?
-
xylanase I
-
-
?
larchwood xylan + H2O
xylobiose + xylotriose + ?
-
-
-
-
?
larchwood xylan + H2O
xylobiose + xylotriose + ?
-
-
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
low activity
-
-
?
lichenan + H2O
?
-
low activity
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
no activity
-
-
?
lichenan + H2O
?
-
no activity
-
-
?
lichenan + H2O
?
-
no activity
-
-
?
lichenan + H2O
?
-
no activity
-
-
?
lichenan + H2O
?
-
low activity, 19% activity compared to xylan
-
-
?
lichenan + H2O
?
-
low activity, 19% activity compared to xylan
-
-
?
low-viscosity wheat arabinoxylan + H2O
?
-
-
-
-
?
low-viscosity wheat arabinoxylan + H2O
?
-
-
-
?
maize cob + H2O
?
-
-
-
-
?
maize cob + H2O
?
-
-
-
-
?
maltose + H2O
?
strong transxylosylation activity
-
-
?
maltose + H2O
?
strong transxylosylation activity
-
-
?
medium viscosity wheat arabinoxylan + H2O
?
-
-
-
-
?
medium viscosity wheat arabinoxylan + H2O
?
-
-
-
?
O-acetyl-4-O-methyl-D-glucuronoxylan + H2O
xylose + xylobiose + ?
-
-
-
-
?
O-acetyl-4-O-methyl-D-glucuronoxylan + H2O
xylose + xylobiose + ?
-
-
-
-
?
oat spelt + H2O
?
-
-
-
-
?
oat spelt + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
thin-layer chromatography determination of reaction products, the major products from oat spelt and birchwood xylan have retention factor values between those of xylose and xylopentaose
-
-
?
oat spelt xylan + H2O
?
-
thin-layer chromatography determination of reaction products, the major products from oat spelt and birchwood xylan have retention factor values between those of xylose and xylopentaose
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
xylanase production only reaches 5.7 and 11.7 U/ml when using pure xylan (oat spelt xylan) as the carbon source at 0.5% and 1% level, respectively
-
-
?
oat spelt xylan + H2O
?
-
xylanase production only reaches 5.7 and 11.7 U/ml when using pure xylan (oat spelt xylan) as the carbon source at 0.5% and 1% level, respectively
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
61.9% activity compared to rye arabinoxylan
-
-
?
oat spelt xylan + H2O
?
Halalkalibacterium halodurans
-
85% activity compared to birchwood xylan
-
-
?
oat spelt xylan + H2O
?
Halalkalibacterium halodurans S7
-
85% activity compared to birchwood xylan
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
50% activity compared to beechwood xylan
-
-
?
oat spelt xylan + H2O
?
-
22.3% activity as compared to beechwood xylan
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
87% of the activity with beechwood xylan
-
-
?
oat spelt xylan + H2O
?
-
87% of the activity with beechwood xylan
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
high affinity
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
53% of the activity with birchwood xylan
-
-
?
oat spelt xylan + H2O
?
53% of the activity with birchwood xylan
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
low activity
-
-
?
oat spelt xylan + H2O
?
low activity
-
-
?
oat spelt xylan + H2O
?
low activity
-
-
?
oat spelt xylan + H2O
?
low activity
-
-
?
oat spelt xylan + H2O
?
low activity
-
-
?
oat spelt xylan + H2O
?
low activity
-
-
?
oat spelt xylan + H2O
?
low activity
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
hydrolysed at 76% compared to the hydrolysis of carboxymethylcellulose. The enzyme shows cellulase and xylanase activity
-
-
?
oat spelt xylan + H2O
?
hydrolysed at 76% compared to the hydrolysis of carboxymethylcellulose. The enzyme shows cellulase and xylanase activity
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
?
-
-
-
-
?
oat spelt xylan + H2O
D-xylose + ?
-
-
-
-
?
oat spelt xylan + H2O
D-xylose + ?
Halalkalibacterium halodurans
-
-
-
-
?
oat spelt xylan + H2O
D-xylose + ?
Halalkalibacterium halodurans PPKS-2
-
-
-
-
?
oat spelt xylan + H2O
D-xylose + xylobiose + ?
with soluble xylan after 12 h of incubation, about 15% (w/w) of the total reaction products is xylose, and 85% is xylobiose. Comparing with the soluble xylan, the activities of XynAS27, XynAS27cd, and XynAS27cdl on insoluble xylan are lower, about 56%, 23% and 24% of the activities on soluble substrate, respectively
-
-
?
oat spelt xylan + H2O
D-xylose + xylobiose + ?
xylose and xylobiose are the predominant products
-
-
?
oat spelt xylan + H2O
D-xylose + xylobiose + ?
Thermochaetoides thermophila
-
-
-
?
oat spelt xylan + H2O
D-xylose + xylobiose + ?
Thermochaetoides thermophila NIBGE 1
-
-
-
?
oat spelt xylan + H2O
xylo-oligosaccharides
-
-
-
-
?
oat spelt xylan + H2O
xylo-oligosaccharides
-
-
-
-
?
oat spelt xylan + H2O
xylo-oligosaccharides
-
-
-
-
?
oat spelt xylan + H2O
xylo-oligosaccharides
-
-
-
-
?
oat spelt xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
oat spelt xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
oat spelt xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
oat spelt xylan + H2O
xylo-oligosaccharides + ?
-
-
-
?
oat spelt xylan + H2O
xylobiose + ?
-
-
-
?
oat spelt xylan + H2O
xylobiose + ?
-
-
-
?
oat spelt xylan + H2O
xylobiose + xylotriose + ?
-
-
-
?
oat spelt xylan + H2O
xylobiose + xylotriose + ?
-
PoXyn3 initially releases larger xylooligosaccharides from oat spelt xylan. These oligosaccharides are principally hydrolyzed to xylobiose and xylotriose
-
-
?
oat spelt xylan + H2O
xylobiose + xylotriose + ?
-
PoXyn3 initially releases larger xylooligosaccharides from oat spelt xylan. These oligosaccharides are principally hydrolyzed to xylobiose and xylotriose
-
-
?
oat spelt xylan + H2O
xylobiose + xylotriose + ?
52% of the activity with birchwood xylan
major products
-
?
oat spelt xylan + H2O
xylose + ?
-
no release of xylo-oligosaccharides detected
-
?
oat spelt xylan + H2O
xylose + ?
-
no release of xylo-oligosaccharides detected
-
?
oat spelt xylan + H2O
xylotriose + ?
-
constitutes the majority of the hydrolyzed products from oat spelt and birchwood xylan
-
?
oat spelt xylan + H2O
xylotriose + ?
-
constitutes the majority of the hydrolyzed products from oat spelt and birchwood xylan
-
?
oat spelts xylan + H2O
D-xylose + ?
-
-
-
?
oat spelts xylan + H2O
D-xylose + ?
-
-
-
?
oat speltxylan + H2O
xylose + xylo-oligosaccharides
-
-
-
?
oat speltxylan + H2O
xylose + xylo-oligosaccharides
-
-
-
?
oat xylan + H2O
?
-
-
-
-
?
oat xylan + H2O
?
-
-
-
-
?
oat xylan + H2O
?
-
-
-
?
oat xylan + H2O
?
-
-
-
?
oat-spelt xylan + H2O
?
-
-
-
?
oat-spelt xylan + H2O
?
-
-
-
?
oatspelt xylan + H2O
xylobiose + ?
-
-
-
-
?
oatspelt xylan + H2O
xylobiose + ?
-
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
?
-
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
?
-
weak substrate for isoforms xynA, xynC, no substrate for xynB
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
?
-
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
-
-
weak reaction
-
?
p-nitrophenyl beta-D-xylopyranoside
?
-
transferase activity on
-
-
?
p-nitrophenyl beta-D-xylopyranoside
?
-
-
-
-
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
-
weak reaction
-
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
-
weak reaction
-
?
p-nitrophenyl-beta-D-xylobioside + H2O
?
-
-
-
-
?
p-nitrophenyl-beta-D-xylobioside + H2O
?
-
-
-
-
?
pachyman + H2O
?
-
no activity
-
-
?
pachyman + H2O
?
-
slight activity with xylanase I, no activity with xylanase II
-
-
?
remazol brilliant blue xylan + H2O
?
-
-
-
?
remazol brilliant blue xylan + H2O
?
-
-
-
?
Remazol brilliant blue-birchwood xylan + H2O
?
-
-
-
?
Remazol brilliant blue-birchwood xylan + H2O
?
-
-
-
?
Remazol brilliant blue-carboxymethylcellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose + high-molecular-mass oligosaccharides
-
cellulose activity
-
?
Remazol brilliant blue-carboxymethylcellulose + H2O
D-glucose + cellobiose + cellotriose + cellotetraose + high-molecular-mass oligosaccharides
-
cellulose activity
-
?
rhodymenan + H2O
xylose + xylobiose + ?
-
-
-
-
?
rhodymenan + H2O
xylose + xylobiose + ?
-
-
-
-
?
rice straw + H2O
?
-
-
-
-
?
rice straw + H2O
?
-
-
-
-
?
rye arabinoxylan + H2O
?
-
-
-
?
rye arabinoxylan + H2O
?
-
-
-
?
rye arabinoxylan + H2O
?
best substrate
-
-
?
rye arabinoxylan + H2O
?
soluble and insoluble, the latter is less active, moderate to lower activity
-
-
?
rye bran + H2O
?
maximum production of xylanase occurs after 144 h of incubation. When waterwashed rye bran is used as substrate, maximum production is reached after 216 h
-
-
?
rye bran + H2O
?
maximum production of xylanase occurs after 144 h of incubation. When waterwashed rye bran is used as substrate, maximum production is reached after 216 h
-
-
?
rye bran + H2O
?
-
low activity with Streptomyces lividans carrying empty vector pN702GEM3
-
-
?
rye bran + H2O
?
-
low activity with Streptomyces lividans carrying empty vector pN702GEM3
-
-
?
soluble birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
-
?
soluble birchwood xylan + H2O
xylo-oligosaccharides + ?
-
-
-
-
?
soluble oat spelt xylan + H2O
?
-
best substrate
-
-
?
soluble oat spelt xylan + H2O
?
-
best substrate
-
-
?
soluble oat spelt xylan + H2O
?
LC132960
-
-
-
?
soluble oat spelt xylan + H2O
?
-
-
-
?
soluble wheat arabinoxylan + H2O
?
best substrate of XYN10G5, Under simulated gastric conditions, XYN10G5 is stable and releases more reducing sugars from soluble wheat arabinoxylan
-
-
?
soluble wheat arabinoxylan + H2O
?
-
-
-
?
soybean fiber + H2O
?
-
-
-
-
?
soybean fiber + H2O
?
-
-
-
-
?
soybean hull + H2O
?
-
-
-
-
?
soybean hull + H2O
?
-
-
-
-
?
starch + H2O
?
-
no activity
-
-
?
starch + H2O
?
-
no activity
-
-
?
starch + H2O
?
strong transxylosylation activity
-
-
?
starch + H2O
?
-
no activity
-
-
?
starch + H2O
?
some affinity for polysaccharides that do not contain beta-1,4 linkages, e.g., starches from potato and wheat
-
-
?
starch + H2O
?
some affinity for polysaccharides that do not contain beta-1,4 linkages, e.g., starches from potato and wheat
-
-
?
starch + H2O
?
-
no activity
-
-
?
starch + H2O
?
-
soluble starch
-
-
?
sucrose + H2O
D-fructose + D-glucose
strong transxylosylation activity
-
-
?
sucrose + H2O
D-fructose + D-glucose
strong transxylosylation activity
-
-
?
sugar cane bagasse + H2O
?
-
-
-
-
?
sugar cane bagasse + H2O
?
-
-
-
-
?
sugar cane bagasse + H2O
?
-
-
-
-
?
wheat arabinoxylan + H2O
?
84% of the activity with xyloheptaose
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
-
?
wheat arabinoxylan + H2O
?
48% of the activity with xyloheptaose
-
-
?
wheat arabinoxylan + H2O
?
92.0% activity compared to rye arabinoxylan
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
117% of the activity with xyloheptaose
-
-
?
wheat arabinoxylan + H2O
?
115% of the activity with birchwood xylan
-
-
?
wheat arabinoxylan + H2O
?
115% of the activity with birchwood xylan
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
-
?
wheat arabinoxylan + H2O
?
soluble and insoluble, the latter is less active, moderate to lower activity
-
-
?
wheat arabinoxylan + H2O
?
soluble and insoluble, the latter is less active, moderate to lower activity
-
-
?
wheat arabinoxylan + H2O
?
soluble and insoluble, the latter is less active, moderate to lower activity
-
-
?
wheat arabinoxylan + H2O
?
soluble and insoluble, the latter is less active, moderate to lower activity
-
-
?
wheat arabinoxylan + H2O
?
soluble and insoluble, the latter is less active, moderate to lower activity
-
-
?
wheat arabinoxylan + H2O
?
soluble and insoluble, the latter is less active, moderate to lower activity
-
-
?
wheat arabinoxylan + H2O
?
soluble and insoluble, the latter is less active, moderate to lower activity
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
35% of the activity with birchwood xylan
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
-
-
-
?
wheat arabinoxylan + H2O
?
-
incomplete utilization of wheat arabinoxylan, which leads to the accumulation of a complex mixture of branched oligosaccharides accounting more than 90% of the starting polysaccharide
-
-
?
wheat arabinoxylan + H2O
xylose + ?
-
-
-
-
?
wheat arabinoxylan + H2O
xylose + ?
-
-
-
-
?
wheat bran + H2O
?
-
xylanase production is highest (19.1 U/ml) when 1% wheat bran is added as the carbon source
-
-
?
wheat bran + H2O
?
-
xylanase production is highest (19.1 U/ml) when 1% wheat bran is added as the carbon source
-
-
?
wheat bran + H2O
?
Halalkalibacterium halodurans
-
-
release of 25.5 mg reducing sugars per g of substrate
-
?
wheat bran + H2O
?
Halalkalibacterium halodurans TSPV1
-
-
release of 25.5 mg reducing sugars per g of substrate
-
?
wheat bran + H2O
?
-
-
-
-
?
wheat bran + H2O
?
-
-
-
-
?
wheat bran + H2O
?
-
-
-
-
?
wheat bran + H2O
?
when waterwashed wheat bran is used as substrate, maximum production is reached after 216 h
-
-
?
wheat bran + H2O
?
when waterwashed wheat bran is used as substrate, maximum production is reached after 216 h
-
-
?
wheat bran + H2O
?
-
low activity with strain Streptomyces lividans carrying empty vector pN702GEM3
-
-
?
wheat bran + H2O
?
-
low activity with strain Streptomyces lividans carrying empty vector pN702GEM3
-
-
?
wheat bran + H2O
?
-
-
-
-
?
wheat bran + H2O
xylo-oligosaccharides + ?
Halalkalibacterium halodurans
-
-
-
?
wheat bran + H2O
xylo-oligosaccharides + ?
Halalkalibacterium halodurans TSEV1
-
-
-
?
wheat bran xylan + H2O
D-xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose
-
can be hydrolyzed by hybrid xylanase and its Aspergillus parent. Hydrolysis products by hybrid xylanase and its Aspergillus parent are D-xylose, xylobiose, xylotriose, xylotetraose, xylopentaose and xylohexaose. Xylotriose is the main product released from birchwood xylan and wheat bran insoluble xylan by hybrid xylanase and its Aspergillus parent, respectively
-
-
?
wheat bran xylan + H2O
D-xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose
-
can be hydrolyzed by hybrid xylanase and its Thermomonospora parent. Hydrolysis products by hybrid xylanase and its Thermomonospora parent are D-xylose, xylobiose, xylotriose, xylotetraose, xylopentaose and xylohexaose. Xylotriose is the main product released from birchwood xylan and wheat bran insoluble xylan by hybrid xylanase. Xylobiose is the main product separately released from birchwood xylan and wheat bran insoluble xylan by the Thermomonospora parent
-
-
?
wheat soluble arabinoxylan + H2O
xylotriose + xylobiose
-
-
predominant production of xylotriose and xylobiose as end products
-
?
wheat soluble arabinoxylan + H2O
xylotriose + xylobiose
-
predominant production of xylotriose and xylobiose as end products
-
?
wheat straw + H2O
?
Halalkalibacterium halodurans
-
-
release of 5.3 mg reducing sugars per g of substrate
-
?
wheat straw + H2O
?
Halalkalibacterium halodurans TSPV1
-
-
release of 5.3 mg reducing sugars per g of substrate
-
?
wheat straw + H2O
?
-
-
-
-
?
wheat straw + H2O
?
hydolysis is 44% in 5 h. Maximum values of xylooligosaccharides are found for beechwood at 12.5 mg/ml. Enzyme immobilized and stabilized on glyoxyl-agarose beads by multipoint covalent attachment, optimal modification consists of surface coating with a bilayer formed by a layer of derived dextran polymers and a layer of polyethylenimine
-
-
?
wheat straw + H2O
?
hydolysis is 44% in 5 h. Maximum values of xylooligosaccharides are found for beechwood at 12.5 mg/ml. Enzyme immobilized and stabilized on glyoxyl-agarose beads by multipoint covalent attachment, optimal modification consists of surface coating with a bilayer formed by a layer of derived dextran polymers and a layer of polyethylenimine
-
-
?
wheat straw + H2O
xylo-oligosaccharides + ?
Halalkalibacterium halodurans
-
-
-
?
wheat straw + H2O
xylo-oligosaccharides + ?
Halalkalibacterium halodurans TSEV1
-
-
-
?
wheat straw xylan + H2O
?
-
-
-
?
wheat straw xylan + H2O
?
-
-
-
?
xylan + H2O
?
-
preferred substrate, soluble and insoluble substrate from oat spelt or birchwood
-
-
?
xylan + H2O
?
-
specific for xylan, soluble and insoluble xylan from birchwood
-
-
?
xylan + H2O
?
-
specific for xylan, soluble and insoluble xylan from birchwood
-
-
?
xylan + H2O
?
-
preferred substrate, soluble and insoluble substrate from oat spelt or birchwood
-
-
?
xylan + H2O
?
-
birchwood xylan preferred
-
-
?
xylan + H2O
?
birchwood xylan
-
-
?
xylan + H2O
?
-
from oat spelt
-
-
?
xylan + H2O
?
-
xylan from oatspelt
-
-
?
xylan + H2O
?
-
beechwood xylan
-
-
?
xylan + H2O
?
-
birchwood xylan is preferred
-
-
?
xylan + H2O
?
from birchwood, beechwood, oatspelt, wheat, or rye
-
-
?
xylan + H2O
?
from birchwood, beechwood, oatspelt, wheat, or rye
-
-
?
xylan + H2O
?
part of hemicelluloses in cell walls
-
-
?
xylan + H2O
?
-
from birchwood
-
-
?
xylan + H2O
?
-
from birchwood
-
-
?
xylan + H2O
?
-
from oatspelt
-
-
?
xylan + H2O
?
-
enzyme might be responsible for rendering substrates for other depolymerizing enzymes instead of producing oligoxylosides for cellular metabolism
-
-
?
xylan + H2O
?
-
activity towards xylans from beech, birch, larch, and arabinoxylans from wheat is higher for xylanase 2 compared to xylanase 1
-
-
?
xylan + H2O
?
-
from birchwood
-
-
?
xylan + H2O
?
-
xylan from birch wood
-
-
?
xylan + H2O
?
from birchwood
-
-
?
xylan + H2O
?
from birchwood
-
-
?
xylan + H2O
?
-
from birchwood, beechwood or oatspelt. Oatspelt xylan is slightly preferred
-
-
?
xylan + H2O
?
-
from larchwood, both isozymes are endo-acting
-
-
?
xylan + H2O
?
-
from larchwood, both isozymes are endo-acting
-
-
?
xylan + H2O
?
molecular weight of 20000-30000, high activity
-
-
?
xylan + H2O
?
molecular weight of 20000-30000, high activity
-
-
?
xylan + H2O
?
molecular weight of 20000-30000, high activity
-
-
?
xylan + H2O
?
molecular weight of 20000-30000, high activity
-
-
?
xylan + H2O
?
molecular weight of 20000-30000, high activity
-
-
?
xylan + H2O
?
molecular weight of 20000-30000, high activity
-
-
?
xylan + H2O
?
molecular weight of 20000-30000, high activity
-
-
?
xylan + H2O
?
-
birchwood and beechwood xylans
-
-
?
xylan + H2O
?
-
birchwood and beechwood xylans
-
-
?
xylan + H2O
?
-
hydrolysis of beta-1,4-linked xylose in the xylan backbone
-
-
?
xylan + H2O
?
-
delignification of hardwood and softwood, the enzymes are differing in their bleaching potential, Xyl1 is more effective tahn Xyl2 and Xyl3
-
-
?
xylan + H2O
?
-
from birchwood or oat spelt
-
-
?
xylan + H2O
?
-
from oat spelt or birchwood, no release of arabinose
-
-
?
xylan + H2O
?
-
from oat spelt or birchwood, no release of arabinose
-
-
?
xylan + H2O
?
-
delignification of hardwood and softwood, the enzymes are differing in their bleaching potential, Xyl1 is more effective tahn Xyl2 and Xyl3
-
-
?
xylan + H2O
?
-
from birchwood or oat spelt
-
-
?
xylan + H2O
?
low viscosity xylan
-
-
?
xylan + H2O
?
Thermomonospora sp.
-
from oat spelt
-
-
?
xylan + H2O
?
-
commercial substrate and from oat spelts and larch sawdust, the latter being the best substrate for wild-type and mutant enzyme
-
-
?
xylan + H2O
?
-
beechwood xylan
-
-
?
xylan + H2O
?
-
beechwood xylan
-
-
?
xylan + H2O
?
-
beechwood xylan
-
-
?
xylan + H2O
?
-
beechwood xylan
-
-
?
xylan + H2O
?
RBB-xylan as substrate
-
-
?
xylan + H2O
?
RBB-xylan as substrate
-
-
?
xylan + H2O
?
-
beechwood xylan
-
-
?
xylan + H2O
?
RBB-xylan as substrate
-
-
?
xylan + H2O
?
RBB-xylan as substrate
-
-
?
xylan + H2O
?
-
hydrolysis of beta-1,4-glycosidic bonds
-
-
?
xylan + H2O
?
-
from birchwood or oatspelt
-
-
?
xylan + H2O
?
-
hydrolysis of beta-1,4-glycosidic bonds
-
-
?
xylan + H2O
?
from birchwood
-
-
?
xylan + H2O
?
-
beechwood xylan
-
-
?
xylan + H2O
?
-
the main end-products are monosaccharides, disaccharides, trisacchraides, and tetrasaccharides, mainly xylose, xylobiose, and xylotetrose
-
?
xylan + H2O
D-xylose + xylobiose + high-molecular-mass oligoxyloside
xylan from birchwood
xylanase activity
-
?
xylan + H2O
D-xylose + xylobiose + high-molecular-mass oligoxyloside
xylan from birchwood
xylanase activity
-
?
xylan + H2O
D-xylotriose + xylotetraose + ?
major constituent of plant hemicellulose forming the cell walls of hards woods, 15-30%, and softwoods, 7-10%
-
-
?
xylan + H2O
D-xylotriose + xylotetraose + ?
from oat spelt and other sources, xylan substrate specificity overview, inverse stereoselectivity, enzyme possesses a large substrate binding cleft with at least 6 xylose-binding sites
-
-
?
xylan + H2O
xylobiose + ?
-
oatpselt xylan is preferred over birchwood xylan
no formation of free xylose
-
?
xylan + H2O
xylobiose + ?
-
diverse xylan substrates, best substrate is wheat arabinoxylan, overview
no formation of xylose
-
?
xylan + H2O
xylobiose + ?
-
diverse xylan substrates, best substrate is wheat arabinoxylan, overview
no formation of xylose
-
?
xylan + H2O
xylobiose + ?
-
-
-
-
?
xylan + H2O
xylobiose + D-xylose + ?
substrate birchwood xylan
after 24 h of hydrolysis, more than 90% of the total hydrolysis products of xylan are xylobiose and D-xylose with almost no xylotetraose, -pentaose, or -hexaose
-
?
xylan + H2O
xylobiose + D-xylose + ?
substrate birchwood xylan
after 24 h of hydrolysis, more than 90% of the total hydrolysis products of xylan are xylobiose and D-xylose with almost no xylotetraose, -pentaose, or -hexaose
-
?
xylan + H2O
xylobiose + xylose + ?
-
-
highly specific substrate
-
?
xylan + H2O
xylobiose + xylose + ?
-
birchwood and soluble oat spelt xylan, endo-acting
main degradation products
-
?
xylan + H2O
xylobiose + xylotetraose + ?
-
xylan substrate from oat spelt
no formation of xylose
-
?
xylan + H2O
xylobiose + xylotetraose + ?
-
xylan substrate from oat spelt
no formation of xylose
-
?
xylan + H2O
xylobiose + xylotriose + ?
-
xylan substrate from birchwood
no formation of xylose
-
?
xylan + H2O
xylobiose + xylotriose + ?
-
xylan substrate from birchwood
no formation of xylose
-
?
xylan + H2O
xylobiose + xylotriose + ?
Halalkalibacterium halodurans
-
xylan from birchwood, oat spelt, and larchwood
main products
-
?
xylan + H2O
xylobiose + xylotriose + ?
Halalkalibacterium halodurans C-1
-
xylan from birchwood, oat spelt, and larchwood
main products
-
?
xylan + H2O
xylobiose + xylotriose + ?
-
lenzing xylan
and small amounts of xylotetraose and xylopentaose
-
?
xylan + H2O
xylobiose + xylotriose + ?
Thermochaetoides thermophila
-
-
xylanase I produces mainly xylobiose and xylotriose. Xylanase II produces mainly xylobiose
-
?
xylan + H2O
xylobiose + xylotriose + xylotetraose + xylooligosaccharides
-
from oat spelt
-
-
?
xylan + H2O
xylobiose + xylotriose + xylotetraose + xylooligosaccharides
-
from oat spelt
-
-
?
xylan + H2O
xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose + xyloheptaose + xylooctaose + xylononaose
-
oat spelt xylan and birchwood xylan
-
-
?
xylan + H2O
xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose + xyloheptaose + xylooctaose + xylononaose
-
oat spelt xylan and birchwood xylan
-
-
?
xylan + H2O
xylooligosaccharides
-
substrate from brichwood, beechwood, or oat spelt soluble fraction, the latter being the best substrate, endoxylanase activity
-
-
?
xylan + H2O
xylooligosaccharides
-
-
-
?
xylan + H2O
xylooligosaccharides
from oat spelt or birchwood
recombinant N-terminal + catalytic domains produce mainl xylobiose, xylotriose and xylotetraose, while the single recombinant catalytic domain produces mainly xylotriose and xylotetraose, no further hydrolysis of the oligomeric products
-
?
xylan + H2O
xylooligosaccharides + D-xylose + xylobiose
-
substrate specificity of isozymes with different xylans: isozymes Ia, Ib, and Ic prefer larchwood arabinoglucurono xylan, isozymes IIa and IIc prefer birchwood glucurono xylan, isozyme IIb and IId prefer beechwood glucuronoxylan, another substrate is xylan from oat spelt, solka floc xylan is utilized only by isozyme Ic
isozyme Ia produces only xylooligosaccharides
-
?
xylan + H2O
xylooligosaccharides + D-xylose + xylobiose
-
substrate specificity of isozymes with different xylans: isozymes Ia, Ib, and Ic prefer larchwood arabinoglucurono xylan, isozymes IIa and IIc prefer birchwood glucurono xylan, isozyme IIb and IId prefer beechwood glucuronoxylan, another substrate is xylan from oat spelt, solka floc xylan is utilized only by isozyme Ic
isozyme Ia produces only xylooligosaccharides
-
?
xylan + H2O
xylose + ?
-
-
-
-
?
xylan + H2O
xylose + ?
-
-
-
-
?
xylan + H2O
xylose + ?
-
-
-
-
?
xylan + H2O
xylose + xylotriose + xylotetraose
-
-
-
-
?
xylan + H2O
xylose + xylotriose + xylotetraose
-
-
-
-
?
xylan + H2O
xylotriose + ?
-
after 25 h of reaction only xylotriose is left in the supernatant. No xylobiose or xylose are detected
-
?
xylan + H2O
xylotriose + ?
-
after 25 h of reaction only xylotriose is left in the supernatant. No xylobiose or xylose are detected
-
?
xylo-oligosaccharide + H2O
?
-
substrates from corn cobs
-
-
?
xylo-oligosaccharide + H2O
?
-
substrates from corn cobs
-
-
?
xylobiose + H2O
2 D-xylose
-
-
-
?
xylobiose + H2O
2 D-xylose
-
-
-
?
xylobiose + H2O
2 D-xylose
-
-
-
-
?
xylobiose + H2O
2 D-xylose
-
-
-
-
?
xylobiose + H2O
2 D-xylose
low activity
-
-
?
xylobiose + H2O
2 D-xylose
low activity
-
-
?
xylobiose + H2O
2 D-xylose
-
can be hydrolyzed by the Thermomonospora parent, no activity with hybrid xylanase
-
-
?
xylobiose + H2O
?
-
can be hydrolyzed by the Aspergillus parent, no activity with hybrid xylanase
-
-
?
xylobiose + H2O
?
-
-
-
-
?
xylobiose + H2O
?
-
no hydrolysis
-
-
?
xylobiose + H2O
?
-
no hydrolysis
-
-
?
xylobiose + H2O
?
-
no hydrolysis
-
-
?
xylobiose + H2O
?
-
no hydrolysis
-
-
?
xylobiose + H2O
?
-
no hydrolysis
-
-
?
xylobiose + H2O
?
-
no hydrolysis
-
-
?
xylobiose + H2O
?
-
no hydrolysis
-
-
?
xylobiose + H2O
?
-
low activity, xylanase A
-
-
?
xylobiose + H2O
?
-
low activity, xylanase A
-
-
?
xylobiose + H2O
?
-
no hydrolysis
-
-
?
xyloheptaose + H2O
?
-
-
-
?
xyloheptaose + H2O
?
-
-
-
?
xyloheptaose + H2O
?
-
-
-
-
?
xyloheptaose + H2O
?
-
-
-
?
xyloheptaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
-
?
xyloheptaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
-
?
xyloheptaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
-
?
xyloheptaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
?
xyloheptaose + H2O
xylotriose + xylotetraose + ?
-
-
-
-
?
xyloheptaose + H2O
xylotriose + xylotetraose + ?
-
-
-
-
?
xylohexaose + H2O
2 xylotriose
-
can be hydrolyzed by the Aspergillus parent and hybrid xylanase
-
-
?
xylohexaose + H2O
2 xylotriose
rapid cleavage
xylohexaose was cleaved to produce mainly xylotriose and to a lesser extent xylobiose and xylotetraose
-
?
xylohexaose + H2O
2 xylotriose
-
-
-
-
?
xylohexaose + H2O
2 xylotriose
-
rapid cleavage
xylohexaose is cleaved initially to produce mainly xylotriose and a small amount of xylobiose and xylotetraose
-
?
xylohexaose + H2O
2 xylotriose
rapid cleavage
xylohexaose is cleaved initially to produce mainly xylotriose and a small amount of xylobiose and xylotetraose
-
?
xylohexaose + H2O
2 xylotriose
-
can be hydrolyzed by the Thermomonospora parent and hybrid xylanase
-
-
?
xylohexaose + H2O
?
-
-
-
?
xylohexaose + H2O
?
-
-
-
?
xylohexaose + H2O
?
81% of the activity with xyloheptaose
-
-
?
xylohexaose + H2O
?
-
-
-
-
?
xylohexaose + H2O
?
-
-
-
-
?
xylohexaose + H2O
?
99% of the activity with xyloheptaose
-
-
?
xylohexaose + H2O
?
-
-
-
-
?
xylohexaose + H2O
?
-
-
-
?
xylohexaose + H2O
?
98% of the activity with xyloheptaose
-
-
?
xylohexaose + H2O
?
-
-
-
-
?
xylohexaose + H2O
?
-
-
-
-
?
xylohexaose + H2O
?
-
-
-
-
?
xylohexaose + H2O
xylobiose + D-xylose + ?
-
-
-
?
xylohexaose + H2O
xylobiose + D-xylose + ?
-
-
-
?
xylohexaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
-
?
xylohexaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
-
?
xylohexaose + H2O
xylose + ?
-
-
-
?
xylohexaose + H2O
xylose + ?
-
-
-
?
xylohexaose + H2O
xylotriose + xylotriose
-
-
-
-
?
xylohexaose + H2O
xylotriose + xylotriose
-
-
-
-
?
xylohexaose + H2O
xylotriose + xylotriose
-
most preferred substrate of TRX II
xylohexaose is hydrolyzed mainly to two xylotrioses, but considerable amounts of xylotetraose and xylobiose are also detected while only traceable amounts of xylopentaose are detected
-
?
xylooctaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
-
?
xylooctaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
-
?
xylooctaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
?
xylooctaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
-
?
xylooligosaccharides + H2O
?
-
-
-
?
xylooligosaccharides + H2O
?
-
-
-
-
?
xylopentaose + H2O
?
-
-
-
?
xylopentaose + H2O
?
45% of the activity with xyloheptaose
-
-
?
xylopentaose + H2O
?
-
-
-
-
?
xylopentaose + H2O
?
54% of the activity with xyloheptaose
-
-
?
xylopentaose + H2O
?
-
-
-
-
?
xylopentaose + H2O
?
-
-
-
?
xylopentaose + H2O
?
49% of the activity with xyloheptaose
-
-
?
xylopentaose + H2O
?
-
-
-
-
?
xylopentaose + H2O
xylobiose + xylotriose
-
-
-
-
?
xylopentaose + H2O
xylobiose + xylotriose
-
-
-
-
?
xylopentaose + H2O
xylobiose + xylotriose
rapid cleavage
-
-
?
xylopentaose + H2O
xylobiose + xylotriose
-
-
-
?
xylopentaose + H2O
xylobiose + xylotriose
-
-
-
?
xylopentaose + H2O
xylobiose + xylotriose
-
rapid cleavage
-
-
?
xylopentaose + H2O
xylobiose + xylotriose
-
-
-
-
?
xylopentaose + H2O
xylobiose + xylotriose
-
-
-
-
?
xylopentaose + H2O
xylobiose + xylotriose
rapid cleavage
-
-
?
xylopentaose + H2O
xylobiose + xylotriose + xylotetraose
-
can be hydrolyzed by the Aspergillus parent and hybrid xylanase
-
-
?
xylopentaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
-
?
xylopentaose + H2O
xylobiose + xylotriose + xylotetraose
-
-
-
-
?
xylopentaose + H2O
xylobiose + xylotriose + xylotetraose
-
can be hydrolyzed by the Thermomonospora parent and hybrid xylanase
-
-
?
xylopentaose + H2O
xylose + ?
-
-
-
?
xylopentaose + H2O
xylose + ?
-
-
-
?
xylopentaose + H2O
xylotriose + xylobiose
-
-
-
?
xylopentaose + H2O
xylotriose + xylobiose
-
-
-
?
xylopentaose + H2O
xylotriose + xylobiose
-
-
xylopentaose is hydrolyzed mainly to xylotriose and xylobiose with only minor amounts of xylotetraose
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
can be hydrolyzed by the Aspergillus parent and hybrid xylanase
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
low activity
-
-
?
xylotetraose + H2O
2 xylobiose
-
low activity
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
low activity
-
-
?
xylotetraose + H2O
2 xylobiose
low activity
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
-
-
?
xylotetraose + H2O
2 xylobiose
-
can be hydrolyzed by the Thermomonospora parent and hybrid xylanase
-
-
?
xylotetraose + H2O
?
-
-
-
?
xylotetraose + H2O
?
8% of the activity with xyloheptaose
-
-
?
xylotetraose + H2O
?
-
-
-
-
?
xylotetraose + H2O
?
-
-
-
-
?
xylotetraose + H2O
?
-
-
-
-
?
xylotetraose + H2O
?
-
-
-
-
?
xylotetraose + H2O
?
14% of the activity with xyloheptaose
-
-
?
xylotetraose + H2O
?
-
-
-
?
xylotetraose + H2O
?
1% of the activity with xyloheptaose
-
-
?
xylotetraose + H2O
?
-
low activity
-
-
?
xylotetraose + H2O
?
-
low activity
-
-
?
xylotetraose + H2O
?
-
-
-
-
?
xylotetraose + H2O
xylobiose + xylotriose
-
-
-
-
?
xylotetraose + H2O
xylobiose + xylotriose
-
-
-
-
?
xylotriose
xylobiose + xylotetraose
-
trans-xylosidation activity
-
?
xylotriose
xylobiose + xylotetraose
-
trans-xylosidation activity
-
?
xylotriose
xylobiose + xylotetraose
-
trans-xylosidation activity
-
?
xylotriose + H2O
?
-
can be hydrolyzed by the Aspergillus parent, no activity with hybrid xylanase
-
-
?
xylotriose + H2O
?
-
-
-
-
?
xylotriose + H2O
?
-
-
-
-
?
xylotriose + H2O
?
-
-
-
-
?
xylotriose + H2O
?
-
-
-
?
xylotriose + H2O
?
-
low activity
-
-
?
xylotriose + H2O
?
low activity
-
-
?
xylotriose + H2O
?
-
-
-
-
?
xylotriose + H2O
?
-
can be hydrolyzed by the Thermomonospora parent, no activity with hybrid xylanase
-
-
?
xylotriose + H2O
xylobiose + ?
-
-
-
?
xylotriose + H2O
xylobiose + ?
-
-
-
-
?
xylotriose + H2O
xylobiose + ?
-
-
-
-
?
xylotriose + H2O
xylobiose + D-xylose
-
-
-
?
xylotriose + H2O
xylobiose + D-xylose
-
-
-
?
xylotriose + H2O
xylobiose + D-xylose
-
-
-
-
?
xylotriose + H2O
xylobiose + xylose
-
-
-
?
xylotriose + H2O
xylobiose + xylose
-
-
-
?
xylotriose + H2O
xylobiose + xylose
-
-
-
?
xylotriose + H2O
xylobiose + xylose
-
-
-
-
?
xylotriose + H2O
xylobiose + xylose
low activity
-
-
?
xylotriose + H2O
xylobiose + xylose
-
hydrolyzed by xylanase I, no activity with xylanase III
xylanase I
?
xylotriose + H2O
xylobiose + xylose
-
weak activity
-
-
?
xylotriose + H2O
xylobiose + xylose
-
-
-
-
?
xylotriose + H2O
xylobiose + xylose
-
-
-
-
?
xylotriose + H2O
xylobiose + xylose
-
-
-
-
?
xylotriose + H2O
xylobiose + xylose
-
-
-
?
xylotriose + H2O
xylobiose + xylose
-
-
-
?
xylotriose + H2O
xylobiose + xylose
-
xylanase A
xylanase A
?
xylotriose + H2O
xylobiose + xylose
-
xylanase A
xylanase A
?
xylotriose + H2O
xylobiose + xylose
-
no activity
-
-
?
xylotriose + H2O
xylobiose + xylose
-
hydrolyzed by the 29000 Da enzyme form, no hydrolysis by the 20000 Da enzyme form
-
-
?
xylotriose + H2O
xylobiose + xylose
-
-
-
-
?
xylotriose + H2O
xylobiose + xylose
-
shortest unit susceptible to hydrolysis
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
soluble wheat straw xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
Rhodymenia palmata xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
corncob xylan
xylobiose is the main product, no production of D-xylose
?
1,4-beta-D-xylan + H2O
additional information
-
-
Remazol Brilliant Blue xylan
xylobiose + xylotriose + xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
birchwood xylan
xylobiose + xylotriose + xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
xylobiose + xylotriose + xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
Remazol Brilliant Blue xylan
xylobiose + xylotriose + xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
birchwood xylan
xylobiose + xylotriose + xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
xylobiose + xylotriose + xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
soluble xylan and insoluble xylan only after arabinosyl-initiated branch points are removed
oligosaccharides of intermediate length especially xylotriose and xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
oligosaccharides of intermediate length especially xylotriose and xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
hydrolyzes soluble xylan more rapidly than insoluble branched xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylobiose + xylotriose are produced from larchwood xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylose + xylobiose + xylotriose + higher oligomers
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylobiose + xylotriose + xylotetraose + xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylobiose + xylotriose + xylotetraose + xylopentaose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
hydrolysis products formed by enzyme component I of strain W1 and W2 are xylobiose + xylotriose + xylotetraose + xylopentaose, xylose is not formed. Hydrolysis products formed by enzyme component I of strain W1 and W2 are xylose + xylobiose + xylotriose + xylopentaose, xylotetraose is not formed. Xylobiose is the predominant product
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
hydrolysis products formed by enzyme component I of strain W1 and W2 are xylobiose + xylotriose + xylotetraose + xylopentaose, xylose is not formed. Hydrolysis products formed by enzyme component I of strain W1 and W2 are xylose + xylobiose + xylotriose + xylopentaose, xylotetraose is not formed. Xylobiose is the predominant product
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylose + xylobiose + xylotriose
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylobiose + xylotriose are produced from larchwood xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
birchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
birchwood xylan
xylose + xylobiose + xylotriose + xylotetraose
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylose + xylobiose + xylotriose
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylobiose + xylotriose are produced from larchwood xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
birchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
birchwood xylan
xylose + xylobiose + xylotriose + xylotetraose
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
soluble larchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
soluble larchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
low activity on larchwood xylan
release of xylobiose and some xylotriose from oat spelt xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
release of xylobiose and some xylotriose from oat spelt xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
release of xylobiose and some xylotriose from oat spelt xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
low activity on larchwood xylan
release of xylobiose and some xylotriose from oat spelt xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
release of xylobiose and some xylotriose from oat spelt xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
release of xylobiose and some xylotriose from oat spelt xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylobiose, xylotriose, xylose and small amounts of xylotetraose
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylanase A hydrolyzes larchwood xylan randomly, yielding xylohexaose, xylopentaose, xylotetraose, xylotriose and xylobiose. Xylanase B hydrolyzes xylan randomly with xylotriose and xylobiose as end products
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylose + xylobiose + xylotriose + higher oligomers
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylose + xylobiose + xylotriose, no arabinose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
at early stages of hydrolysis, polysaccharides of an intermediate degree of polymerization are detected. After complete hydrolysis, xylose and xylobiose are the major products
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylose + xylobiose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylose + xylobiose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
hyrolysis products formed by xylanase I are xylose, xylobiose and xylotriose. Xylobiose and xylotriose are the main products with xylanase III
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylose + xylobiose + xylotriose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
all basic types of plant xylan
D-xylose + 1,4-beta-D-xylooligosaccharides
?
1,4-beta-D-xylan + H2O
additional information
-
-
all basic types of plant xylan
D-xylose + 1,4-beta-D-xylooligosaccharides
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + arabinose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylose + xylobiose + xylotriose + xylotetraose + xylopentaose + arabinose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylose + xylobiose + xylotriose + xylotetraose are products formed by endo-beta-D-xylanase A. Xylobiose, xylotriose + xylotetraose are formed by endo-beta-D-xylanase B
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylose + xylobiose + xylotriose + xylotetraose are products formed by endo-beta-D-xylanase A. Xylobiose, xylotriose + xylotetraose are formed by endo-beta-D-xylanase B
?
1,4-beta-D-xylan + H2O
additional information
-
Pomacea insularus
-
birchwood xylan
xylobiose + xylotriose + xylotetraose + larger xylooligosaccharides
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
hydrolysis products with enzyme X-a are xylose + arabinose + glucose + xylobiose + xylooligosaccharides. The hydrolysis products with enzyme X-b-I and X-b-II are xylose + xylobiose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
hydrolysis products with enzyme X-a are xylose + arabinose + glucose + xylobiose + xylooligosaccharides. The hydrolysis products with enzyme X-b-I and X-b-II are xylose + xylobiose
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
with oat spelt xylan activity of the catalytic domain XYL-A1 is restricted to regions where xylopyranosyl residues do not carry arabinofuranosyl substituents, catalytic domain XYLA-C2 is able to release heterooligosaccharides carrying arabinofuranosyl residues
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
birchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
birchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylobiose is the main product
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
xylobiose is the main product
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
xylobiose is the main product
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
xylobiose is the main product
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
production of xylobiose, a mixture of xylo-oligosaccharides and a small amount of xylose
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
xylotriose + xylotetraose are the main products from soluble oat spelt xylan, xylose is produced at very low levels
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
xylotriose + xylotetraose are the main products from soluble oat spelt xylan, xylose is produced at very low levels
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylobiose and a small amount of xylose
?
1,4-beta-D-xylan + H2O
additional information
-
-
corncob xylan
production of xylose and xylobiose as main products from hardwood xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
hardwood xylan
production of xylose and xylobiose as main products from hardwood xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylobiose and a small amount of xylose
?
1,4-beta-D-xylan + H2O
additional information
-
-
corncob xylan
production of xylose and xylobiose as main products from hardwood xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
hardwood xylan
production of xylose and xylobiose as main products from hardwood xylan
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylobiose and traces of xylose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylobiose and traces of xylose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
xylan from oat spelt, xylanase A
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
xylan from oat spelt, xylanase A
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat xylan
production of xylose-containing oligosaccharides of 3-12 residues at the early stage of the reaction, xylobiose + xylotriose are produced after prolonged incubation
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
production of xylose-containing oligosaccharides of 3-12 residues at the early stage of the reaction, xylobiose + xylotriose are produced after prolonged incubation
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylooligosaccharides are observed at the beginning and after prolonged incubation, xylotriose and xylobiose are predominant, with a small amount of xylose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
aspen D-xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
birchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
birchwood xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat spelt xylan
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
insoluble birch xylan
xylobiose and higher xylo-oligomers as main hydrolysis products
?
1,4-beta-D-xylan + H2O
additional information
-
-
oat hulls xylan
xylobiose and higher xylo-oligomers as main hydrolysis products
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylobiose + small amounts of xylose
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
xylan from pear cell wall
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
larchwood xylan
-
-
?
acetylxylan + H2O
additional information
-
-
-
xylotriose + xylotetraose + xylopentaose + xylohexaose + xyloheptaose
?
arabinoxylan + H2O
additional information
-
-
-
xylotriose
?
arabinoxylan + H2O
additional information
-
-
-
-
-
?
arabinoxylan + H2O
additional information
-
-
-
-
-
?
arabinoxylan + H2O
additional information
-
-
arabinoxylan from rice-straw
xylobiose + arabinoxylan
?
arabinoxylan + H2O
additional information
-
-
from wheat bran
-
-
?
arabinoxylan + H2O
additional information
-
-
arabinoxylan from rice-straw
xylobiose + arabinoxylan
?
arabinoxylan + H2O
additional information
-
-
from wheat bran
-
-
?
arabinoxylan + H2O
additional information
-
-
-
xylobiose + arabinotetraose + smaller amounts of xylose, arabinoxylopentaose, xylotriose and traces of branched arabino-xylose oligosaccharides with a degree of polymerization from 4-9. Xylanase B produces less xylose but more xylotriose and xylotetraose than xylanase A
?
arabinoxylan + H2O
additional information
-
-
L-arabino-D-xylan
-
-
?
arabinoxylan + H2O
additional information
-
-
L-arabino-D-xylan
-
-
?
arabinoxylan + H2O
additional information
-
-
-
-
-
?
arabinoxylan + H2O
additional information
-
-
-
-
-
?
arabinoxylan + H2O
additional information
-
-
-
-
-
?
arabinoxylan + H2O
additional information
-
-
-
-
-
?
carboxymethylxylan + H2O
additional information
-
-
-
digestion with xylanase X results in a rapid fall in viscosity. Xylanase D hydrolyzes only the substituent oligosaccharides of xylan without affecting the degree of polymerization of the polysaccharide
?
feruloylxylan + H2O
additional information
-
-
-
xylobiose + xylotriose + xylotetraose + xylopentaose + xylohexaose + xyloheptaose
?
glucuronoxylan + H2O
additional information
-
-
enzymes from Trichoderma reesei and enzymes XlnB and XlnC of Streptomyces lividans release aldopentauronic acid as the shortest fragment
-
-
?
glucuronoxylan + H2O
additional information
-
-
Cryptococcus albidus enzyme and enzyme XlnA of Streptomyces lividans libertate aldotetrauronic acid as the shortest acidic fragment
-
-
?
glucuronoxylan + H2O
additional information
-
-
enzymes from Trichoderma reesei and enzymes XlnB and XlnC of Streptomyces lividans release aldopentauronic acid as the shortest fragment
-
-
?
glucuronoxylan + H2O
additional information
-
-
Cryptococcus albidus enzyme and enzyme XlnA of Streptomyces lividans libertate aldotetrauronic acid as the shortest acidic fragment
-
-
?
glucuronoxylan + H2O
additional information
-
-
Cryptococcus albidus enzyme and enzyme XlnA of Streptomyces lividans libertate aldotetrauronic acid as the shortest acidic fragment
-
-
?
glucuronoxylan + H2O
additional information
-
-
enzymes from Trichoderma reesei and enzymes XlnB and XlnC of Streptomyces lividans release aldopentauronic acid as the shortest fragment
-
-
?
additional information
?
-
acts predominantly on polysaccharides with xylan as the main chain and substituted with varying amounts of glucuronic acids, such as in beechwood xylan, birchwood xylan and 4-O-methylglucuronoxylan
-
-
?
additional information
?
-
-
enzyme also acts on arabinoxylans, reaction of EC 3.2.1.55
-
-
?
additional information
?
-
-
CtXynGH30 shows the release of a series of higher xylooligosaccharides, implying the endo-acting cleavageby the enzyme. No activity on 4-nitrophenyl-beta-D-xylopyranoside indicating that CtXynGH30 lacks exo-cleaving activity. No activity with carob galactomannan, galactan (lupin), beta-D-glucan (barley), carboxy methylcellulose, pecticgalactan (apple), pecticgalactan (Citrus), pecticgalactan (lupin), rhamnogalacturonan, curdlan, pullulan, and pustulan
-
-
?
additional information
?
-
-
the enzyme does not present activity against arabinan, oat spelt xylan, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-L-arabinopyranoside, and 4-nitrophenyl alpha L-arabinopyranoside
-
-
?
additional information
?
-
-
the enzyme does not present activity against arabinan, oat spelt xylan, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl beta-L-arabinopyranoside, and 4-nitrophenyl alpha L-arabinopyranoside
-
-
?
additional information
?
-
acts predominantly on polysaccharides with xylan as the main chain and substituted with varying amounts of glucuronic acids, such as in beechwood xylan, birchwood xylan and 4-O-methylglucuronoxylan
-
-
?
additional information
?
-
-
residues Asp60, Tyr35 and Glu141 play a role in the pH-dependent activity of xylanase XYL1p, overview
-
-
?
additional information
?
-
-
Xyn10A is an endoxylanase. No activity with cellulose, carboxymethyl cellulose, and xanthan gum
-
-
?
additional information
?
-
no activity with 4-nitrophenyl galactopyranoside, 4-nitrophenyl glucopyranoside, Avicel and carboxymethyl cellulose
-
-
?
additional information
?
-
the purified recombinant enzyme Xyn10B is highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Xyn10B is a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities, the latter two with p-nitrophenyl arabinofuranoside and p-nitrophenyl acetate as substrates, respectively. No activity with Avicel, carboxymethyl cellulose, p-nitrophenyl galactopyranoside, and p-nitrophenyl glucopyranoside
-
-
?
additional information
?
-
-
Xyn10A is an endoxylanase. No activity with cellulose, carboxymethyl cellulose, and xanthan gum
-
-
?
additional information
?
-
no activity with 4-nitrophenyl galactopyranoside, 4-nitrophenyl glucopyranoside, Avicel and carboxymethyl cellulose
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl galactopyranoside, 4-nitrophenyl glucopyranoside, Avicel and carboxymethyl cellulose
-
-
?
additional information
?
-
the purified recombinant enzyme Xyn10B is highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Xyn10B is a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities, the latter two with p-nitrophenyl arabinofuranoside and p-nitrophenyl acetate as substrates, respectively. No activity with Avicel, carboxymethyl cellulose, p-nitrophenyl galactopyranoside, and p-nitrophenyl glucopyranoside
-
-
?
additional information
?
-
-
the purified recombinant enzyme Xyn10B is highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Xyn10B is a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities, the latter two with p-nitrophenyl arabinofuranoside and p-nitrophenyl acetate as substrates, respectively. No activity with Avicel, carboxymethyl cellulose, p-nitrophenyl galactopyranoside, and p-nitrophenyl glucopyranoside
-
-
?
additional information
?
-
no activity with 4-nitrophenyl galactopyranoside, 4-nitrophenyl glucopyranoside, Avicel and carboxymethyl cellulose
-
-
?
additional information
?
-
the purified recombinant enzyme Xyn10B is highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Xyn10B is a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities, the latter two with p-nitrophenyl arabinofuranoside and p-nitrophenyl acetate as substrates, respectively. No activity with Avicel, carboxymethyl cellulose, p-nitrophenyl galactopyranoside, and p-nitrophenyl glucopyranoside
-
-
?
additional information
?
-
-
substrates are oat spelt xylan, corncob, corn hull, cane bagasse, and rice straw. Purified recombinant XynS14 shows more endo-1,4-beta-xylanase activity on xylan and xylooligosaccharides than on xylotriose
-
-
?
additional information
?
-
-
substrates are oat spelt xylan, corncob, corn hull, cane bagasse, and rice straw. Purified recombinant XynS14 shows more endo-1,4-beta-xylanase activity on xylan and xylooligosaccharides than on xylotriose
-
-
?
additional information
?
-
the enzyme is an arabinofuranose that may also act as xylanosidase. The enzyme additionally releases xylobiose and xylotriose from wheat arabinoxylan and is active on xylooligosaccharides (xylohexaose 1.2/mM/min, xylopentaose 6.9/mM/min, and xylotetraose 19.7/mM/min), however a lower level of activity
-
-
?
additional information
?
-
-
no activity with starch, glucose, fructose, sorbitol, or maltose
-
-
?
additional information
?
-
-
no activity with starch, glucose, fructose, sorbitol, or maltose
-
-
?
additional information
?
-
AfXynB rapidly hydrolyzes xylotetraose and slightly hydrolyze xylotriose to xylobiose as the major end product without formation of the corresponding amount of xylose, but hardly hydrolyzes xylobiose. No activity with 4-nitrophenyl beta-D-xylopyranoside and carboxymethyl cellulose
-
-
?
additional information
?
-
-
AfXynB rapidly hydrolyzes xylotetraose and slightly hydrolyze xylotriose to xylobiose as the major end product without formation of the corresponding amount of xylose, but hardly hydrolyzes xylobiose. No activity with 4-nitrophenyl beta-D-xylopyranoside and carboxymethyl cellulose
-
-
?
additional information
?
-
the extracellular xylanase has an endohydrolytic mode of action and hydrolyzes xylotriose to xylobiose through transglycosylation. It can efficiently degrade xylan to mainly yield xylobiose, xylotriose, xylopentose and xylohexaose. In addition, enzyme AfXynA is effective in hydrolyzing pretreated corncobs. No activity with carboxymethyl cellulose, barley glucan, and debranched arabinan or the 4-nitrophenyl glycosides such as 4-nitrophenyl-beta-xylopyranoside
-
-
?
additional information
?
-
-
the extracellular xylanase has an endohydrolytic mode of action and hydrolyzes xylotriose to xylobiose through transglycosylation. It can efficiently degrade xylan to mainly yield xylobiose, xylotriose, xylopentose and xylohexaose. In addition, enzyme AfXynA is effective in hydrolyzing pretreated corncobs. No activity with carboxymethyl cellulose, barley glucan, and debranched arabinan or the 4-nitrophenyl glycosides such as 4-nitrophenyl-beta-xylopyranoside
-
-
?
additional information
?
-
AfXynB rapidly hydrolyzes xylotetraose and slightly hydrolyze xylotriose to xylobiose as the major end product without formation of the corresponding amount of xylose, but hardly hydrolyzes xylobiose. No activity with 4-nitrophenyl beta-D-xylopyranoside and carboxymethyl cellulose
-
-
?
additional information
?
-
the extracellular xylanase has an endohydrolytic mode of action and hydrolyzes xylotriose to xylobiose through transglycosylation. It can efficiently degrade xylan to mainly yield xylobiose, xylotriose, xylopentose and xylohexaose. In addition, enzyme AfXynA is effective in hydrolyzing pretreated corncobs. No activity with carboxymethyl cellulose, barley glucan, and debranched arabinan or the 4-nitrophenyl glycosides such as 4-nitrophenyl-beta-xylopyranoside
-
-
?
additional information
?
-
AfXynB rapidly hydrolyzes xylotetraose and slightly hydrolyze xylotriose to xylobiose as the major end product without formation of the corresponding amount of xylose, but hardly hydrolyzes xylobiose. No activity with 4-nitrophenyl beta-D-xylopyranoside and carboxymethyl cellulose
-
-
?
additional information
?
-
the extracellular xylanase has an endohydrolytic mode of action and hydrolyzes xylotriose to xylobiose through transglycosylation. It can efficiently degrade xylan to mainly yield xylobiose, xylotriose, xylopentose and xylohexaose. In addition, enzyme AfXynA is effective in hydrolyzing pretreated corncobs. No activity with carboxymethyl cellulose, barley glucan, and debranched arabinan or the 4-nitrophenyl glycosides such as 4-nitrophenyl-beta-xylopyranoside
-
-
?
additional information
?
-
AfXynB rapidly hydrolyzes xylotetraose and slightly hydrolyze xylotriose to xylobiose as the major end product without formation of the corresponding amount of xylose, but hardly hydrolyzes xylobiose. No activity with 4-nitrophenyl beta-D-xylopyranoside and carboxymethyl cellulose
-
-
?
additional information
?
-
the extracellular xylanase has an endohydrolytic mode of action and hydrolyzes xylotriose to xylobiose through transglycosylation. It can efficiently degrade xylan to mainly yield xylobiose, xylotriose, xylopentose and xylohexaose. In addition, enzyme AfXynA is effective in hydrolyzing pretreated corncobs. No activity with carboxymethyl cellulose, barley glucan, and debranched arabinan or the 4-nitrophenyl glycosides such as 4-nitrophenyl-beta-xylopyranoside
-
-
?
additional information
?
-
AfXynB rapidly hydrolyzes xylotetraose and slightly hydrolyze xylotriose to xylobiose as the major end product without formation of the corresponding amount of xylose, but hardly hydrolyzes xylobiose. No activity with 4-nitrophenyl beta-D-xylopyranoside and carboxymethyl cellulose
-
-
?
additional information
?
-
the extracellular xylanase has an endohydrolytic mode of action and hydrolyzes xylotriose to xylobiose through transglycosylation. It can efficiently degrade xylan to mainly yield xylobiose, xylotriose, xylopentose and xylohexaose. In addition, enzyme AfXynA is effective in hydrolyzing pretreated corncobs. No activity with carboxymethyl cellulose, barley glucan, and debranched arabinan or the 4-nitrophenyl glycosides such as 4-nitrophenyl-beta-xylopyranoside
-
-
?
additional information
?
-
AfXynB rapidly hydrolyzes xylotetraose and slightly hydrolyze xylotriose to xylobiose as the major end product without formation of the corresponding amount of xylose, but hardly hydrolyzes xylobiose. No activity with 4-nitrophenyl beta-D-xylopyranoside and carboxymethyl cellulose
-
-
?
additional information
?
-
the extracellular xylanase has an endohydrolytic mode of action and hydrolyzes xylotriose to xylobiose through transglycosylation. It can efficiently degrade xylan to mainly yield xylobiose, xylotriose, xylopentose and xylohexaose. In addition, enzyme AfXynA is effective in hydrolyzing pretreated corncobs. No activity with carboxymethyl cellulose, barley glucan, and debranched arabinan or the 4-nitrophenyl glycosides such as 4-nitrophenyl-beta-xylopyranoside
-
-
?
additional information
?
-
-
negligible activity is observed on carboxymethylcellulose
-
-
?
additional information
?
-
-
negligible activity is observed on carboxymethylcellulose
-
-
?
additional information
?
-
-
facilitating hemicellulose degradation
-
-
?
additional information
?
-
-
endo mechanism of Xln-1 and substrate specificity, overview, no activity with carboxymethyl cellulose, starch, pectin, and 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
almost no activity on xylobiose
-
-
?
additional information
?
-
-
almost no activity on xylobiose
-
-
?
additional information
?
-
no substrate: xylotriose
-
-
?
additional information
?
-
-
endo mechanism of Xln-1 and substrate specificity, overview, no activity with carboxymethyl cellulose, starch, pectin, and 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
almost no activity on xylobiose
-
-
?
additional information
?
-
ribose, fructose, galactose, glucose, mannose, cellobiose, raffinose, lactose and xylitol do not induce xylanase activity
-
-
?
additional information
?
-
ribose, fructose, galactose, glucose, mannose, cellobiose, raffinose, lactose and xylitol do not induce xylanase activity
-
-
?
additional information
?
-
-
no activity against synthetic o- and p-nitrophenyl derivatives of xylose and glucopyranose, carboxylmethylcellulose, locust bean gum, avicel, and laminarin
-
-
?
additional information
?
-
-
no activity against synthetic o- and p-nitrophenyl derivatives of xylose and glucopyranose, carboxylmethylcellulose, locust bean gum, avicel, and laminarin
-
-
?
additional information
?
-
has negligible activity against insoluble and soluble cellulose substrates (avicel and carboxymethyl cellulose, respectively) and other glucose-based substrates (laminarin and lichenan)
-
-
?
additional information
?
-
-
has negligible activity against insoluble and soluble cellulose substrates (avicel and carboxymethyl cellulose, respectively) and other glucose-based substrates (laminarin and lichenan)
-
-
?
additional information
?
-
-
the enzyme shows exo-acting activity against synthetic 4-nitrophenyl xylopyranoside substrates. Molecular interaction analysis of the enzyme with xylobiose, xylotriose, xylotetraose, xylopentaose, and xylohexose, and of xyloologisaccharides with the sugar binding domain (BIAXBP) of probiotic strains, detailed overview. The purified extrecllular enzyme shows maximum activity 2.7 U/ml against beechwood xylan, 2.3 U/ml with birchwood xylan, 1.2 U/ml with glucuronoxylan, and 0.8 U/ml with arabinoxylan
-
-
?
additional information
?
-
-
the enzyme shows exo-acting activity against synthetic 4-nitrophenyl xylopyranoside substrates. Molecular interaction analysis of the enzyme with xylobiose, xylotriose, xylotetraose, xylopentaose, and xylohexose, and of xyloologisaccharides with the sugar binding domain (BIAXBP) of probiotic strains, detailed overview. The purified extrecllular enzyme shows maximum activity 2.7 U/ml against beechwood xylan, 2.3 U/ml with birchwood xylan, 1.2 U/ml with glucuronoxylan, and 0.8 U/ml with arabinoxylan
-
-
?
additional information
?
-
has negligible activity against insoluble and soluble cellulose substrates (avicel and carboxymethyl cellulose, respectively) and other glucose-based substrates (laminarin and lichenan)
-
-
?
additional information
?
-
the main product of hydrolysis by XynA are xylobiose, xylotriose, xylotetraose and other xylooligosaccharides, only trace amount of xylose appear
-
-
?
additional information
?
-
-
the main product of hydrolysis by XynA are xylobiose, xylotriose, xylotetraose and other xylooligosaccharides, only trace amount of xylose appear
-
-
?
additional information
?
-
the main product of hydrolysis by XynA are xylobiose, xylotriose, xylotetraose and other xylooligosaccharides, only trace amount of xylose appear
-
-
?
additional information
?
-
-
the main product of hydrolysis by XynA are xylobiose, xylotriose, xylotetraose and other xylooligosaccharides, only trace amount of xylose appear
-
-
?
additional information
?
-
-
transferase activity
-
-
?
additional information
?
-
-
transferase activity
-
-
?
additional information
?
-
-
substrate specificity shows a high activity on xylan-containing substrate and cellulase-free nature as endoxylanase
-
-
?
additional information
?
-
-
no activity with Avicel, carboxymethyl cellulose, cellulose, and pectin
-
-
?
additional information
?
-
-
substrate specificity shows a high activity on xylan-containing substrate and cellulase-free nature as endoxylanase
-
-
?
additional information
?
-
-
no activity with Avicel, carboxymethyl cellulose, cellulose, and pectin
-
-
?
additional information
?
-
-
digestion of a (1, 3),(1, 4)-beta-D-linkage sequence xylan from Rhodymenia into 4-linked xylobiose and xylotriose and 3,4-mixed linked oligosaccharides having a degree of polymerization of four or more
-
-
?
additional information
?
-
displays no transxylosylation activity toward xylitol, cellulose, chitin, chitosan, pectin, sorbitol, ribose, phenol, guaiacol, o-nitorphenol, vanilin and alcoholic compounds (methanol, ethanol, ethylene grecol and grecerol)
-
-
?
additional information
?
-
-
AMX-4 xylanase is not active toward other polysaccharides including carboxymethylcellulose, locust bean gum, lichenan, laminarin, and Avicel or toward synthetic substrate derivatives such as 4-nitrophenyl-beta-xylopyranoside, 4-nitrophenyl-beta-mannoside, and 4-nitrophenyl-beta-cellobioside, it can hydrolyze only beta-1,4-xylosidic linkages and has no beta-xylosidase activity
-
-
?
additional information
?
-
-
AMX-4 xylanase is not active toward other polysaccharides including carboxymethylcellulose, locust bean gum, lichenan, laminarin, and Avicel or toward synthetic substrate derivatives such as 4-nitrophenyl-beta-xylopyranoside, 4-nitrophenyl-beta-mannoside, and 4-nitrophenyl-beta-cellobioside, it can hydrolyze only beta-1,4-xylosidic linkages and has no beta-xylosidase activity
-
-
?
additional information
?
-
displays no transxylosylation activity toward xylitol, cellulose, chitin, chitosan, pectin, sorbitol, ribose, phenol, guaiacol, o-nitorphenol, vanilin and alcoholic compounds (methanol, ethanol, ethylene grecol and grecerol)
-
-
?
additional information
?
-
enzyme is responsible for softening of fruits during ripening, it is involved in cell wall degradation
-
-
?
additional information
?
-
or beta-1,4-glycosidic linkages in major plant structural polysaccharides
-
-
?
additional information
?
-
-
or beta-1,4-glycosidic linkages in major plant structural polysaccharides
-
-
?
additional information
?
-
or beta-1,4-glycosidic linkages in major plant structural polysaccharides
-
-
?
additional information
?
-
-
can not decompose carboxymethyl cellulose or xylobiose
-
-
?
additional information
?
-
no substrates: carboxymethyl cellulose or xylobiose
-
-
?
additional information
?
-
-
can not decompose carboxymethyl cellulose or xylobiose
-
-
?
additional information
?
-
no substrates: carboxymethyl cellulose or xylobiose
-
-
?
additional information
?
-
-
very low activity against xylooligosaccharides
-
-
?
additional information
?
-
no substrate: xylotriose
-
-
?
additional information
?
-
the enzyme is more active on xylans with high content of arabinose (rye arabinoxylan and wheat arabinoxylan) than on xylans with low content of arabinose (oat spelts xylan, birchwood xylan and beechwood xylan)
-
-
?
additional information
?
-
-
the enzyme is more active on xylans with high content of arabinose (rye arabinoxylan and wheat arabinoxylan) than on xylans with low content of arabinose (oat spelts xylan, birchwood xylan and beechwood xylan)
-
-
?
additional information
?
-
-
xylobiose and xylotriose do not bind at the cleft of Xyn11A
-
-
?
additional information
?
-
-
xylobiose and xylotriose do not bind at the cleft of Xyn11A
-
-
?
additional information
?
-
Mxyn10 shows activity on cellulose. Glu163 and Glu271 are the most likely residues located in the catalytic site of Mxyn10
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
enzyme displays high endo-1,4-beta-D-xylanase and low endo-beta-1,3-1,4-glucanase activities
-
-
?
additional information
?
-
enzyme displays high endo-1,4-beta-D-xylanase and low endo-beta-1,3-1,4-glucanase activities
-
-
?
additional information
?
-
enzyme displays high endo-1,4-beta-D-xylanase and low endo-beta-1,3-1,4-glucanase activities
-
-
?
additional information
?
-
-
enzyme displays high endo-1,4-beta-D-xylanase and low endo-beta-1,3-1,4-glucanase activities
-
-
?
additional information
?
-
-
no substrate: carboxymethylcellulose
-
-
?
additional information
?
-
Halalkalibacterium halodurans
-
no activity toward p-nitrophenyl-beta-D-xyloside, p-nitrophenyl-beta-D-glucoside, p-nitrophenyl-alpha-L-arabinofuranoside, p-nitrophenyl-acetate, or carboxymethylcellulose
-
-
?
additional information
?
-
Halalkalibacterium halodurans
-
no detectable activity with carboxymethyl cellulose, avicel, laminarin, p-nitrophenyl-beta-galactopyranoside, p-nitrophenyl-alpha-glucopyranoside, p-nitrophenyl-beta-xylopyranoside, p-nitrophenyl-alpha-L-arabinofuranoside, p-nitrophenyl-acetate or p-nitrophenyl-alpha-D-xylopyranoside
-
-
?
additional information
?
-
Halalkalibacterium halodurans
the alkaliphilic bacterium produces an alkaline active xylanase, the alkaline active xylanases have highly acidic surfaces and fewer solvent exposed alkali labile residues, mechanisms of high pH stability and catalysis, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans
residues Val169, Ile170 and Asp171 are important to hydrolyze xylan at high pH
-
-
?
additional information
?
-
Halalkalibacterium halodurans C-1
-
no activity toward p-nitrophenyl-beta-D-xyloside, p-nitrophenyl-beta-D-glucoside, p-nitrophenyl-alpha-L-arabinofuranoside, p-nitrophenyl-acetate, or carboxymethylcellulose
-
-
?
additional information
?
-
Halalkalibacterium halodurans S7
-
no detectable activity with carboxymethyl cellulose, avicel, laminarin, p-nitrophenyl-beta-galactopyranoside, p-nitrophenyl-alpha-glucopyranoside, p-nitrophenyl-beta-xylopyranoside, p-nitrophenyl-alpha-L-arabinofuranoside, p-nitrophenyl-acetate or p-nitrophenyl-alpha-D-xylopyranoside
-
-
?
additional information
?
-
Halalkalibacterium halodurans S7
the alkaliphilic bacterium produces an alkaline active xylanase, the alkaline active xylanases have highly acidic surfaces and fewer solvent exposed alkali labile residues, mechanisms of high pH stability and catalysis, overview
-
-
?
additional information
?
-
Halalkalibacterium halodurans S7
residues Val169, Ile170 and Asp171 are important to hydrolyze xylan at high pH
-
-
?
additional information
?
-
-
xylanase 1 and xylanase 2 are both inactive toward Avicel, carboxymethylcellulose, beta-glucan, arabinan (linear and branched), and (galacto)mannans. NO activity with xylotriose
-
-
?
additional information
?
-
hydrolysis of xylan, extracted of bagasse, by XYN11Ks_480 produces xylooligosaccharides without xylose formation. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-1,4-xylosidic bridges
-
-
?
additional information
?
-
hydrolysis of xylan, extracted of bagasse, by XYN11Ks_480 produces xylooligosaccharides without xylose formation. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-1,4-xylosidic bridges
-
-
?
additional information
?
-
-
hydrolysis of xylan, extracted of bagasse, by XYN11Ks_480 produces xylooligosaccharides without xylose formation. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-1,4-xylosidic bridges
-
-
?
additional information
?
-
XYN10Ks_480 shows high hydrolytic activity with xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-(1,4)-xylosidic bridges
-
-
?
additional information
?
-
XYN10Ks_480 shows high hydrolytic activity with xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-(1,4)-xylosidic bridges
-
-
?
additional information
?
-
-
XYN10Ks_480 shows high hydrolytic activity with xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-(1,4)-xylosidic bridges
-
-
?
additional information
?
-
hydrolysis of xylan, extracted of bagasse, by XYN11Ks_480 produces xylooligosaccharides without xylose formation. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-1,4-xylosidic bridges. No activityy with carboxymethylcellulose, soluble starch, and Avicel. Substrate specificity, overview
-
-
?
additional information
?
-
hydrolysis of xylan, extracted of bagasse, by XYN11Ks_480 produces xylooligosaccharides without xylose formation. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-1,4-xylosidic bridges. No activityy with carboxymethylcellulose, soluble starch, and Avicel. Substrate specificity, overview
-
-
?
additional information
?
-
-
hydrolysis of xylan, extracted of bagasse, by XYN11Ks_480 produces xylooligosaccharides without xylose formation. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-1,4-xylosidic bridges. No activityy with carboxymethylcellulose, soluble starch, and Avicel. Substrate specificity, overview
-
-
?
additional information
?
-
XYN10Ks_480 shows high hydrolytic activity with xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-(1,4)-xylosidic bridges. No activityy with carboxymethylcellulose, soluble starch, and Avicel. Substrate specificity, overview
-
-
?
additional information
?
-
XYN10Ks_480 shows high hydrolytic activity with xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-(1,4)-xylosidic bridges. No activityy with carboxymethylcellulose, soluble starch, and Avicel. Substrate specificity, overview
-
-
?
additional information
?
-
-
XYN10Ks_480 shows high hydrolytic activity with xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-(1,4)-xylosidic bridges. No activityy with carboxymethylcellulose, soluble starch, and Avicel. Substrate specificity, overview
-
-
?
additional information
?
-
hydrolysis of xylan, extracted of bagasse, by XYN11Ks_480 produces xylooligosaccharides without xylose formation. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-1,4-xylosidic bridges
-
-
?
additional information
?
-
hydrolysis of xylan, extracted of bagasse, by XYN11Ks_480 produces xylooligosaccharides without xylose formation. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-1,4-xylosidic bridges
-
-
?
additional information
?
-
hydrolysis of xylan, extracted of bagasse, by XYN11Ks_480 produces xylooligosaccharides without xylose formation. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-1,4-xylosidic bridges. No activityy with carboxymethylcellulose, soluble starch, and Avicel. Substrate specificity, overview
-
-
?
additional information
?
-
hydrolysis of xylan, extracted of bagasse, by XYN11Ks_480 produces xylooligosaccharides without xylose formation. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-1,4-xylosidic bridges. No activityy with carboxymethylcellulose, soluble starch, and Avicel. Substrate specificity, overview
-
-
?
additional information
?
-
XYN10Ks_480 shows high hydrolytic activity with xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-(1,4)-xylosidic bridges
-
-
?
additional information
?
-
XYN10Ks_480 shows high hydrolytic activity with xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-(1,4)-xylosidic bridges
-
-
?
additional information
?
-
XYN10Ks_480 shows high hydrolytic activity with xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-(1,4)-xylosidic bridges. No activityy with carboxymethylcellulose, soluble starch, and Avicel. Substrate specificity, overview
-
-
?
additional information
?
-
XYN10Ks_480 shows high hydrolytic activity with xylan extracted of bagasse, three types of xylan-based substrates are used to produce xylose and xylooligosaccharides. Xylose sugar oligomers contain 2-7 xylose units (X2-X7) linked by beta-(1,4)-xylosidic bridges. No activityy with carboxymethylcellulose, soluble starch, and Avicel. Substrate specificity, overview
-
-
?
additional information
?
-
-
does not hydrolyze xylobiose
-
-
?
additional information
?
-
activity decreases in the following order: oat spelt xylan, beechwood xylan, birchwood xylan, wheat arabinoxylan. No substrates: xyloglucan, carboxymethylcellulose, locust beangum, and 4-nitrophenyl sugar derivatives
-
-
?
additional information
?
-
enzyme exhibits strict specificity for various xylans as substrates, but displays no activity toward avicel, carboxymethyl cellulose, locust bean gum and lichenan, or 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-fucopyranoside and 4-nitrophenyl beta-D-galactopyranoside
-
-
?
additional information
?
-
enzyme exhibits strict specificity for various xylans as substrates, but displays no activity toward avicel, carboxymethyl cellulose, locust bean gum and lichenan, or 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-fucopyranoside and 4-nitrophenyl beta-D-galactopyranoside
-
-
?
additional information
?
-
-
xylanase B shows high glycosyltransferase activity
-
-
?
additional information
?
-
no substrates: barley beta-glucan, carboxymethyl cellulose sodium salt, laminarin, microcrystalline cellulose, or 2 mmol/l 4-nitrophenyl-beta-D-xylopyranoside
-
-
?
additional information
?
-
-
substrate specificity for different xylans, overview, isozyme Ia, Ib, Ic, and IIa show also arabinose-releasing property on larchwood xylan
-
-
?
additional information
?
-
-
substrate specificity for different xylans, overview, isozyme Ia, Ib, Ic, and IIa show also arabinose-releasing property on larchwood xylan
-
-
?
additional information
?
-
no substrate: cellulose
-
-
?
additional information
?
-
no substrate: cellulose
-
-
?
additional information
?
-
no substrate: cellulose
-
-
?
additional information
?
-
-
no substrate: cellulose
-
-
?
additional information
?
-
no substrate: cellulose
-
-
?
additional information
?
-
no substrate: cellulose
-
-
?
additional information
?
-
no substrate: cellulose
-
-
?
additional information
?
-
enzyme displays endo-beta-1,4-xylanase activity together with beta-1,3/beta-1,4-glucanase activity. No substrate: xylobiose
-
-
?
additional information
?
-
enzyme displays endo-beta-1,4-xylanase activity together with beta-1,3/beta-1,4-glucanase activity. No substrate: xylobiose
-
-
?
additional information
?
-
enzyme degrades degraded xylooligosaccharides more than xylotetraose. No substrates: avicel, carboxymethyl cellulose, lichenan, soluble starch, glucomannan, galactomannan, or arabinan, 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-L-arabinopyranoside. The enzyme also catalyzes transglycosylation. Xylobiose to xylohexaose are transglycolated by xylobiose units during the early degradation step, respectively
-
-
?
additional information
?
-
-
enzyme degrades degraded xylooligosaccharides more than xylotetraose. No substrates: avicel, carboxymethyl cellulose, lichenan, soluble starch, glucomannan, galactomannan, or arabinan, 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-L-arabinopyranoside. The enzyme also catalyzes transglycosylation. Xylobiose to xylohexaose are transglycolated by xylobiose units during the early degradation step, respectively
-
-
?
additional information
?
-
enzyme degrades degraded xylooligosaccharides more than xylotetraose. No substrates: avicel, carboxymethyl cellulose, lichenan, soluble starch, glucomannan, galactomannan, or arabinan, 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-L-arabinopyranoside. The enzyme also catalyzes transglycosylation. Xylobiose to xylohexaose are transglycolated by xylobiose units during the early degradation step, respectively
-
-
?
additional information
?
-
-
enzyme degrades degraded xylooligosaccharides more than xylotetraose. No substrates: avicel, carboxymethyl cellulose, lichenan, soluble starch, glucomannan, galactomannan, or arabinan, 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-L-arabinopyranoside. The enzyme also catalyzes transglycosylation. Xylobiose to xylohexaose are transglycolated by xylobiose units during the early degradation step, respectively
-
-
?
additional information
?
-
-
purified xylanase shows the maximum specificity for beechwood xylan and wheat bran. No substrates: avicel, carboxymethyl cellulose
-
-
?
additional information
?
-
-
purified xylanase shows the maximum specificity for beechwood xylan and wheat bran. No substrates: avicel, carboxymethyl cellulose
-
-
?
additional information
?
-
no activity against carboxy methyl cellulose, beta-glucan, lichenan, laminarin, agarose, starch, and kappa-carageenan
-
-
?
additional information
?
-
-
no activity against carboxy methyl cellulose, beta-glucan, lichenan, laminarin, agarose, starch, and kappa-carageenan
-
-
?
additional information
?
-
no substrate: xylotriose
-
-
?
additional information
?
-
-
capable of hydrolyzing 1,3-alpha-L-arabinofuranosyl branch points
-
-
?
additional information
?
-
-
capable of hydrolyzing 1,3-alpha-L-arabinofuranosyl branch points
-
-
?
additional information
?
-
the proximal sugar-ring of the substrate distorts from 4C1 chair to 2,5B boat conformation. Key role of Tyr69 in stabilizing the boat in preference to the 4C1 chair conformation
-
-
?
additional information
?
-
beta-1,4-endoxylanases are enzymes which randomly hydrolyse the beta-1,4-glycosidic bonds in the xylan backbone
-
-
?
additional information
?
-
the enzyme has an endohydrolytic mode of action and can hydrolyse xylotriose to xylobiose through transglycosylation
-
-
?
additional information
?
-
beta-1,4-endoxylanases are enzymes which randomly hydrolyse the beta-1,4-glycosidic bonds in the xylan backbone
-
-
?
additional information
?
-
the enzyme has an endohydrolytic mode of action and can hydrolyse xylotriose to xylobiose through transglycosylation
-
-
?
additional information
?
-
no activity with Avicel, carboxymethyl cellulose, and D-(+)-cellobiose
-
-
?
additional information
?
-
no activity with Avicel, carboxymethyl cellulose, and D-(+)-cellobiose
-
-
?
additional information
?
-
can effectively hydrolyze agricultural wastes, e.g., corn cob, corn hull, rice husk (which has a strong structure and is normally not easy to hydrolyze), rice straw, and bagasse
-
-
?
additional information
?
-
-
can effectively hydrolyze agricultural wastes, e.g., corn cob, corn hull, rice husk (which has a strong structure and is normally not easy to hydrolyze), rice straw, and bagasse
-
-
?
additional information
?
-
the enzyme hydrolyzes birchwood xylan and xylooligosaccharides, to produce mainly xylobiose, acting as an endoxylanase. Xyn10B also shows transglycosylation activity with xylooligosaccharides, overview
-
-
?
additional information
?
-
-
the enzyme hydrolyzes birchwood xylan and xylooligosaccharides, to produce mainly xylobiose, acting as an endoxylanase. Xyn10B also shows transglycosylation activity with xylooligosaccharides, overview
-
-
?
additional information
?
-
-
enzyme exhibits endo-xylanase, beta-xylosidase, and arabinoxylan arabinofuranohydrolase, EC 3.2.1.55, activities. It prefers to hydrolyze long-chain xylooligosaccharides rather than xylobiose
-
-
?
additional information
?
-
-
enzyme shows bifunctional degradation activity toward xylan and beta-glucan and also degrades microcrystalline cellulose
-
-
?
additional information
?
-
enzyme shows exo-beta-xylanase EC 3.2.1.37, endoxylanase EC 3.2.1.8 and alpha-L-arabinofuranosidase EC 3.2.1.55 activities
-
-
?
additional information
?
-
-
enzyme exhibits endo-xylanase, beta-xylosidase, and arabinoxylan arabinofuranohydrolase, EC 3.2.1.55, activities. It prefers to hydrolyze long-chain xylooligosaccharides rather than xylobiose
-
-
?
additional information
?
-
-
enzyme shows bifunctional degradation activity toward xylan and beta-glucan and also degrades microcrystalline cellulose
-
-
?
additional information
?
-
can effectively hydrolyze agricultural wastes, e.g., corn cob, corn hull, rice husk (which has a strong structure and is normally not easy to hydrolyze), rice straw, and bagasse
-
-
?
additional information
?
-
-
can effectively hydrolyze agricultural wastes, e.g., corn cob, corn hull, rice husk (which has a strong structure and is normally not easy to hydrolyze), rice straw, and bagasse
-
-
?
additional information
?
-
enzyme shows exo-beta-xylanase EC 3.2.1.37, endoxylanase EC 3.2.1.8 and alpha-L-arabinofuranosidase EC 3.2.1.55 activities
-
-
?
additional information
?
-
-
no activity with xylobiose and xylotriose
-
-
?
additional information
?
-
no substrates: avicel, carboxymethyl cellulose, cellulose
-
-
?
additional information
?
-
no substrates: avicel, carboxymethyl cellulose, cellulose
-
-
?
additional information
?
-
-
clarification of fruit juice with Pediococcus acidilactici GC25 xylanase, overview
-
-
?
additional information
?
-
-
clarification of fruit juice with Pediococcus acidilactici GC25 xylanase, overview
-
-
?
additional information
?
-
no activity against p-nitrophenyl-beta-D-xylopyranoside and p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
additional information
?
-
-
no activity against p-nitrophenyl-beta-D-xylopyranoside and p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
additional information
?
-
no activity against p-nitrophenyl-beta-D-xylopyranoside and p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
additional information
?
-
-
no detectable activity on xylobiose
-
-
?
additional information
?
-
-
catalytic residue is E85. No activity with xylotriose by XynB. Molecular determinants of substrate and inhibitor specificities of the GH11 enzyme, kinetic analysis and homology modeling, overview
-
-
?
additional information
?
-
-
specificities of xylanases against birchwood xylan, oat spelt xylan, carboxymethylcellulose, Overview
-
-
?
additional information
?
-
no activity towards carboxymethylcellulose-sodium, lichenan, or barley beta-glucan
-
-
?
additional information
?
-
composition of the hydrolysis products from oat spelt xylan, birchwood xylan, and soluble wheat arabinoxylan are 43.3% xylose and 56.7% xylobiose, 41.0% xylose and 59.0% xylobiose, and 42.4% xylose, and 57.6% xylobiose, respectively
-
-
?
additional information
?
-
-
no arabinose-releasing activity with arabinoxylan substrates from rye arabinoxylan and birchwood xylan
-
-
?
additional information
?
-
-
no arabinose-releasing activity with arabinoxylan substrates from rye arabinoxylan and birchwood xylan
-
-
?
additional information
?
-
-
does not use rice bran, cellulose, starch and pullulan as a substrate
-
-
?
additional information
?
-
-
does not use rice bran, cellulose, starch and pullulan as a substrate
-
-
?
additional information
?
-
unrooted evolutionary tree, overview
-
-
?
additional information
?
-
enzyme shows no cellulase, chitosanase, and lichenase activity
-
-
?
additional information
?
-
-
no activity against other polysaccharides, no arabinofuranosidase and beta-xylosidase activity, enzyme contains no xylan-binding domain
-
-
?
additional information
?
-
enzyme PsGH10A hydrolyzes products of xylan and substituted xylan indicate production of series of short-chain xylooligosaccharides and arabinoxylo-saccharides, substrate specificity, overview
-
-
?
additional information
?
-
enzyme PsGH10A hydrolyzes products of xylan and substituted xylan indicate production of series of short-chain xylooligosaccharides and arabinoxylo-saccharides, substrate specificity, overview
-
-
?
additional information
?
-
enzyme PsGH10A hydrolyzes products of xylan and substituted xylan indicate production of series of short-chain xylooligosaccharides and arabinoxylo-saccharides, substrate specificity, overview
-
-
?
additional information
?
-
enzyme PsGH10A hydrolyzes products of xylan and substituted xylan indicate production of series of short-chain xylooligosaccharides and arabinoxylo-saccharides, substrate specificity, overview
-
-
?
additional information
?
-
enzyme PsGH10A hydrolyzes products of xylan and substituted xylan indicate production of series of short-chain xylooligosaccharides and arabinoxylo-saccharides, substrate specificity, overview
-
-
?
additional information
?
-
enzyme PsGH10A hydrolyzes products of xylan and substituted xylan indicate production of series of short-chain xylooligosaccharides and arabinoxylo-saccharides, substrate specificity, overview
-
-
?
additional information
?
-
enzyme PsGH10A hydrolyzes products of xylan and substituted xylan indicate production of series of short-chain xylooligosaccharides and arabinoxylo-saccharides, substrate specificity, overview
-
-
?
additional information
?
-
-
enzyme acts xylanolytic with no side-activities against other plant polysaccharides
-
-
?
additional information
?
-
-
enzyme acts xylanolytic with no side-activities against other plant polysaccharides
-
-
?
additional information
?
-
-
no activity with cellulose, cellobiose, and carboxymethyl cellulose
-
-
?
additional information
?
-
-
no substrates: carboxymethyl cellulose, cellulose, cellobiose
-
-
?
additional information
?
-
-
no activity with cellulose, cellobiose, and carboxymethyl cellulose
-
-
?
additional information
?
-
-
no substrates: carboxymethyl cellulose, cellulose, cellobiose
-
-
?
additional information
?
-
-
no activity towards xylobiose and xylotriose
-
-
?
additional information
?
-
-
no activity towards xylobiose and xylotriose
-
-
?
additional information
?
-
-
neither the catalytic domain XYLA-A1 nor XYLA-C2 can hydrolyze oligomers of DP 4 and lower. Except in the case of xylohexaose the rate of attack of different xylooligosaccharides by XYLA-A1 is higher than that shown by XYLA-C2
-
-
?
additional information
?
-
hydrolysis of best substrate beechwood xylan by the enzyme results in formation of xylobiose and xylose as major products. The enzyme is specific for xylan acting as an endo-type xylanase. Soluble oat spelt xylan is also a good substrate, while insoluble oat spelt xylan is not. No activity with Avicel, 4-nitrophenyl beta-D-xylopyranoside, and locust bean gum
-
-
?
additional information
?
-
hydrolysis of best substrate beechwood xylan by the enzyme results in formation of xylobiose and xylose as major products. The enzyme is specific for xylan acting as an endo-type xylanase. Soluble oat spelt xylan is also a good substrate, while insoluble oat spelt xylan is not. No activity with Avicel, 4-nitrophenyl beta-D-xylopyranoside, and locust bean gum
-
-
?
additional information
?
-
no substrates: caboxymethyl cellulose, avicel, filter paper
-
-
?
additional information
?
-
no substrates: carboxymethyl cellulose, Avicel, galactan, barley beta-glucan, and xyloglucan
-
-
?
additional information
?
-
no substrates: carboxymethyl cellulose, Avicel, galactan, barley beta-glucan, and xyloglucan
-
-
?
additional information
?
-
-
no substrates: carboxymethyl cellulose, Avicel, galactan, barley beta-glucan, and xyloglucan
-
-
?
additional information
?
-
MK331807
the xylobiose yield from 10 g corncob and moso bamboo reached 1.123 g and 0.229 g, respectively, at pH 6.5 and 70 °C. High ratios of xylobiose in the xylose-based product of about 85% are obtained from corncob, moso bamboo sawdust, cassava stem and Chinese fir sawdust
-
-
?
additional information
?
-
-
the xylobiose yield from 10 g corncob and moso bamboo reached 1.123 g and 0.229 g, respectively, at pH 6.5 and 70 °C. High ratios of xylobiose in the xylose-based product of about 85% are obtained from corncob, moso bamboo sawdust, cassava stem and Chinese fir sawdust
-
-
?
additional information
?
-
-
no activity on CM-cellulose
-
-
?
additional information
?
-
-
substrate specificity, no activity with cellulose, carboxymethylcellulose, 4-nitrophenyl beta-D-xylopyranoside, and 4-nitrophenyl beta-D-glucopyranoside
-
-
?
additional information
?
-
-
substrate specificity, no activity with cellulose, carboxymethylcellulose, 4-nitrophenyl beta-D-xylopyranoside, and 4-nitrophenyl beta-D-glucopyranoside
-
-
?
additional information
?
-
carbohydrate-binding module (CBM) of XynAS27 plays a key role in the hydrolysis of insoluble substrate, and the CBM and linker region are also important for the enzyme stability, and the linker region contributes more
-
-
?
additional information
?
-
-
no activity on CM-cellulose
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
releases chromophoric material from bagasse pulp. Amounts of reducing sugars released by the enzyme from bagasse pulp are significantly greater than that released from wheat and rice straw pulps. It decreases the kappa number of pulps, improves pulp brightness and reduces the chlorine dioxide consumption on pulp
-
-
?
additional information
?
-
no detectable activity on xylobiose
-
-
?
additional information
?
-
the catalytic efficiency increases slightly with increasing their chain length with a small difference of the XynD catalytic efficiency against the different xylooligosaccharides
-
-
?
additional information
?
-
-
the catalytic efficiency increases slightly with increasing their chain length with a small difference of the XynD catalytic efficiency against the different xylooligosaccharides
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
the enzyme acts as an endoxylanase. The enzyme is also active on xylooligosaccharides, main product is xylobiose and very little xylose is produced. No transglycosylation occurs
-
-
?
additional information
?
-
-
the enzyme acts as an endoxylanase. The enzyme is also active on xylooligosaccharides, main product is xylobiose and very little xylose is produced. No transglycosylation occurs
-
-
?
additional information
?
-
the enzyme acts as an endoxylanase. The enzyme is also active on xylooligosaccharides, main product is xylobiose and very little xylose is produced. No transglycosylation occurs
-
-
?
additional information
?
-
enzyme TtGH8 is effective at the degradation of xylan-based substrates, notably beta-1,4-xylan and mixed-linkage (beta-1,3/beta-1,4) marine xylan
-
-
?
additional information
?
-
-
enzyme TtGH8 is effective at the degradation of xylan-based substrates, notably beta-1,4-xylan and mixed-linkage (beta-1,3/beta-1,4) marine xylan
-
-
?
additional information
?
-
the enzyme TtGH8 is a xylan-active endoxylanase with six catalytically relevant subsites and notably a maximal activity towards mixed-linkage (beta-1,3/beta-1,4) marine xylan, TtGH8 catalyses the hydrolysis of beta-1,4-xylohexaose and displays maximal activity against mixed-linked marine polymeric xylans
-
-
?
additional information
?
-
-
the enzyme TtGH8 is a xylan-active endoxylanase with six catalytically relevant subsites and notably a maximal activity towards mixed-linkage (beta-1,3/beta-1,4) marine xylan, TtGH8 catalyses the hydrolysis of beta-1,4-xylohexaose and displays maximal activity against mixed-linked marine polymeric xylans
-
-
?
additional information
?
-
enzyme TtGH8 is effective at the degradation of xylan-based substrates, notably beta-1,4-xylan and mixed-linkage (beta-1,3/beta-1,4) marine xylan
-
-
?
additional information
?
-
the enzyme TtGH8 is a xylan-active endoxylanase with six catalytically relevant subsites and notably a maximal activity towards mixed-linkage (beta-1,3/beta-1,4) marine xylan, TtGH8 catalyses the hydrolysis of beta-1,4-xylohexaose and displays maximal activity against mixed-linked marine polymeric xylans
-
-
?
additional information
?
-
enzyme TtGH8 is effective at the degradation of xylan-based substrates, notably beta-1,4-xylan and mixed-linkage (beta-1,3/beta-1,4) marine xylan
-
-
?
additional information
?
-
the enzyme TtGH8 is a xylan-active endoxylanase with six catalytically relevant subsites and notably a maximal activity towards mixed-linkage (beta-1,3/beta-1,4) marine xylan, TtGH8 catalyses the hydrolysis of beta-1,4-xylohexaose and displays maximal activity against mixed-linked marine polymeric xylans
-
-
?
additional information
?
-
-
substrate specificity, active with arabinoxylan and arabinogalactan, least specificity towards amylopectin and guar gum, overview
-
-
?
additional information
?
-
-
enzyme tolerates the replacement of beta-xylopyranosyl units in several artificial substrates by beta-glucopyranosyl, alpha-L-arabinopyranosyl, and alpha-L-arabinofuranosyl units
-
-
?
additional information
?
-
-
no substrates: cellulose powder, carboxymethyl cellulose and avicel
-
-
?
additional information
?
-
-
no substrates: cellulose powder, carboxymethyl cellulose and avicel
-
-
?
additional information
?
-
Thermochaetoides thermophila
recombinant Xyn11A fails to hydrolyze CMC, avicel or p-nitrophenyl beta-xylopyranoside
-
-
?
additional information
?
-
Thermochaetoides thermophila
the bifunctional enzyme also shows endoglucanase activity (EC 3.2.1.4) hydrolyzing carboxymethyl cellulose and barley beta-glucan. Substrate specificity, overview. The enzyme shows endoglucanase, but not xylanase, activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively. No xylanase activity with (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose
-
-
?
additional information
?
-
Thermochaetoides thermophila CBS 144.50
the bifunctional enzyme also shows endoglucanase activity (EC 3.2.1.4) hydrolyzing carboxymethyl cellulose and barley beta-glucan. Substrate specificity, overview. The enzyme shows endoglucanase, but not xylanase, activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively. No xylanase activity with (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose
-
-
?
additional information
?
-
Thermochaetoides thermophila DSM 1495
the bifunctional enzyme also shows endoglucanase activity (EC 3.2.1.4) hydrolyzing carboxymethyl cellulose and barley beta-glucan. Substrate specificity, overview. The enzyme shows endoglucanase, but not xylanase, activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively. No xylanase activity with (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose
-
-
?
additional information
?
-
Thermochaetoides thermophila IMI 039719
the bifunctional enzyme also shows endoglucanase activity (EC 3.2.1.4) hydrolyzing carboxymethyl cellulose and barley beta-glucan. Substrate specificity, overview. The enzyme shows endoglucanase, but not xylanase, activity with pretreated wheat straw and filter paper. CTendo7 produces cellooligosaccharides and xylooligosaccharides from the continuous enzymatic saccharification of carboxymethyl cellulose-Na and xylan, respectively. No xylanase activity with (+)-arabinogalactan, D-galacto-D-mannan, amylose, chitin, and sucrose
-
-
?
additional information
?
-
Thermochaetoides thermophila NIBGE 1
recombinant Xyn11A fails to hydrolyze CMC, avicel or p-nitrophenyl beta-xylopyranoside
-
-
?
additional information
?
-
-
no arabinofuranosidase activity
-
-
?
additional information
?
-
-
no activity with mannan, araban, galactomannan, inulin, Avicel, soluble starch, sodium carboxymethylcellulose, 2- or 4-nitrophenyl-gluco-, xylo-, manno-, galacto-pyranosides, and arabinofuranoside
-
-
?
additional information
?
-
-
facilitating hemicellulose degradation
-
-
?
additional information
?
-
-
no activity with corn fiber xylan
-
-
?
additional information
?
-
-
releases chromophoric material from bagasse pulp. Amounts of reducing sugars released by the enzyme from bagasse pulp are significantly greater than that released from wheat and rice straw pulps. It decreases the kappa number of pulps, improves pulp brightness and reduces the chlorine dioxide consumption on pulp
-
-
?
additional information
?
-
-
enzyme displays no other enzyme activity such as cellulase, beta-glucosidase, beta-mannosidase, alpha-arabinofuranosidase, or beta-xylosidase
-
-
?
additional information
?
-
-
no substrates: 4-nitrophenyl beta-D--xyloside, 4-nitrophenyl beta-cellobioside
-
-
?
additional information
?
-
-
no substrates: 4-nitrophenyl beta-D--xyloside, 4-nitrophenyl beta-cellobioside
-
-
?
additional information
?
-
-
enzyme displays no other enzyme activity such as cellulase, beta-glucosidase, beta-mannosidase, alpha-arabinofuranosidase, or beta-xylosidase
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl beta-D-xylopyranoside and 4-nitrophenyl cellobioside
-
-
?
additional information
?
-
the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover
-
-
?
additional information
?
-
the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover
-
-
?
additional information
?
-
the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover
-
-
?
additional information
?
-
the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover
-
-
?
additional information
?
-
the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover
-
-
?
additional information
?
-
the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover
-
-
?
additional information
?
-
the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover
-
-
?
additional information
?
-
the enzyme significantly cooperates with a commercial cellulase, it perfoms saccharification of the pretreated corn stover
-
-
?
additional information
?
-
-
no substrate: avicel
-
-
?
additional information
?
-
-
enzyme displays both endo- and exoglucanase activities. No substrate: avicel
-
-
?
additional information
?
-
-
enzyme exhibits both endoglucanase and xylanase activites, reactions of EC 3.2.1.4 and 3.2.1.8, respectively
-
-
?
additional information
?
-
-
no substrate: avicel
-
-
?
additional information
?
-
-
enzyme displays both endo- and exoglucanase activities. No substrate: avicel
-
-
?
additional information
?
-
-
substrate specificity, no activity with Avicel, filter paper, starch, amylopectin, pullulan, galactoglucomannan, or galactomannan
-
-
?
additional information
?
-
-
substrate specificity, no activity with Avicel, filter paper, starch, amylopectin, pullulan, galactoglucomannan, or galactomannan
-
-
?
additional information
?
-
no activity against Avicel, starch, laminarin and Whatman filter paper 42 is observed
-
-
?
additional information
?
-
no activity against Avicel, starch, laminarin and Whatman filter paper 42 is observed
-
-
?
additional information
?
-
-
no activity with sucrose and maltose
-
-
?
additional information
?
-
-
facilitating hemicellulose degradation
-
-
?
additional information
?
-
pretreatment of substrates canola meal and mustard bran significantly increases the relative content of pentose sugars
-
-
?
additional information
?
-
-
xylobiose is not hydrolyzed
-
-
?
additional information
?
-
B2CNY5
no activity with Avicel, carboxymethylcellulose, and gellan gum
-
-
?
additional information
?
-
-
no activity with Avicel, carboxymethylcellulose, and gellan gum
-
-
?
additional information
?
-
-
Xyn2 shows no activity with gellan gum, Avicel, and carboxymethyl cellulose
-
-
?
additional information
?
-
B2CNY5
no activity with Avicel, carboxymethylcellulose, and gellan gum
-
-
?
additional information
?
-
-
no activity with Avicel, carboxymethylcellulose, and gellan gum
-
-
?
additional information
?
-
the endo-1,4-beta-xylanase activity is determined according to the colorimetric method of Biely using 4-O-methyl-D-glucurono-D-xylan as substrate and Remazol Brilliant Blue R dye
-
-
?
additional information
?
-
-
the endo-1,4-beta-xylanase activity is determined according to the colorimetric method of Biely using 4-O-methyl-D-glucurono-D-xylan as substrate and Remazol Brilliant Blue R dye
-
-
?
additional information
?
-
RuCelA is a bifunctional xylanase/endoglucanase showing activity against xylan and carboxymethyl cellulose. Using xylan and barley glucan as substrates, RuCelA displays obvious synergistic effects with beta-1,4-xylosidase and beta-1,4-glucosidase. RuCelA can produce xylo-oligosaccharides and cello-oligosaccharides in the continuous saccharification of pretreated rice straw
-
-
?
additional information
?
-
no activitiy with beta-1,3-glucan, laminarin, or Avicel as substrates
-
-
?
additional information
?
-
substrate specificity and hydrolysis pattern
-
-
?
oat spelt xylan + H2O
additional information
-
-
87% activity compared to beechwood xylan
xylooligosaccharides are the enzymatic products of xylan hydrolysis, the smallest degradation product is xylobiose
-
?
oat spelt xylan + H2O
additional information
-
-
87% activity compared to beechwood xylan
xylooligosaccharides are the enzymatic products of xylan hydrolysis, the smallest degradation product is xylobiose
-
?
rhodymenan + H2O
additional information
-
-
-
Cryptococcus albidus enzyme and enzyme XlnA of Streptomyces lividans libertate an isomeric xylotriose of the structure Xylbeta1-3Xylbeta1-4Xyl as the shortest acidic fragment
?
rhodymenan + H2O
additional information
-
-
-
releases besides 1,4-beta-linked product, isomeric xylooligosaccharides containing 1,3-beta linkages
?
rhodymenan + H2O
additional information
-
-
-
enzymes from Trichoderma reesei and enzymes XlnB and XlnC of Streptomyces lividans libertate an isomeric xylotetraose as the shortest fragment containing a beta-1,3-linkage
?
rhodymenan + H2O
additional information
-
-
-
releases besides 1,4-beta-linked product, isomeric xylooligosaccharides containing 1,3-beta linkages
?
rhodymenan + H2O
additional information
-
-
-
Cryptococcus albidus enzyme and enzyme XlnA of Streptomyces lividans libertate an isomeric xylotriose of the structure Xylbeta1-3Xylbeta1-4Xyl as the shortest acidic fragment
?
rhodymenan + H2O
additional information
-
-
-
enzymes from Trichoderma reesei and enzymes XlnB and XlnC of Streptomyces lividans libertate an isomeric xylotetraose as the shortest fragment containing a beta-1,3-linkage
?
rhodymenan + H2O
additional information
-
-
-
Cryptococcus albidus enzyme and enzyme XlnA of Streptomyces lividans libertate an isomeric xylotriose of the structure Xylbeta1-3Xylbeta1-4Xyl as the shortest acidic fragment
?
rhodymenan + H2O
additional information
-
-
-
3-O-beta-xylopyranosyl-4-O-beta-D-xylopyranosyl-D-xylose + xylose
?
rhodymenan + H2O
additional information
-
-
-
enzymes from Trichoderma reesei and enzymes XlnB and XlnC of Streptomyces lividans libertate an isomeric xylotetraose as the shortest fragment containing a beta-1,3-linkage
?
xylan + H2O
additional information
-
-
xylan from birchwood and wheat bran insoluble xylan
reaction products are xylose to xylopentaose with xylotriose as the major product
-
?
xylan + H2O
additional information
-
Halalkalibacterium halodurans
-
xylan from birchwood, oat spelt, and larchwood
a series of xylooligosaccharides larger than xylotriose are released as the major products by Xyl I
-
?
xylan + H2O
additional information
-
Halalkalibacterium halodurans C-1
-
xylan from birchwood, oat spelt, and larchwood
a series of xylooligosaccharides larger than xylotriose are released as the major products by Xyl I
-
?
xylohexaose + H2O
additional information
-
-
-
-
-
?
xylohexaose + H2O
additional information
-
-
-
-
-
?
xylohexaose + H2O
additional information
-
-
-
xylotriose is produced by the catalytic domain XYLA-A1, xylobiose, xylotriose and xylotetraose are produced by the catalytic domain XYLA-A1
?
xylohexaose + H2O
additional information
-
-
-
-
-
?
xylohexaose + H2O
additional information
-
-
-
-
-
?
xylopentaose + H2O
additional information
-
-
-
-
-
?
xylopentaose + H2O
additional information
-
-
-
-
-
?
xylopentaose + H2O
additional information
-
-
-
xylose + xylobiose + xylotriose
?
xylopentaose + H2O
additional information
-
-
-
-
-
?
xylopentaose + H2O
additional information
-
-
-
xylobiose + xylotriose
?
xylopentaose + H2O
additional information
-
-
-
-
-
?
xylopentaose + H2O
additional information
-
-
-
-
-
?
xylopentaose + H2O
additional information
-
-
-
-
-
?
xylotetraose + H2O
additional information
-
-
-
xylanase I produces xylobiose + xylose + xylotriose. Xylanase II produces only xylobiose in the early stage of reaction
?
xylotetraose + H2O
additional information
-
-
-
-
-
?
xylotetraose + H2O
additional information
-
-
-
-
-
?
xylotetraose + H2O
additional information
-
-
-
-
-
?
xylotetraose + H2O
additional information
-
-
-
-
-
?
xylotetraose + H2O
additional information
-
-
-
-
-
?
xylotetraose + H2O
additional information
-
-
-
-
-
?
xylotetraose + H2O
additional information
-
-
xylanase A
xylobiose + small amounts of xylose and xylotriose, xylanase A
?
xylotetraose + H2O
additional information
-
-
xylanase A
xylobiose + small amounts of xylose and xylotriose, xylanase A
?
xylotetraose + H2O
additional information
-
-
no activity
-
-
?
xylotetraose + H2O
additional information
-
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-4,5-epoxypentyl-beta-D-xyloside
-
-
1,10-phenanthroline
-
6 mM, 70% inhibition
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
-
at 100 mM 20% inhibition of PhX20, 30% inhibition of PhX33
1-Fluoro-2,4-dinitrobenzene
-
-
2,4,6-Trinitrobenzenesulfonic acid
-
at 1 mM 90% inhibition of PhX20, 30% inhibition of PhX33
2,4-dinitrophenyl 2-deoxy-2-fluoro-beta-D-xylobioside
2,4-dinitrophenolate is released, due to covalent inactivation of the active enzyme, used for active site titrations
2-Hydroxy-5-nitrobenzyl bromide
5,5'-dithiobis-(2-nitrobenzoic acid)
citraconic anhydride
-
at 50 mM no inhibition of PhX20, 10% inhibition of PhX33
Cr2+
-
7.5 mM, strong inhibition
D-xylan
-
above 1% w/v, substrate inhibition
diethyldicarbonate
-
at 5 mM 95% inhibition of PhX20, 10% inhibition of PhX33
ethanol
5%, 16% inhibition of activity with carboxymethyl cellulose, 24% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
guanidine hydrochloride
84% inhibition at 2 M
Isopropanol
5%, 21.6% inhibition of activity with carboxymethyl cellulose, 53% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
leupeptin
-
inhibits the native enzyme
mercuribenzoate
-
5 mM, 40% inhibition of enzyme component I of strain W1 and W2
methanol
5%, 26.5% inhibition of activity with carboxymethyl cellulose, 13.5% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
MnCl2
-
1 mM, 29% inhibition of xylanase 2, 20% inhibition of xylanase 1
N-Acetylimidazole
-
100 mM, 79% inhibition
N-bromosuccinamide
-
oxidation of one or two tryptophan residues by N-bromosuccinamide per enzyme molecule is sufficient to inhibit the enzyme activity completely
N-ethyl-5-phenylisoxazolium-3'-sulfonate
-
-
N-ethylmaleimide
-
inhibits the native enzyme
N-tosyl-L-phenylalanine chloromethyl ketone
-
inhibits the native enzyme
NaH2PO4
-
100 mM, 50% inhibition
NaN3
0.1%, 45.2% inhibition of activity with carboxymethyl cellulose, 12.25% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
NiCl2
-
1 mM, 19% inhibition of xylanase 2, no inhibition of xylanase 1
omega-epoxyalkyl glycosides of D-xylopyranose
-
irreversible
-
oxo(phenyl)acetaldehyde
-
-
PEG 200
4%, 46% inhibition
pepstatin A
Thermomonospora sp.
-
50% inhibition at 0.0005 mM, inhibition is due to interference in the electronic microenvironment and disruption of hydrogen bonding network around the essential histidine residue
phenyl methane sulfonyl fluoride
-
-
Phenylglyoxal
-
at 10 mM 25% inhibition of PhX20, no inhibition of PhX33
Phenylmethylsulfonylfluoride
-
at 10 mM 15% inhibition of PhX20, 10% inhibition of PhX33
phosphate buffer
has a negative effect on the xylanase activity, as it reduces the activity around to 60%
-
polyhexamethylbiguanid
-
77.29% residual activity at 2 mM
RbCl
-
5 mM, 55% inhibition
Ru2+
Halalkalibacterium halodurans
-
95% residual activity at 1 mM
trans-1,2-diaminocyclohexane-N',N',N',N'-tetraacetic acid
-
strong inhibition
Triticum aestivum endoxylanase inhibitor-I
-
-
Triticum aestivum endoxylanase inhibitor-II
-
-
Triticum aestivum xylanase inhibitor
-
Triticum aestivum xylanase inhibitor-I
-
Triticum aestivum xylanase inhibitor-II
-
-
-
Tween 60
0.05%, 78% residual activity
Tween 80
1%, 33.29% loss of activity
xylanase inhibiting protein
-
xylanase inhibitor protein
-
xylanase inhibitor protein-I
-
xylanase-inhibiting protein
-
XIP
-
xylotriose
-
acts as the end product inhibitor of Xyn11A
ZnSO4
-
1 mM, 19% inhibition of xylanase 2, no inhibition of xylanase 1
2-Hydroxy-5-nitrobenzyl bromide
1 mM, 27% inhibition
2-Hydroxy-5-nitrobenzyl bromide
-
10 mM, 94% inhibition
2-mercaptoethanol
-
-
2-mercaptoethanol
1 mM, 88% residual activity
5,5'-dithiobis-(2-nitrobenzoic acid)
-
-
5,5'-dithiobis-(2-nitrobenzoic acid)
-
-
Ag+
-
weak inhibition
Ag+
-
5 mM, enzyme component I and II of strain W1 and W2, partial inhibition
Ag+
-
1 mM, 52% inhibition
Ag+
1 mM, no residual activity
Ag+
-
complete inhibition above 0.15 mM
Ag+
complete inhibition at 1 mM
Ag+
90% inhibition at 5 mM
Ag+
complete inhibition of XYN10G at 5 mM
Ag+
Pomacea insularus
-
AgNO3
Ag+
complete inhibition at 2 mM
Ag+
-
1 mM, 25% residual activity
Ag+
1 mM, 14% residual activity
Ag+
5 mM, no residual activity
Ag+
-
strongly inhibits by 69.1% even at the concentration of 1 mM
Ag+
1 mM inhibits about 60% of the activity of XynAS27, and less than 20% of the activities of XynAS27cd and XynAS27cdl
Ag+
1 mM strongly inhibits
Ag+
Thermochaetoides thermophila
18.5% inhibition at 1 mM, 62.5% inhibition at 5 mM; 5 mM, 62.5% loss of activity, substrate: xylan; 5 mM, 68.25% loss of activity, substrate: carboxymethyl cellulose
Ag+
-
10 mM, 16% residual activity
Ag2+
-
1 mM Ag(NO3)2, 33% inhibition
Ag2+
-
90% residual activity at 1 mM
Ag2+
-
5 mM, 20% residual activtiy
Al3+
27% inhibition at 1 mM
Al3+
-
70 mM, xylanase I and II
Al3+
-
1 mM, 46% inhibition
Al3+
1 mM, 46% residual activity
Al3+
-
5 mM, 25% of initial activity
Ba2+
-
1 mM, isoform xyl I, 49% inhibition, xyl II, 11% inhibition
Ba2+
10 mM, 77% residual activity
Ba2+
inhibits hydrolysis activity
Ba2+
-
inhibition of isozyme Ic
Ba2+
42% inhibition at 2 mM
Ba2+
1 mM, 72% residual activity
Ba2+
-
10 mM, 65% residual activity
Ba2+
-
5 mM, 88% residual activity
beta-mercaptoethanol
-
22% inhibition at 10 mM
Ca2+
-
slight inhibition
Ca2+
about 90% residual activity at 1 mM
Ca2+
-
1 mM, isoform xyl I, 71% inhibition, xyl II, 9% inhibition
Ca2+
completely inhibits hydrolysis activity
Ca2+
-
inactivation of xylanase B and C, slight inactivation of xylanase A
Ca2+
10 mM, more than 80% inhibition
Ca2+
-
10 mM, 4% inhibition
Ca2+
Halalkalibacterium halodurans
-
81% residual activity at 5 mM
Ca2+
-
95.39% residual activity at 2 mM
Ca2+
high inhibition at 5 mM
Ca2+
-
inhibits slightly at 5 mM
Ca2+
-
5 mM, 76% of initial activity
Ca2+
-
10 mM reduces the enzyme activity by 9.7%
Ca2+
7% inhibition at 1 mM
Ca2+
-
20 mM, mild inhibition
Ca2+
-
10 mM, significant inhibition
Ca2+
10 mM, activity decreased to 45%
Cd2+
-
CdCl2
Cd2+
1 mM, 73% residual activity
Cd2+
Halalkalibacterium halodurans
strong inhibition
Cd2+
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
Cd2+
10 mM, 37% loss of activity
Co2+
-
-
Co2+
-
1 mM, 81% inhibition
Co2+
-
70 mM, xylanase I and II
Co2+
-
10 mM, 25% inhibition
Co2+
inhibits hydrolysis activity
Co2+
1 mM, 64% residual activity
Co2+
10 mM, more than 80% inhibition
Co2+
-
10 mM, 19% inhibition
Co2+
-
1 mM, 22% inhibition
Co2+
Halalkalibacterium halodurans
-
63% residual activity at 5 mM
Co2+
-
in the presence of 10 mM, the relative xylanase activity decreases by 5%
Co2+
-
inhibition of isozyme Ic
Co2+
-
complete inhibition of xylanase II at 10 mM, 50% at 2 mM, no inhibition of xylanase I
Co2+
24% inhibition at 10 mM
Co2+
strong inhibition of XYN10G at 1 mM
Co2+
39% inhibition at 2 mM
Co2+
-
10 mM reduces the enzyme activity by 26.1%
Co2+
10 mM partially inhibits the activity of XynAS27
Co2+
10 mM partialy inhibits
Co2+
19% inhibition at 10mM
Co2+
Thermochaetoides thermophila
5 mM, 2% loss of activity, substrate: xylan
Co2+
1 mM, 11% inhibition
Co2+
10 mM, activity decreased to 60%
Cr3+
-
70 mM, xylanase I and II
Cr3+
18% inhibition at 10 mM
Cu2+
-
-
Cu2+
-
strong, both xylanase I and xylanase II
Cu2+
-
1 mM, 37% inhibition
Cu2+
-
70 mM, xylanase I and II
Cu2+
-
7.5 mM, strong inhibition
Cu2+
-
complete inhibition at 5 mM
Cu2+
-
10 mM, 66% inhibition
Cu2+
-
2 mM, complete inhibition
Cu2+
inhibits activity from 10 mM (72%) to 20 mM (88%)
Cu2+
-
5 mM, enzyme component I and II of strain W1 and W2, partial inhibition
Cu2+
-
1 mM, 30% loss of activity
Cu2+
-
inhibits the native enzyme
Cu2+
inhibits hydrolysis activity
Cu2+
5 mM, about 60% residual activity
Cu2+
-
inactivation of xylanase B and C, low inactivation of xylanase A
Cu2+
10 mM, more than 80% inhibition
Cu2+
-
1 mM, 95% inhibition
Cu2+
-
10 mM, 46% inhibition
Cu2+
Halalkalibacterium halodurans
-
13% residual activity at 5 mM
Cu2+
Halalkalibacterium halodurans
strong inhibition
Cu2+
-
in the presence of 10 mM, the relative xylanase activity decreases by 58.1%
Cu2+
2 mM, 77% residual activity; 2 mM, no residual activity; 2 mM, no residual activity
Cu2+
1 mM, 18% inhibition
Cu2+
-
91.44% residual activity at 2 mM
Cu2+
1 mM, 4.8% residual activity
Cu2+
-
1 mM, 85% residual activity
Cu2+
-
slight inhibition at 3 or 6 mM
Cu2+
-
strong inhibition of xylanase I and xylanase II
Cu2+
40% inhibition at 5-10 mM
Cu2+
strong inhibition of XYN10G at 1 mM
Cu2+
10 mM, 97% loss of activity
Cu2+
Pomacea insularus
-
-
Cu2+
-
87% residual activity at 1 mM
Cu2+
16% inhibition at 1 mM
Cu2+
85% inhibition at 2 mM
Cu2+
1 mM, no residual activity
Cu2+
-
1 mM, 2% residual activity
Cu2+
-
5 mM, 73% of initial activity
Cu2+
5 mM, 72% residual activity
Cu2+
-
10 mM reduces the enzyme activity by 49.6%
Cu2+
10 mM partialy inhibits
Cu2+
33% inhibition at 10mM
Cu2+
77% inhibition at 1 mM
Cu2+
-
10 mM, mild inhibition
Cu2+
-
5 mM, 121% of initial activity, 10 mM, 69% residual activity
Cu2+
Thermochaetoides thermophila
5 mM, complete loss of activity, substrate: carboxymethyl cellulose; 5 mM, complete loss of activity, substrate: xylan; complete inhibition at 1-5 mM
Cu2+
-
1 mM CuCl2, patial inhibition, xylanase A
Cu2+
5 mM, 1.6fold activation of activity with carboxymethyl cellulose, 16.4% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Cu2+
-
1 mM, 47% resiudal activity
Cu2+
-
5 mM, 40% residual activity
Cu2+
1 mM, 20% inhibition
Cu2+
10 mM, activity decreased to 20%
CuSO4
-
1 mM, isoform xyl I, 85% inhibition, xyl II, 24% inhibition
CuSO4
-
1 mM, 41% inhibition of xylanase 2, no inhibition of xylanase 1
diethyl dicarbonate
-
-
diethyl dicarbonate
-
22% inhibition at 10 mM
dithiothreitol
-
21% inhibition at 10 mM
dithiothreitol
1 mM, 83% residual activity
dithiothreitol
Halalkalibacterium halodurans
-
90% residual activity at 5 mM
dithiothreitol
Halalkalibacterium halodurans
-
1 mM, 65% residual activity
dithiothreitol
Pomacea insularus
-
-
dithiothreitol
-
5 mM, 70% residual activtiy
dithiothreitol
-
10 mM, 85% residual activity
DTNB
-
-
DTT
-
-
EDTA
about 78% residual activity at 50 mM
EDTA
-
19% inhibition at 10 mM
EDTA
-
10 mM, 67% inhibition
EDTA
-
2 mM, 62% residual activity
EDTA
-
5 mM, enzyme component I and II of strain W1 and W2, partial inhibition
EDTA
completely inhibits hydrolysis activity
EDTA
1 mM, about 60% residual activity
EDTA
1 mM, 79% residual activity
EDTA
-
unaffected by 5 mM EDTA
EDTA
Halalkalibacterium halodurans
-
61% residual activity at 5 mM
EDTA
-
in the presence of 10 mM, the relative xylanase activity decreases by 12.6%
EDTA
high inhibition at 5 mM
EDTA
1 mM, 73% residual activity
EDTA
-
inhibition of xylanase I and xylanase II
EDTA
36% inhibition at 2 mM
EDTA
1 mM, 35% residual activity
EDTA
59% inhibition at 5 mM
EDTA
-
strong inhibition at 20 mM, weak inhibition at 2 mM
EDTA
5 mM, 90.6% inhibition of activity with carboxymethyl cellulose, 1.1fold activation of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
EDTA
-
5 mM, 72% residual activity
EDTA
-
10 mM, 72% residual activity
Fe2+
-
-
Fe2+
10 mM, 83% residual activity
Fe2+
-
10 mM, 14% inhibition
Fe2+
inhibits activity at 20 mM by 27%
Fe2+
-
marked inactivation of xylanase A, B and C
Fe2+
10 mM, more than 80% inhibition
Fe2+
-
10 mM, 37% inhibition
Fe2+
-
in the presence of 10 mM, the relative xylanase activity decreases by 21.1%
Fe2+
-
81.9% residual activity at 2 mM
Fe2+
-
10 mM reduces the enzyme activity by 31.0%
Fe2+
-
5 mM, 74% residual activity
Fe2+
-
1 mM FeSO4, complete inhibition, xylanase A
Fe2+
5 mM, 2.9fold activation of activity with carboxymethyl cellulose, 6.7% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Fe3+
-
70 mM, xylanase I and II
Fe3+
-
inhibits the native enzyme
Fe3+
-
10 mM, 75% inhibition
Fe3+
-
inhibition of isozyme Ic
Fe3+
-
slight inhibition at 3 or 6 mM
Fe3+
40% inhibition at 10 mM
Fe3+
10 mM, 37% loss of activity
Fe3+
1 mM, 60% residual activity
Fe3+
-
10 mM reduces the enzyme activity by 11.3%
Fe3+
10 mM partially inhibits the activity of XynAS27
Fe3+
Thermochaetoides thermophila
5 mM, 70.3% loss of activity, substrate: carboxymethyl cellulose; 5 mM, 78.5% loss of activity, substrate: xylan; 8.3% inhibition at 1 mM, 78.5% inhibition at 5 mM
Fe3+
-
Fe2(SO4)3, 1 mM, complete inhibition, xylanase A
Fe3+
-
5 mM, 78% residual activity
Fe3+
5 mM, 1.1fold activation of activity with carboxymethyl cellulose, 9.1% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
FeSO4
-
FeSO4
-
1 mM, 61% residual activity
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
both isoform xyl I, xyl II, complete inhibition
Hg2+
-
96% inhibition at 10 mM
Hg2+
-
strong, both xylanase I and xylanase II
Hg2+
-
1 mM, complete inhibition
Hg2+
-
0.07 mM, xylanase I and II
Hg2+
-
7.5 mM, strong inhibition
Hg2+
-
10 mM, 70% inhibition
Hg2+
-
2 mM, complete inhibition
Hg2+
-
5 mM, enzyme component I and II of strain W1 and W2, completely inhibited
Hg2+
-
1 mM, complete inhibition
Hg2+
-
strong, no reactivation by EDTA
Hg2+
-
inhibits the native enzyme
Hg2+
-
HgCl2, xylanase A, B and C
Hg2+
1 mM, 32% residual activity
Hg2+
-
1 mM, complete inhibition of xylanase A and B
Hg2+
-
10 mM, 85% inhibition
Hg2+
-
0.1 mM, 30% inhibition
Hg2+
Halalkalibacterium halodurans
-
75% residual activity at 5 mM
Hg2+
Halalkalibacterium halodurans
-
1 mM, 10% residual activity
Hg2+
Halalkalibacterium halodurans
strong inhibition
Hg2+
1 mM, complete loss of activity
Hg2+
1 mM, no residual activity
Hg2+
-
inhibition of isozymes Ic and IIb
Hg2+
2 mM, 23% residual activity; 2 mM, 73% residual activity; 2 mM, no residual activity
Hg2+
1 mM, no residual activity
Hg2+
1 mM, 1% residual activiy
Hg2+
complete inhibition at 1 mM
Hg2+
-
no activity at 2 mM
Hg2+
almost complete inhibition at 5 mM
Hg2+
1 mM, 4.2% residual activity
Hg2+
-
strong inhibitory effect
Hg2+
-
strong inhibition of xylanase I and xylanase II
Hg2+
complete inhibition at 5 mM
Hg2+
-
2 mM, 20% residual activity for isoforms xynA, xynC, 67% residual activity for isoform xynB
Hg2+
complete inhibition of XYN10G at 5 mM
Hg2+
Pomacea insularus
-
-
Hg2+
-
27% residual activity at 1 mM
Hg2+
31% inhibition at 1 mM
Hg2+
complete inhibition at 2 mM
Hg2+
-
5 mM, 10% residual activtiy
Hg2+
1 mM, 60% residual activity
Hg2+
-
5 mM, 8% of initial activity
Hg2+
1 mM, 3% residual activity
Hg2+
5 mM, 34% residual activity
Hg2+
-
1 mM completely inhibits
Hg2+
almost completely inhibits
Hg2+
1 mM completely inhibits
Hg2+
complete inhibition at 1 mM
Hg2+
complete inhibition at 1 mM
Hg2+
-
2 mM, complete loss of activity; 2 mM HgCl2, complete inactivation
Hg2+
-
5 mM, no residual activity
Hg2+
-
10 mM, significant inhibition
Hg2+
-
1 mM HgCl2, complete inhibition, xylanase A
Hg2+
-
10 mM, 65% residual activity
Hg2+
-
6 mM, complete inhibition
Hg2+
-
6 mM, complete inhibition. Addition of 40 mM EDTA does not recover any lost activity
Hg2+
-
1 mM, 55% resiudal activity
Hg2+
-
5 mM, no residual activity
Hg2+
1 mM, 50% inhibition
HgCl2
-
1 mM, 85% inhibition of xylanase 2, 49% inhibition of xylanase 1
HgCl2
-
strong inhibition
iodoacetamide
59% inhibition at 5 mM
iodoacetate
-
5 mM, 21% loss of activity
iodoacetate
-
xylanase A, B and C
iodoacetate
-
isozymes A and B
iodoacetate
-
strong inhibition at 20 mM, weak inhibition at 2 mM
iodoacetate
-
10 mM, 13% inhibition
K+
-
about 80% residual activity at 20 mM
K+
10 mM, 33% loss of activity
K+
-
10 mM reduces the enzyme activity by 11.1%
K+
10 mM partialy inhibits
K+
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 13% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
KMnO4
-
-
KMnO4
-
almost complete inhibition of all 3 isozymes at 1 mM
Li+
-
weak inhibition
Li+
10 mM, 39% loss of activity
Li+
54% inhibition at 2 mM
Li+
-
10 mM reduces the enzyme activity by 16.1%
Mg2+
-
about 77% residual activity at 20 mM
Mg2+
-
10 mM, 3% inhibition
Mg2+
inhibits hydrolysis activity
Mg2+
Halalkalibacterium halodurans
-
90% residual activity at 5 mM
Mg2+
-
in the presence of 10 mM, the relative xylanase activity decreases by 19.1%
Mg2+
-
82.55% residual activity at 2 mM
Mg2+
high inhibition at 5 mM
Mg2+
-
slight inhibition at 3 or 6 mM
Mg2+
-
inhibits slightly at 5 mM
Mg2+
10 mM, 13% loss of activity
Mg2+
1 mM, 46% residual activity
Mg2+
Thermochaetoides thermophila
22.7% inhibition at 1 mM, 50.6% inhibition at 5 mM; 5 mM, 51% loss of activity, substrate: xylan; 5 mM, 64.5% loss of activity, substrate: carboxymethyl cellulose
Mg2+
-
5 mM, 74% residual activity
Mg2+
5 mM, 2.3fold activation of activity with carboxymethyl cellulose, 6.5% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
Mg2+
-
1 mM, 69% resiudal activity
Mg2+
-
5 mM, 54% residual activity
Mg2+
10 mM, activity decreased to 70%
Mn2+
40% inhibition at 1 mM; about 55% residual activity at 1 mM
Mn2+
-
strongly inhibits 80.5% of xylanase activity
Mn2+
more than 50% inhibition
Mn2+
-
1 mM, 87% inhibition
Mn2+
-
7.5 mM, strong inhibition
Mn2+
inhibits activity at 20 mM by 25%
Mn2+
inhibits hydrolysis activity
Mn2+
1 mM, 71% residual activity
Mn2+
-
1 mM, 38% inhibition
Mn2+
Halalkalibacterium halodurans
-
3% residual activity at 5 mM
Mn2+
Halalkalibacterium halodurans
-
1 mM, 4.8% residual activity
Mn2+
-
in the presence of 10 mM, the relative xylanase activity decreases by 44.3%
Mn2+
-
inhibition of isozyme Ic
Mn2+
high inhibition at 5 mM
Mn2+
-
strong inhibitory effect
Mn2+
10% inhibition at 1 mM
Mn2+
4 mM, 87% inhibition
Mn2+
1 mM, 73% residual activity
Mn2+
5 mM, 54% residual activity
Mn2+
10 mM partialy inhibits
Mn2+
19% inhibition at 5 mM, 60% at 10mM
Mn2+
-
10 mM, 65% residual activity
Mn2+
-
1 mM, 57% resiudal activity
Mn2+
-
5 mM, 46% residual activity
Mn2+
1 mM, 71% inhibition
N-bromosuccimide
-
-
N-bromosuccimide
complete inhibition at 5 mM
N-bromosuccinimide
-
partial protection by xylan
N-bromosuccinimide
-
complete inhibition at 5 mM
N-bromosuccinimide
-
inactivation
N-bromosuccinimide
-
strong inhibition, isozymes A and B
N-bromosuccinimide
-
xylan protects from inactivation
N-bromosuccinimide
5 mM, complete loss of activity
N-bromosuccinimide
-
inhibition of isozymes Ic and IIb
N-bromosuccinimide
1 mM, 39.6% residual ativity
N-bromosuccinimide
almost complete inhibition at 5 mM
N-bromosuccinimide
-
1 mM, 59% residual activity
N-bromosuccinimide
Pomacea insularus
-
-
N-bromosuccinimide
-
complete inhibition of PhX33 and PhX20 at 1 mM
N-bromosuccinimide
-
5 mM
N-bromosuccinimide
-
strong inhibition
N-bromosuccinimide
-
5 mM, 82% inhibition
N-bromosuccinimide
-
low inhibition
Na+
-
about 70% residual activity at 20 mM
Na+
-
strongly inhibits 33.2% of xylanase activity
Na+
-
retains 33% activity at 4 M Na+
Na+
-
92.1% residual activity at 2 mM
Na+
-
10 mM reduces the enzyme activity by 9.8%
Na+
5 mM, 1.3fold activation of activity with carboxymethyl cellulose, 6% inhibition of xylanase activity, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
NaCl
-
-
NaCl
-
1 mM, isoform xyl I, 28% inhibition, xyl II, 19% inhibition
NaCl
5 M, 86% residual activity
NEM
-
-
NEM
-
xylanase A, B and C
NEM
49% inhibition at 5 mM
NH4Cl
-
2 mM, 87% residual activity
NH4Cl
-
activates xylanase I, inhibits xylanase II
Ni2+
-
about 60% residual activity at 20 mM
Ni2+
about 95% residual activity at 1 mM
Ni2+
-
complete inhibition at 10 mM
Ni2+
-
5 mM, complete inhibition
Ni2+
-
10 mM, 49% inhibition
Ni2+
2 mM, 28% residual activity; 2 mM, 63% residual activity; 2 mM, 78% residual activity
Ni2+
1 mM, 51% residual activity
Ni2+
10% inhibition at 5-10 mM
Ni2+
strong inhibition of XYN10G at 1 mM
Ni2+
10 mM, 44 % loss of activity
Ni2+
6% inhibition at 1 mM
Ni2+
48% inhibition at 2 mM
Ni2+
10 mM partially inhibits the activity of XynAS27
Ni2+
-
1 mM, 77% resiudal activity
Ni2+
-
5 mM, 58% residual activity
p-chloromercuribenzoate
-
isozymes A and B
p-chloromercuribenzoate
-
at 50 mM 50% inhibition of PhX20, 40% inhibition of PhX33
Pb(CH3COO)2
-
-
Pb(CH3COO)2
-
activates xylanase II and inhibits xylanase I at 10 mM
Pb(CH3COO)2
-
2 mM, activity is reduced by 25%
Pb(NO3)2
-
-
Pb(NO3)2
-
1 mM, 43% inhibition of xylanase 2, no inhibition of xylanase 1
Pb2+
-
Pb2+
-
1 mM, 60% inhibition of xylanase A
Pb2+
Halalkalibacterium halodurans
strong inhibition
Pb2+
2 mM, 18% residual activity; 2 mM, 46% residual activity; 2 mM, no residual activity
Pb2+
-
78.93% residual activity at 2 mM
Pb2+
42% inhibition at 10 mM
Pb2+
-
2 mM, 70% residual activity for isoforms xynA, xynC, 80% residual activity for isoform xynB
Pb2+
65% inhibition at 2 mM
Pb2+
-
10 mM reduces the enzyme activity by 32.9%
Pb2+
10 mM partially inhibits the activity of XynAS27
Pb2+
10 mM partialy inhibits
Pb2+
18% inhibition at 10mM
Pb2+
-
2 mM, 25% loss of activity
Pb2+
-
8 mM, 26% loss ofv activity
Pb2+
-
8 mM, 74% residual activity. Addition of 40 mM EDTA does not recover any lost activity
PCMB
-
20 mM, complete inhibition
PCMB
Pomacea insularus
-
-
PCMB
-
1 mM, complete inhibition, xylanase A
PHMB
-
protection by xylan
PHMB
-
1 mM, 77% inhibition
PMSF
-
10 mM, 53% inhibition
PMSF
-
inhibits the native enzyme
PMSF
-
activates xylanase I, inhibits xylanase II
SDS
-
-
SDS
20% inhibition at 0.5%; about 78% residual activity at 0.5% (w/v)
SDS
more than 50% inhibition
SDS
-
10 mM, 70% inhibition
SDS
complete inhibition at 5 mM
SDS
-
1% w/w, 86% loss of activity
SDS
1 mM, no residual activity
SDS
-
inhibition of isozyme IIb
SDS
-
37.46% residual activity at 2 mM
SDS
-
strong inhibition of xylanase I and xylanase II, complete inhibition at 2 mM and 10 mM, respectively
SDS
54% inhibition at 1 mM, 92% at 10 mM
SDS
complete inhibition of XYN10G at 5 mM
SDS
2%, 60% loss of activity
SDS
55% inhibition at 0.25% w/v
SDS
strongly inhibits by 94.4%
SDS
5 mM, 51% residual activity
SDS
-
10 mM reduces the enzyme activity by 59.2%
SDS
almost completely inhibits
SDS
84% inhibition at 5 mM, complete at 10mM
SDS
-
1%, no residual activity
Sn2+
Halalkalibacterium halodurans
strong inhibition
Sodium azide
-
-
Sodium azide
43% inhibition at 5 mM
sodium dodecylsulfate
-
strong, both xylanase I and xylanase II
sodium dodecylsulfate
10 mM, 72% residual activity
sodium dodecylsulfate
-
2 mM, 22% residual activity
sodium dodecylsulfate
0.5%, about 40% residual activity
sodium dodecylsulfate
-
1 mM, 95% residual activity
sodium dodecylsulfate
0.1%, 82% residual activity
TAXI-I
-
-
TAXI-I
endoxylanase inhibitor protein I, strong, competitive
-
TLXI
-
-
Triticum aestivum xylanase inhibitor
-
-
-
Triticum aestivum xylanase inhibitor
inhibits only microbial endoxylanases
-
Triticum aestivum xylanase inhibitor
inhibits only microbial endoxylanases. Microbial enzymes present in wheat flour are hardly active due to rapid inhibition by enzyme inhibitors present in wheat flour
-
Triticum aestivum xylanase inhibitor
TAXI, 44-50% inhibition of the wild-type enzyme, nearly no inhibition of enzyme mutant D11F/R122D
-
Triticum aestivum xylanase inhibitor
-
-
-
Triticum aestivum xylanase inhibitor
-
TAXI
-
Triticum aestivum xylanase inhibitor-I
-
-
Triticum aestivum xylanase inhibitor-I
-
-
-
Triticum aestivum xylanase inhibitor-I
-
-
Triticum aestivum xylanase inhibitor-I
-
-
Triton X-100
-
Triton X-100
1%, 88% of initial activity
Urea
-
-
Urea
80% inhibition at 0.5 M
XIP-I
-
xylanase inhibitor protein
-
XIP-I
-
a wheat xylanase inhibitor, that inhibits only XynB mutant DELTAP130/K131S/K132S, but not mutant K131S/K132S and the wild-type XynB
-
XIP-I
xylanase inhibitor protein I, strong, competitive
-
xylanase inhibiting protein
inhibits only fungal endoxylanases
-
xylanase inhibiting protein
inhibits only fungal endoxylanases. Microbial enzymes present in wheat flour are hardly active due to rapid inhibition by enzyme inhibitors present in wheat flour
-
xylanase inhibitor protein
-
-
-
xylanase inhibitor protein
-
-
-
xylanase inhibitor protein-I
-
-
xylanase inhibitor protein-I
-
-
xylanase inhibitor protein-I
-
-
xylanase inhibitor protein-I
-
-
xylobiose
-
acts as the end product inhibitor of Xyn11A
xylose
-
no inhibition
xylose
40 mM, 81% residual activity
Zn2+
-
Zn2+
-
1 mM, isoform xyl I, 70% inhibition, xyl II, 10% inhibition
Zn2+
16% inhibition at 1 mM
Zn2+
-
81% inhibition at 10 mM
Zn2+
-
10 mM, 40% inhibition
Zn2+
-
2 mM, 56% residual activity
Zn2+
inhibits activity from 10 mM (7%) to 20 mM (21%)
Zn2+
completely inhibits hydrolysis activity
Zn2+
-
5 mM, complete inhibition
Zn2+
-
10 mM, 49% inhibition
Zn2+
-
in the presence of 10 mM, the relative xylanase activity decreases by 9.2%
Zn2+
2 mM, 39% residual activity; 2 mM, 57% residual activity; 2 mM, 5% residual activity
Zn2+
-
91.11% residual activity at 2 mM
Zn2+
-
slight inhibition at 3 or 6 mM
Zn2+
-
inhibition of xylanase I and xylanase II
Zn2+
14% inhibition at 1 mM
Zn2+
51% inhibition at 2 mM
Zn2+
-
1 mM, 2.3% residual activity
Zn2+
-
5 mM, 52% residual activtiy
Zn2+
10 mM partially inhibits the activity of XynAS27
Zn2+
-
5 mM, 74% residual activity
Zn2+
-
10 mM, significant inhibition
Zn2+
Thermochaetoides thermophila
17.1% inhibition at 1 mM, 55.2% at 5 mM; 5 mM, 4.4% loss of activity, substrate: carboxymethyl cellulose; 5 mM, 55% loss of activity, substrate: xylan
Zn2+
-
1 mM ZnCl2, patial inhibition, xylanase A
Zn2+
1 mM, 21% inhibition
Zn2+
10 mM, activity decreased to 15%
additional information
no inhibition by 1-10 mM EDTA
-
additional information
-
K+, Li+, Fe2+, Cu2+, and Zn2+ have no significant effect on activity. Slight decrease in xylanase production for both oat spelt xylan medium and wheat bran medium when prolonging the cultivation time
-
additional information
cellulose-binding domain decreases the recombinant EGXA's specific activities on p-nitrophenyl-beta-D-cellobioside and sodium carboxymethyl cellulose
-
additional information
-
cellulose-binding domain decreases the recombinant EGXA's specific activities on p-nitrophenyl-beta-D-cellobioside and sodium carboxymethyl cellulose
-
additional information
the enzyme displays an excellent tolerance to trypsin and pepsin proteases but is degraded by proteinase K, and slightly by alkaline protease
-
additional information
-
the enzyme displays an excellent tolerance to trypsin and pepsin proteases but is degraded by proteinase K, and slightly by alkaline protease
-
additional information
poor inhibition by DTT and EDTA. Various proteases have poor effects on the xylanase AfXynA, overview
-
additional information
-
poor inhibition by DTT and EDTA. Various proteases have poor effects on the xylanase AfXynA, overview
-
additional information
-
Ce2+, Li2+, NH4+ and Mg2+ have no significant effect on xylanase activity at 10 mM
-
additional information
addition of 1% D-glucose to media supplemented with xylan, xylose or beta-methylxyloside represses xylanase production. Glucose repression is alleviated by addition of cAMP or dibutyryl-cAMP
-
additional information
-
no significant loss of activity is detected up to 2 M NaCl
-
additional information
hydrolytic activity almost entirely inhibits at acidic pH
-
additional information
XYLD shows resistant to pepsin and part resistant to trypsin
-
additional information
poor inhibition by Ni2+ and Co2+
-
additional information
no inhibition by EDTA and DTT
-
additional information
-
1 mM dithiothreitol has no effect on the enzyme activity
-
additional information
not inhibitory: Mg2+, Mn2+
-
additional information
-
activity is not affected by L-cysteine and 1,1-dithioerythreitol
-
additional information
-
not inhibitory: XIP-I; not inhibitory: xylanase inhibitor protein XIP-I
-
additional information
not inhibitory: XIP-I; not inhibitory: xylanase inhibitor protein XIP-I
-
additional information
-
insensitive to Triticum aestivum xylanase inhibitor (TAXI) and xylanase inhibitor protein (XIP)
-
additional information
Halalkalibacterium halodurans
-
not inhibited by Fe2+, Sn2+, Ni2+, and Na+
-
additional information
no inhibition by xylose; no inhibition by xylose
-
additional information
no inhibition by xylose; no inhibition by xylose
-
additional information
-
no inhibition by xylose; no inhibition by xylose
-
additional information
Kxyn is not affected by 2-mercaptoethanol, DTT, or SDS
-
additional information
stimulation or inhibition by 1 mM of Ca2+,Ni2+, Zn2+, Mg2+, Mn2+, Sn2+, Ba2+, Co2+, and Fe2+ is marginal
-
additional information
not inhibitory at 1 mM: iodoacetate, N-ethylmaleimide, o-phenanthroline, EDTA, EGTA, dithiothreitol, 2-mercaptoethanol, 1-ethyl-3-dimethyl aminopropylcarbadimide, N-bromosuccinimide, phenylmethansulfonylfluoride, 4-chloromercuribenzoate, SDS, Tween 80, and Triton X-100. Not inhibitory: Ca2+, Sr2+, Co2+, Mg2+, Pb2+, Ni2+, Mn2+, Fe2+, Sn2+, Zn2+, and Fe3+
-
additional information
-
not inhibitory at 1 mM: iodoacetate, N-ethylmaleimide, o-phenanthroline, EDTA, EGTA, dithiothreitol, 2-mercaptoethanol, 1-ethyl-3-dimethyl aminopropylcarbadimide, N-bromosuccinimide, phenylmethansulfonylfluoride, 4-chloromercuribenzoate, SDS, Tween 80, and Triton X-100. Not inhibitory: Ca2+, Sr2+, Co2+, Mg2+, Pb2+, Ni2+, Mn2+, Fe2+, Sn2+, Zn2+, and Fe3+
-
additional information
not inhibited by XIP-I
-
additional information
-
not inhibited by XIP-I
-
additional information
the enzyme is not affected by 1 mM of EDTA, 2-mercaptoethanol, and PMSF
-
additional information
-
the enzyme is not affected by 1 mM of EDTA, 2-mercaptoethanol, and PMSF
-
additional information
not inhibitory: Fe2+, Cu2+, Mg2+, Ni2+
-
additional information
-
not inhibitory: Fe2+, Cu2+, Mg2+, Ni2+
-
additional information
-
EDTA, Ca2+ and Ni2+ do not show any effect on xylanase activity
-
additional information
-
XynA is insensitive towards protein XIP-I
-
additional information
no or poor inhibition by Na+, Li+, K+, Mg2+, and Ca2+
-
additional information
after treatment with pepsin and trypsin at 37°C for 1 h, XYN10G retains 64.7% and 100% activity, respectively
-
additional information
-
not affected by urea, iodoacetamide, Fe3+, K+, Na+, p-chloromercuribenzoate and N-ethylmaleimide
-
additional information
-
no or poor inhibition of PhX33 and PhX20 by N-ethylmaleimide, iodoacetate, 2,3-butanedione, and N-acetylimidazole
-
additional information
modular endoxylanase containing a xylan-binding domain, which after processing in the culture supernatant loses the afore mentioned domain and thus its capacity to bind xylan. Sharp decrease (up to 50%) in activity after 15 min of incubation at 70 or 80°C
-
additional information
-
modular endoxylanase containing a xylan-binding domain, which after processing in the culture supernatant loses the afore mentioned domain and thus its capacity to bind xylan. Sharp decrease (up to 50%) in activity after 15 min of incubation at 70 or 80°C
-
additional information
not inhibitory: EDTA, Ca2+, Na+, Ni2+, and Mg2+
-
additional information
shows resistance to neutral and alkaline proteases, enzyme activity is unchanged after incubation for 2 h with trypsin, chymotrypsin, collagenase, subtilisin A, proteinase K, and proleather, and retains over 60% of its activity following treatment with high concentrations of an alkaline protease from Bacillus pumilus
-
additional information
-
shows resistance to neutral and alkaline proteases, enzyme activity is unchanged after incubation for 2 h with trypsin, chymotrypsin, collagenase, subtilisin A, proteinase K, and proleather, and retains over 60% of its activity following treatment with high concentrations of an alkaline protease from Bacillus pumilus
-
additional information
not inhibitory: EDTA
-
additional information
-
EDTA, Ni2+, Zn2+ and Mg2+ have no effect on activity
-
additional information
Na+, Ca2+, Ni2+, Mg2+, Fe3+, Zn2+, Li+, EDTA and sodium dodecyl sulfate have no effect
-
additional information
no or poor inhibition by Ni2+, Cr3+, Mg2+, Li+, Fe3+, K+, Na+, Ca2+, and EDTA
-
additional information
not inhibitory: endoxylanase inhibitor protein TAXI-II
-
additional information
-
not inhibitory: endoxylanase inhibitor protein TAXI-II
-
additional information
-
CuSO4, NaN3, MgSO4, and iodoacetic acid do not show any inhibitory effect
-
additional information
-
the xylanase was not affected by copper sulfate, zinc sulfate, calcium chloride, cobalt chloride, barium chloride, magnesium sulfate, and EDTA at concentrations of 2 mM
-
additional information
Thermochaetoides thermophila
removal of fusion protein rather decreases activity
-
additional information
-
native XynA loses 80% activity after 90 min at 80°C and 70% activity at pH 10
-
additional information
the enzyme activity is not affected by EDTA; the enzyme activity is not affected by EDTA
-
additional information
the enzyme activity is not affected by EDTA; the enzyme activity is not affected by EDTA
-
additional information
the enzyme shows maximum activity even in the presence of di/trivalent metal cations Ca2+, Cd2+, Pb2+, Mg2+, Ni2+ and Fe3+
-
additional information
-
wheat kernels contain endogenous endoxylanase inhibitors that interfere with enzyme activity and differ between the wheat varieties
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.087
-
crude extract, using birchwood xylan in 100 mM sodium acetate buffer pH 5.0 as the substrate
0.1
-
with celobiose as inducer
0.11
-
with avicel as inducer
0.12
-
with CMC as inducer
0.35
-
with glucose as inducer
0.5
-
substrate: xylan, pH 5.0, 50°C
0.52
substrate rye arabinoxylan xylan, wild-type, pH 6.0, 50°C
0.58
-
with xylose as inducer
0.65
-
substrate 4-nitrophenyl beta-D-xylopyranose, pH 7.0, 50°C
0.67
substrate oat spelt xylan, wild-type, pH 6.0, 50°C
0.87
substrate rye arabinoxylan xylan, fusion protein with XylZ CBM domain, pH 6.0, 50°C
0.88
substrate oat spelt xylan, fusion protein with XylZ CBM domain, pH 6.0, 50°C
0.9
recombinant EGXA with p-nitrophenyl beta-D-cellobioside as substrate
1.1
-
crude extract, using oat spelt xylan as a substrate, at pH 7.0, at 80°C
1.2
-
substrate: xylan, pH 5.0, 70°C
1.4
-
substrate: xylan, pH 5.0, 50°C
1.9
-
substrate: xylan, pH 5.0, 70°C
1001
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Arthrinium sp. aff. sacchari, GenBank Accession: HQ630961
1014
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Gibberella sp. aff. moniliformis, Genbank Accession: HQ630966
102
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
1022
-
substrate oat spelt xylan, purified recombinant enzyme
1028
substrate beechwood xylan, pH 6.5, 50°C
1037
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
1081
truncated variant XynAGN16L, substrate birchwood xylan, pH 6.5, 37°C
1085
-
mutant R7T, at 30°C, with wheat arabinoxylan as substrate
1088
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
1099
-
substrate beechwood xylan, purified recombinant enzyme
11.4
-
after 10.4fold purification, using oat spelt xylan as a substrate, at pH 7.0, at 80°C
11.68
-
isozyme IIb, substrate oat spelt xylan
1100
-
wild-type, at 30°C, with wheat arabinoxylan as substrate
1109
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
112.1
-
purified isozyme I
1122
-
37°C, pH 5.0, release of xylose from xylan, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Hypocrea sp. aff. lixii, GenBank Accession: HQ630960
1146
-
mutant DELTAD130, at 30°C, with wheat arabinoxylan as substrate
115.9
purified recombinant enzyme, substrate high viscosity arabinoxylan, pH 5.0, 70°C
1177
truncated variant XynAGN16Lpd, substrate birchwood xylan, pH 6.5, 37°C
12
-
substrate carboxymethylcellulose, purified recombinant enzyme
12.5
wild-type EGX with sodium carboxymethyl cellulose as substrate
12.7
purified recombinant His-tagged enzyme, pH 6.0, 40°C, substrate insoluble wheat arabinoxylan
1226
-
mutant F14Y, at 30°C, with wheat arabinoxylan as substrate
123
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
1232
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
1234
truncated variant XynAGN16L, substrate beechwood xylan, pH 6.5, 37°C
1242
truncated variant XynAGN16L, substrate oat spelt xylan, pH 6.5, 37°C
125
Thermochaetoides thermophila
purified enterokinase-digested endoxylanase
1257
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
1260
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
1266
truncated variant XynAGN16Lpd, substrate beechwood xylan, pH 6.5, 37°C
1284
-
wild-type, pH 5, 65°C
13
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
13.3
native enzyme, pH 6.0, 37°C
130.4
-
purified enzyme toward oat spelt xylan
134
-
substrate insoluble birchwood xylan, pH 6.0, temperature not specified in the publication
1342
-
purified recombinant wild-type AnxB
1352
substrate beechwood xylan, pH 6.5, 65°C
1363
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
1382
-
37°C, pH 5.0, release of xylose from xylan, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Hypocrea sp. aff. lixii, GenBank Accession: HQ630960
1386
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
14.9
substrate oat spelt xylan, pH 6.0, 50°C
140
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
1411
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Trichoderma sp. aff. atroviride, GenBank Accession: HQ630969
1412.5
purified recombinant enzyme, pH 7.0, 60°C
142
LC132960
mutant Q286A/N340Y, substrate soluble oat spelt xylan, pH 6.0, 50°C
142.7
-
isozyme Ic, substrate oat spelt xylan
1429
recombinant enzyme, substrate oat spelt xylan
143
LC132960
wild-type, substrate soluble oat spelt xylan, pH 6.0, 50°C
1436
-
purified native enzyme
1459
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
1460
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
1462
-
37°C, pH 5.0, release of xylose from xylan, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Hypocrea sp. aff. lixii, GenBank Accession: HQ630960
1464
-
mutant Q121R, at 30°C, with wheat arabinoxylan as substrate
1478
substrate oat spelt xylan, pH 6.5, 50°C
1484
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Gibberella sp. aff. avenacea, Genbank Accession: HQ630977
1486
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
1487
-
substrate soluble birchwood xylan, pH 6.0, temperature not specified in the publication
1489
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
15
substrate azurine cross-linked arabinoxylan xylan, pH 5, 50°C
15.4
substrate insoluble oat spelt xylan, pH 7.0, 60°C
150
substrate beechwood xylan, pH 4.0, 50°C
152
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
1533.7
purified recombinant enzyme, pH 6.0, 60°C
1536
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
15501
-
wild-type, pH 6.0, 50°C
1597
-
37°C, pH 5.0, release of xylose from xylan, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Hypocrea sp. aff. lixii, GenBank Accession: HQ630960
16.4
recombinant enzyme, culture supernatant
1620
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
163.1
-
substrate: 2-nitrophenyl xylopyranoside, pH 5, 50°C, xylanase II
1660
-
purified wild-type enzyme
175
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Gibberella sp. aff. moniliformis, Genbank Accession: HQ630966
1756
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
17778
-
mutant M7, pH 6.0, 50°C
1783
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
1785
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Arthrinium sp. aff. sacchari, GenBank Accession: HQ630961
18.7
purified recombinant His-tagged enzyme, pH 6.0, 40°C, substrate insoluble rye arabinoxylan
1833
purified recombinant enzyme, pH 6.0, 70°C, substrate beechwood xylan
1869
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
18830
purified recombinant Xyl10C
19.2
substrate birchwood xylan, pH 6.0, 50°C
19.6
LC132960
wild-type, substrate insoluble oat spelt xylan, pH 6.0, 50°C
19.8
Halalkalibacterium halodurans
-
after 7.9fold purification, in 50 mM sodium phosphate buffer, pH 7.0, at 70°C
1902
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
1914
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Hypocrea sp. aff. koningii, GenBank Accession: HQ630959
192
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
1920
substrate birchwood xylan, pH 6.5, 65°C
196.9
purified recombinant enzyme
197.75
MK331807
substrate: beech wood xylan, pH 6.5, 75°C
1983
toward oat spelt xylan
2.1
substrate 4-nitrophenyl beta-D-cellobioside, pH 6.0, 50°C
2.5
Halalkalibacterium halodurans
-
crude enzyme, in 50 mM sodium phosphate buffer, pH 7.0
2.56
-
substrate birchwood xylan, pH 7.0, 50°C
2.58
substrate beechwood xylan, wild-type, pH 6.0, 50°C
2.86
substrate birchwood xylan, pH 7.0, 50°C
2.9
-
substrate: 4-nitrophenyl xylopyranoside, pH 5, 50°C, xylanase II
20.34
-
with birchwood xylan as substrate
200
-
isoform xylanase IIIA, pH 5.6, 50°C
2020
recombinant enzyme, substrate 4-O-methyl-D-glucuronoxylan
2051
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Arthrinium sp. aff. sacchari, GenBank Accession: HQ630961
207.2
purified recombinant XYN10G5, substrate oat spelt xylan, pH 4.0, 70°C
21.2
substrate beechwood xylan, pH 6.0, 50°C
2117
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
214
Halalkalibacterium halodurans
-
pH 11, 70°C
2144
recombinant enzyme, substrate birchwood xylan
2174
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
22
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
22.3
purified recombinant His-tagged enzyme, pH 6.0, 40°C, substrate soluble wheat arabinoxylan
2202
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
23
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
2304
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Hypocrea sp. aff. koningii, GenBank Accession: HQ630959
2317
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
2360
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
2361
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Arthrinium sp. aff. sacchari, GenBank Accession: HQ630961
2392
purified recombinant enzyme, pH 7.0, 60°C
24
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
240.9
-
purified isozyme xylanase II
2463
recombinant enzyme, substrate beechwood xylan
249.1
-
purified isozyme xylanase I
25.6
-
at pH 7.5 and 85°C
254
substrate oat spelt xylan, wild-type, pH 6.0, 65°C
2560
-
substrate beechwood xylan, pH 9.0, 60°C
2573
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
2592
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
2595
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
26.6
substrate insoluble wheat arabinoxylan xylan, pH 7.0, 60°C
2600
pH 6.0, 95°C, substrate, birchwood xylan
2621
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
264
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Trichoderma sp. aff. spirale, GenBank Accession: HQ630962
2643
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
2665
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Trichoderma sp. aff. atroviride, GenBank Accession: HQ630969
2740
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
275
wild-type EGX with xylan as substrate
277
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
280
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Gibberella sp. aff. avenacea, Genbank Accession: HQ630977
287.5
-
substrate: 4-nitrophenyl-4-O-beta-D-xylopyranosyl-beta-D-xylopyranose, pH 5, 50°C, xylanase II
2873
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
2895
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Trichoderma sp. aff. atroviride, GenBank Accession: HQ630969
2906
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
2974
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Trichoderma sp. aff. atroviride, GenBank Accession: HQ630969
2995
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
2997
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
3 - 3.9
purified recombinant enzyme, pH 5.0, 70°C
3.03
substrate beechwood xylan, fusion protein with XylZ CBM domain, pH 6.0, 50°C
3.05
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, pH 5.0, 55°C, substrate beta-xylan
3.13
-
with lactose as inducer
3.33
-
isozyme IIa, substrate oat spelt xylan
3.5
-
substrate: xylan, pH 5.0, 70°C
3.7
purified recombinant enzyme, substrate oat spelt xylan
3.91
-
isozyme IId, substrate oat spelt xylan
30.75
-
purified isozyme XA-1
300
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
304.2
6.7fold purified enzyme
3085
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
31
-
substrate birchwood xylan, pH 6.0, 70°C
310
-
partially purified enzyme
312
-
purified enzyme, pH 8.0, 40°C, substrate birchwood xylan
3126
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
315
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Fusarium sp. aff. proliferatum, GenBank Accession: HQ630965
316
substrate arabinoxylan, pH 5.0, 40°C
318.45
-
purified native enzyme, pH 7.0, 40°C
3197
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
32
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
322
-
purified wild-type enzyme
3236
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
325
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
3264
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
3270
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
34
-
substrate beechwood glucuronoxylan, pH 6.0, 70°C
342
Halalkalibacterium halodurans
-
after purification
35.44
-
purified mutant enzyme S100C/N150C
350
wild-type, pH 3.8, 45°C
350.6
purified recombinant XYN10G5, substrate soluble wheat arabinoxylan, pH 4.0, 70°C
3525
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Arthrinium sp. aff. phaeospermum, GenBank Accession: HQ630967
358
-
purified enzyme, substrate oat spelt xylan, pH 3.0, 45°C
36.58
-
isozyme Ib, substrate oat spelt xylan
360
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
360.7
-
after 14.2fold purification
37.22
-
after 427.83fold purification, using birchwood xylan in 100 mM sodium acetate buffer pH 5.0 as the substrate
373
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Trichoderma sp. aff. spirale, GenBank Accession: HQ630962
375
Halalkalibacterium halodurans
substrate birchwood xylan, pH 9.0, 80°C
38.1
Thermochaetoides thermophila
untreated endoxylanase
383.4
purified native extracellular enzyme, pH 7.5, 55°C, substrate beechwood xylan
3869
-
60°C, pH not specified in the publication
39
purified mutant XynC-C
390
purified mutant XynZ-C
391.8
recombinant EGXA with xylan as substrate
397
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Hypocrea sp. aff. koningii, GenBank Accession: HQ630959
3991
wild-type, pH 5.0, 50°C
4.5
-
substrate: xylan, pH 5.0, 70°C
40
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
40.3
wild-type EGX with p-nitrophenyl beta-D-cellobioside as substrate
40.58
-
purified wild type enzyme
4027
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
403
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Trichoderma sp. aff. spirale, GenBank Accession: HQ630962
41
substrate birchwood xylan, pH 6.5, 80°C
41.2
substrate beechwood xylan, pH 7.0, 60°C
41.8
substrate beechwood xylan, pH 6.5, 65°C
414
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Gibberella sp. aff. avenacea, Genbank Accession: HQ630977
427
-
purified recombinant wild-type SlxB
43
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Exophiala sp. aff. spinifera, GenBank Accession: HQ631027
438
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
44
-
isoform xylanase IA, pH 6.6, 50°C
441
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Fusarium sp. aff. proliferatum, GenBank Accession: HQ630965
453.7
7.1fold purified enzyme
454
substrate birchwood xylan, pH 6.5, 65°C
455
Thermomonospora sp.
-
purified enzyme
4659
mutant S35C/N44H/Y61M/T62C/N63L/D65P/N66G/T101P/S102N, pH 5.0, 50°C
47
purified recombinant His-tagged enzyme, pH 6.0, 40°C, substrate 4-O methyl-glucuronoxylan
47.6
recombinant enzyme from concentrated cell culture supernatant, pH 7.0, 60°C
475.1
-
purified native enzyme, beechwood xylan
4780
-
purified isozyme B
48.74
-
isozyme Ia, substrate oat spelt xylan
49.3
LC132960
mutant Q286A/N340Y, substrate insoluble oat spelt xylan, pH 6.0, 50°C
49.99
-
purified isozyme XA-2
493
-
mutant S44D, at 30°C, with wheat arabinoxylan as substrate
497.2
-
purified native enzyme, birchwood xylan
5.45
-
crude culture, in 50 mM sodium acetate buffer (pH 4.5) at 30°C
5.5
-
substrate: xylan, pH 5.0, 50°C
50.4
purified recombinant enzyme, substrate birchwood xylan, pH 5.0, 70°C
509
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Fusarium sp. aff. proliferatum, GenBank Accession: HQ630965
512
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Fusarium sp. aff. proliferatum, GenBank Accession: HQ630965
516
recombinant protein with His-tag, pH 8.0, 80°C
52
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Exophiala sp. aff. spinifera, GenBank Accession: HQ631027
529.9
-
purified native enzyme, oat spelt xylan
53
substrate wheat arabinoxylan xylan, pH 9.0, 60°C
539
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
55.1
substrate soluble oat spelt xylan, pH 7.0, 60°C
550
-
mutant N257D, pH 5.5, 70°C
557
recombinant wild-type protein, pH 8.0, 80°C
558
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
566
-
purified extracellular enzyme
57.1
purified recombinant His-tagged enzyme, pH 6.0, 40°C, substrate xylan with MW of 20000-30000
57.9
purified recombinant enzyme, substrate oat-spelt xylan
5700
-
purified Xyl1, substrate birchwood xylan, at 50°C
576
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Fusarium sp. aff. aethiopicum, GenBank Accession: HQ630964
5768
substrate beechwood xylan, pH 5.0, 40°C
582
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Gibberella sp. aff. moniliformis, Genbank Accession: HQ630966
585
mutant T64S, presence of Al3+, pH 3.8, 45°C
59.6
-
recombinant XynBE18, substrate oat spelt xylan
59.7
purified recombinant His-tagged enzyme, pH 6.0, 40°C, substrate beechwood xylan
6.31
-
isozyme IIc, substrate oat spelt xylan
60
substrate birch wood xylan, pH 4.0, 50°C
601.32
MK331807
substrate: wheat arabinoxylan, pH 6.5, 75°C
603
mutant T64S, presence of Ca2+, pH 3.8, 45°C
61.57
-
recombinant XynBE18, substrate birchwood xylan
626
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
627
-
mutant S129G/DELTAD130, at 30°C, with wheat arabinoxylan as substrate
629
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Gibberella sp. aff. avenacea, Genbank Accession: HQ630977
63.5
substrate birchwood xylan, pH 7.0, 60°C
64
-
substrate gellan gum, purified recombinant enzyme
660
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
667
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Fusarium sp. aff. aethiopicum, GenBank Accession: HQ630964
67
substrate soluble wheat arabinoxylan xylan, pH 7.0, 60°C
6820
-
purified isozyme A
6853
substrate birchwood xylan, pH 5.0, 50°C
687
mutant T64S, presence of dithiothreitol, pH 3.8, 45°C
689
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
69
-
37°C, pH 5.0, release of xylose from xylan, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
69.6
38.7fold purified enzyme
695.2
purified recombinant deglycosylated extracellular enzyme, pH 5.0, 55°C, substrate birchwood xylan
70.3
purified enzyme, substrate is xylan from birchwood
706.1
purified recombinant XynA
707
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
72.6
substrate oat spelt xylan, pH 4.0, 50°C
720
-
X-I after 77.4fold purification, at 60°C and pH 6.0
723
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
728
purified extracellular recombinant enzyme, pH 6.0, 50°C, substrate rye arabinoxylan
73
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
738
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
755
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Hypocrea sp. aff. koningii, GenBank Accession: HQ630959
763
-
mutant Q158R, pH 4.5, 65°C
764
-
mutant S129G, at 30°C, with wheat arabinoxylan as substrate
769
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
77.4
recombinant enzyme, pH 6.0, 37°C
774
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
79
purified mutant XynZ-BDC
796
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
7988
purified recombinant enzyme
799
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks, Fusarium sp. aff. aethiopicum, GenBank Accession: HQ630964
8
purified recombinant His-tagged enzyme, pH 6.0, 40°C, substrate oat spelt xylan
801
-
purified recombinant wild-type SoxB
805
lichenin as substrate, pH 7.0, 65°C
819
truncated variant XynAGN16Lpd, substrate oat spelt xylan, pH 6.5, 37°C
838.2
purified native extracellular enzyme XynA, pH 7.5, 55°C, substrate beechwood xylan
844
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
86.1
-
purified isozyme II
861
-
substrate oat spelt xylan, pH 9.0, 60°C
866
-
mutant S129G/S44N, at 30°C, with wheat arabinoxylan as substrate
867
-
substrate birchwood xylan, purified recombinant enzyme
87
-
purified native enzyme, pH 7.0, 60°C, substrate birchwood xylan
878
substrate birchwood xylan, pH 6.5, 50°C
879
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Fusarium sp. aff. aethiopicum, GenBank Accession: HQ630964
893.6
-
after 2.25fold purification, at 60°C, in 0.2 M glycine-NaOH buffer, pH 9.0
9
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Exophiala sp. aff. spinifera, GenBank Accession: HQ631027
9.3
-
supernatant, at 60°C and pH 6.0
9.4
Halalkalibacterium halodurans
-
after 3.8fold purification, in 50 mM sodium phosphate buffer, pH 7.0, at 60°C
90.38
-
after purification, in 50 mM sodium acetate buffer (pH 4.5) at 30°C
908
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
92.6
-
substrate: 2-nitrophenyl xylopyranoside, pH 5, 50°C, xylanase III
938
barley glucan as substrate, pH 7.0, 65°C
95
-
mutant S129G/S44D, at 30°C, with wheat arabinoxylan as substrate
954
-
mutant S44N, at 30°C, with wheat arabinoxylan as substrate
97
substrate oat spelt xylan, pH 9.0, 60°C
97.6
139.4fold purifed enzyme
973
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Gibberella sp. aff. moniliformis, Genbank Accession: HQ630966
984
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
992
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
0.2
substrate 4-nitrophenyl beta-D-xylopyranoside, pH 6.0, 50°C
0.2
-
substrate: 4-nitrophenyl xylopyranoside, pH 5, 50°C, xylanase III
0.2
-
substrate: xylan, pH 5.0, 50°C
0.4
-
substrate: 4-nitrophenyl-4-O-beta-D-xylopyranosyl-beta-D-xylopyranose, pH 5, 50°C, xylanase III
0.4
-
substrate: xylan, pH 5.0, 50°C
1.46
-
substrate oat spelt xylan, pH 7.0, 50°C
1.46
substrate oat spelt xylan, pH 7.0, 50°C
141
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
16
-
crude extract
16
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
164
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Exophiala sp. aff. spinifera, GenBank Accession: HQ631027
164
-
substrate lichenan, purified recombinant enzyme
17
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
17
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
1849
-
pH 5.0, 50°C
1849
-
purified enzyme, substrate birch wood xylan, pH 5.0, 75°C
1849
-
mutant H209N, pH 5.0, 65°C
19
substrate azo-xylan pH 5, 50°C
19
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
20
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks
20
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
2350
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
2350
B2CNY5
purified recombinant enzyme
25.4
-
from crude cell extract
25.4
purified recombinant His-tagged enzyme, pH 6.0, 40°C, substrate soluble rye arabinoxylan
2500
-
purified mutant enzyme
2500
-
pH not specified in the publication, temperature not specified in the publication
259
pH 6, 50°C
259
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Trichoderma sp. aff. spirale, GenBank Accession: HQ630962
264.1
purified recombinant enzyme, pH 7.0, 65°C
264.1
xylan as substrate, pH 7.0, 65°C
27
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
27
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
3 - 8
purified mutant XynC-BC
3 - 8
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Exophiala sp. aff. salmonis, GenBank Accession: HQ630990
30
-
substrate 4-O-methyl-beta-D-glucuronoxylan, pH 6.0, 70°C
30
-
substrate laminarin, purified recombinant enzyme
32.6
pH 6.0, 40°C
32.6
Thermochaetoides thermophila
enterokinase-digested endoxylanase
33
30°C, pH 6.8
33
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week, Fusarium sp. aff. equiseti, GenBank Accession: HQ630976
367
-
X-II after 40fold purification, at 60°C and pH 6.0
367
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
37.3
-
-
37.3
purified recombinant His-tagged enzyme, pH 6.0, 40°C, substrate birchwood xylan
4
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
4
-
substrate: xylan, pH 5.0, 70°C
407
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 4 weeks, Phoma sp. aff. herbarum, GenBank Accession: HQ630963
45
-
37°C, pH 5.0, release of xylose from xylan, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 2 weeks
45
-
mutant S44A, at 30°C, with wheat arabinoxylan as substrate
55
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 1 week
55
substrate beechwood xylan, pH 6.5, 80°C
5890
-
wild type enzyme, at pH 7.0
7.5
recombinant EGXA with sodium carboxymethyl cellulose as substrate
74.8
substrate oat spelt xylan, C-terminal truncated mutant, pH 6.0, 65°C
74.8
-
purified isozyme III
75
-
after 4.7fold purification
75
substrate birchwood xylan, pH 6.5, 65°C
75
substrate birchwood xylan, pH 9.0, 60°C
8.9
purified recombinant enzyme, substrate birchwood xylan
8.9
Halalkalibacterium halodurans
-
culture supernatant
83
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks
83
-
37°C, pH 5.0, activity in crude-cell-free fungal extracts collected from fungal cultures on Miscanthus cell walls after 8 weeks, Fusarium sp. aff. equiseti, GenBank Accession: HQ630976
83
substrate beechwood xylan, pH 9.0, 60°C
additional information
Acacia verek
-
-
additional information
activities of wild-type XynC, and its domain deletion mutants, overview
additional information
activities of wild-type XynC, and its domain deletion mutants, overview
additional information
activities of wild-type XynZ, and its domain deletion mutants, overview
additional information
activities of wild-type XynZ, and its domain deletion mutants, overview
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
activities of wild-type and mutant enzymes, overview
additional information
-
enzyme activity is proportional to water activity (ratio of the equilibrium water vapor pressure over a material to that over pure water, roughly corresponding to the water content), enzyme activity as low as at a water activity of 0.59, 0.1 M sodium acetate, pH 4.5, 60°C
additional information
-
174 U/ml
additional information
-
113 U/ml
additional information
-
the purified extrecllular enzyme shows maximum activity 2.7 U/ml against beechwood xylan, 2.3 U/ml with birchwood xylan, 1.2 U/ml with glucuronoxylan, and 0.8 U/ml with arabinoxylan
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
substrate specificity, pH-dependent activity with different substrates, overview
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
activity with different xylans, overview
additional information
-
-
additional information
Pomacea insularus
-
-
additional information
-
-
additional information
-
activities of wild-type and mutant enzymes, overview
additional information
-
-
additional information
-
-
additional information
-
-
additional information
substrate specificity, overview
additional information
substrate specificity with different arabinoxylans, overview
additional information
-
substrate specificity with different arabinoxylans, overview
additional information
-
-
additional information
-
activities of wild-type and mutant enzymes, overview
additional information
Thermochaetoides thermophila
recombinant xylanase from gene xyn698 with intron gives 15.6 U/ml, that of gene xyn699 without intron results in 1.26 U/ml after 96 h growth
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
enzyme activity is proportional to water activity (ratio of the equilibrium water vapor pressure over a material to that over pure water, roughly corresponding to the water content), enzyme activity at a water activity between 0.91 and 0.83, 0.1 M sodium phosphate, pH 6.0, 60°C
additional information
-
enzyme activity is proportional to water activity (ratio of the equilibrium water vapor pressure over a material to that over pure water, roughly corresponding to the water content), enzyme activity as low as at a water activity of 0.59, 0.1 M sodium acetate, pH 4.5, 50°C
additional information
-
-
additional information
B2CNY5
purified recombinant enzyme, 281.2 U/ml with birchwood xylan, 211.0 U/ml with beechwood xylan, and 261.0 U/ml with oat spelt xylan
additional information
-
purified recombinant enzyme, 281.2 U/ml with birchwood xylan, 211.0 U/ml with beechwood xylan, and 261.0 U/ml with oat spelt xylan
additional information
-
2836 U/g dry weight, secreted enzymes
additional information
-
-
additional information
-
only relative enzyme activities are measured: microbial endoxylanase activity is higher than endogenous enzyme activity, higher total endoxylanase activity in variety Legat than Astuce, significant lower enzyme activity in bread from washed kernels in Astuce variety not in Legat wheat
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
x * 45000, calcuated
?
-
x * 60000, SDS-PAGE, x * 61200, calculated
?
-
x * 60000, recombinant enzyme, SDS-PAGE, x * 61200, about, sequence calculation
?
-
x * 45000, calcuated
-
?
-
x * 69000, SDS-PAGE
-
?
-
x * 69000, SDS-PAGE
-
?
-
x * 22630-22165, SDS-PAGE and mass spectrometry
?
-
x * 22630-22165, SDS-PAGE and mass spectrometry
-
?
x * 42500, about, sequence calculation
?
x * 131500, calculated, x * 130000, SDS-PAGE
?
-
x * 131500, calculated, x * 130000, SDS-PAGE
-
?
x * 21000, SDS-PAGE, x * 24000, claculated
?
x * 20200, extracellular enzyme, SDS-PAGE
?
-
x * 32200, SDS-PAGE
-
?
-
x * 20200, extracellular enzyme, SDS-PAGE
-
?
-
x * 32200, SDS-PAGE
-
?
-
x * 20200, extracellular enzyme, SDS-PAGE
-
?
-
x * 32200, SDS-PAGE
-
?
-
x * 20200, extracellular enzyme, SDS-PAGE
-
?
-
x * 32200, SDS-PAGE
-
?
-
x * 20200, extracellular enzyme, SDS-PAGE
-
?
-
x * 32200, SDS-PAGE
-
?
-
x * 20200, extracellular enzyme, SDS-PAGE
-
?
-
x * 24500, mass spectrometry, x* 25000, SDS-PAGE
?
-
x * 24500, mass spectrometry, x* 25000, SDS-PAGE
-
?
-
x * 21000, xylanase I, x * 24000, xylanase II, SDS-PAGE
?
-
x * 25100, native enzyme, SDS-PAGE
?
-
x * 25100, native enzyme, SDS-PAGE
-
?
x * 23000, SDS-PAGE, x * 23300, calculated
?
-
x * 23000, SDS-PAGE, x * 23300, calculated
-
?
-
x * 34000, SDS-PAGE
-
?
-
x * 23000, SDS-PAGE
-
?
-
x * 33000, SDS-PAGE
-
?
-
x * 38000, native extracellular enzyme, SDS-PAGE
?
-
x * 38000, native extracellular enzyme, SDS-PAGE
-
?
-
x * 23000, SDS-PAGE
-
?
-
x * 45000, recombinant enzyme, SDS-PAGE
?
-
x * 44700, recombinat enzyme, calculation from nucleotide sequence
?
-
x * 21500, enzyme component I from strain W1, SDS-PAGE
?
-
x * 22500, enzyme component II from strain W1, SDS-PAGE
?
-
x * 19000, native enzyme, SDS-PAGE
?
-
x * 23475, calculated
-
?
-
x * 20000, SDS-PAGE
-
?
-
x * 45000, recombinant enzyme, SDS-PAGE
-
?
-
x * 44700, recombinat enzyme, calculation from nucleotide sequence
-
?
-
x * 24000, SDS-PAGE
-
?
-
x * 99000, SDS-PAGE
-
?
-
x * 23000, SDS-PAGE
-
?
-
x * 19000, native enzyme, SDS-PAGE
-
?
-
x * 23253, sequence calculation, x * 23000, SDS-PAGE
?
-
x * 21400, SDS-PAGE
-
?
-
x * 23253, sequence calculation, x * 23000, SDS-PAGE
-
?
-
x * 35000, SDS-PAGE
-
?
-
x * 32000, SDS-PAGE
-
?
x * 449000, Xyl10C, sequence calculation, x * 90000, about, glycosylated recombinant Xyl10C, SDS-PAGE, x * 55000, deglycosylated recombinant Xyl10C, SDS-PAGE
?
x * 49800, about, sequence calculation, mature enzyme protein
?
x * 32500, purified mature enzyme, SDS-PAGE, x * 64960, unprocessed enzyme, amino acid sequence calculation
?
-
x * 56000, wild-type and mutant strain enzyme, SDS-PAGE
?
-
x * 49000, SDS-PAGE
-
?
-
x * 56000, wild-type and mutant strain enzyme, SDS-PAGE
-
?
-
x * 38000, SDS-PAGE
-
?
-
x * 29000, SDS-PAGE
-
?
x * 39000, SDS-PAGE, x * 42925, calculated
?
-
x * 39000, SDS-PAGE, x * 42925, calculated
-
?
x * 34441, sequence calculation, x * 37000, recombinant extracellular His- and c-myc-tagged enzyme, SDS-PAGE
?
x * 49000, about, sequence calculation
?
-
x * 21200, SDS-PAGE
-
?
Halalkalibacterium halodurans
x * 45000, SDS-PAGE
?
Halalkalibacterium halodurans
-
x * 24000, SDS-PAGE
?
Halalkalibacterium halodurans PPKS-2
-
x * 24000, SDS-PAGE
-
?
Halalkalibacterium halodurans TSEV1
-
x * 45000, SDS-PAGE
-
?
-
x * 21000, xylanase 2, SDS-PAGE
?
-
x * 6000, xylanase 1, SDS-PAGE
?
-
x * 24000, Xyl16-3, SDS-PAGE, x * 53000, Xylam, SDS-PAGE, x * 65000, Xyl1-3, SDS-PAGE, x * 90000, Xyl6-6, SDS-PAGE
?
x * 49000, SDS-PAGE, recombinant protein, x * 50480, calculated
?
-
x * 30000, xylanase B, SDS-PAGE
?
-
x * 21000, xylanase A, SDS-PAGE
?
x * 45000, SDS-PAGE, x * 43170, calculated
?
-
x * 24000, SDS-PAGE, isoform xylanase IIIA
?
-
x * 38000, SDS-PAGE, isoform xylanase IA
?
-
x * 68000, SDS-PAGE
-
?
-
x * 42000, SDS-PAGE
-
?
-
x * 86000, SDS-PAGE
-
?
-
x * 41584, calculated
-
?
-
x * 21000, SDS-PAGE
-
?
-
x * 48000, SDS-PAGE
-
?
x * 25827, mutant N38Y/F52W/G56Y/G201L, calculated, x * 25800, SDS-PAGE
?
x * 26000, recombinantenzyme, SDS-PAGE
?
-
x * 26000, recombinantenzyme, SDS-PAGE
-
?
-
x * 33000, xylanase I, SDS-PAGE
?
-
x * 30000, xylanase II, SDS-PAGE
?
-
x * 33000, xylanase I, SDS-PAGE
-
?
-
x * 30000, xylanase II, SDS-PAGE
-
?
x * 26132, XynA, sequence calculation, x * 28000, XynA, SDS-PAGE
?
-
x * 26132, XynA, sequence calculation, x * 28000, XynA, SDS-PAGE
-
?
-
x * 41000, SDS-PAGE
-
?
-
x * 53400, calculated, x * 56000, SDS-PAGE
?
-
x * 53400, calculated, x * 56000, SDS-PAGE
-
?
-
x * 39000, SDS-PAGE
-
?
-
x * 20200, SDS-PAGE
-
?
-
x * 156700, calculated
-
?
x * 20000, SDS-PAGE, x * 20674, calculated
?
x * 20000, recombinant extracellular deglycosylated enzyme, SDS-PAGE, x * 60000, above, recombinant extracellular glycosylated enzyme, SDS-PAGE
?
-
x * 20000, SDS-PAGE, x * 20674, calculated
-
?
-
x * 20000, recombinant extracellular deglycosylated enzyme, SDS-PAGE, x * 60000, above, recombinant extracellular glycosylated enzyme, SDS-PAGE
-
?
-
x * 21300, recombinant XynB, SDS-PAGE and sequence calculation
?
-
x * 21300, SDS-PAGE
-
?
-
x * 22000, Xyn3, SDS-PAGE, x * 21730, Xyn3, sequence calculation
?
-
x * 22000, Xyn3, SDS-PAGE, x * 21730, Xyn3, sequence calculation
-
?
x * 21500, about, sequence calculation
?
-
x * 41600, isoform xynA, x * 28600, isoform xynB, x * 40300, isoform xynC, calculated, x * 52000, isoform xynA, x * 50000, isoform xynB, x * 32000, isoform xynC, SDS-PAGE
?
x * 55000, recombinant enzyme, SDS-PAGE, x * 40000, about, sequence calculation
?
x * 42200, calculated from sequence
?
-
x * 43000, SDS-PAGE
-
?
-
x * 42200, calculated from sequence
-
?
Pomacea insularus
-
x * 47000, SDS-PAGE
?
x * 45982, mass spectrometry
?
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 40531, calculated, x * 40000, SDS-PAGE
?
-
x * 40531, calculated, x * 40000, SDS-PAGE
-
?
-
x * 33500, about, PhX33, mass spectrometry, x * 20100, about, PhX20, mass spectrometry
?
-
x * 33500, about, PhX33, mass spectrometry, x * 20100, about, PhX20, mass spectrometry
-
?
x * 38800, calculated, x * 47000, SDS-PAGE, His-tagged protein
?
-
x * 76000, xylanase X-a, SDS-PAGE
?
-
x * 54000, xylanase X-b-I, SDS-PAGE
?
-
x * 45000, xylanase X-b-II, SDS-PAGE
?
-
x * 76000, xylanase X-a, SDS-PAGE
-
?
-
x * 54000, xylanase X-b-I, SDS-PAGE
-
?
-
x * 45000, xylanase X-b-II, SDS-PAGE
-
?
-
x * 27000, SDS-PAGE
-
?
-
x * 85000, SDS-PAGE
-
?
x * 37300, calculated from sequence
?
-
x * 57000, SDS-PAGE
-
?
-
x * 37300, calculated from sequence
-
?
-
x * 36000, SDS-PAGE
-
?
-
x * 30500, isoform XynB, x * 30000, XynC, SDS-PAGE
?
1 * 42800, SDS-PAGE, 1 * 35000, SDS-PAGE. Heavier protein band (42.8 kDa) is observed after 12 h of culture, while the lighter band (35 kDa) appears 12 h later
?
-
1 * 42800, SDS-PAGE, 1 * 35000, SDS-PAGE. Heavier protein band (42.8 kDa) is observed after 12 h of culture, while the lighter band (35 kDa) appears 12 h later
-
?
x * 45000, SDS-PAGE, x * 47000, calculated
?
-
x * 45000, SDS-PAGE, x * 47000, calculated
-
?
MK331807
x * 44000, SDS-PAGE
?
-
x * 42000, SDS-PAGE
-
?
-
x * 24500, Xyl1, SDS-PAGE, x * 37500, Xyl2, SDS-PAGE, x * 38000, Xyl3, SDS-PAGE
?
x * 47000, SDS-PAGE, XynAS27. x * 33000, SDS-PAGE, XynAS27cd. x * 34000, SDS-PAGE, XynAS27cdl
?
-
x * 24500, Xyl1, SDS-PAGE, x * 37500, Xyl2, SDS-PAGE, x * 38000, Xyl3, SDS-PAGE
-
?
x * 38000, recombinant enzyme, SDS-PAGE
?
x * 43962, sequence calculation
?
-
x * 43962, sequence calculation
-
?
x * 43000, SDS-PAGE, x * 25902, calculated, x * 29949-34912, ESI-MS
?
x * 64000, SDS-PAGE, x * 46000, about, deglycoylated enzyme, mass spectrometry, x * 41540, sequence calculation
?
-
x * 30000, isozyme I, SDS-PAGE, x * 25500, isozyme II, SDS-PAGE, x * 33500, isozyme III, SDS-PAGE
?
x * 51000, SDS-PAGE of N-deglycosylated protein, x * 42000, calculated
?
x * 40997, sequence calculation, x * 60000, recombinant enzyme, SDS-PAGE
?
-
x * 40997, sequence calculation, x * 60000, recombinant enzyme, SDS-PAGE
-
?
-
x * 27000, SDS-PAGE
-
?
Thermochaetoides thermophila
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
?
Thermochaetoides thermophila CBS 144.50
-
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
-
?
Thermochaetoides thermophila DSM 1495
-
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
-
?
Thermochaetoides thermophila IMI 039719
-
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
-
?
-
x * 44377, calculation from nucleotide sequence
?
-
x * 54000, recombinant xylanase A produced in Escherichia coli, SDS-PAGE
?
-
x * 54000, recombinant xylanase A produced in Escherichia coli, SDS-PAGE
-
?
Thermomonospora sp.
-
x * 38000
?
x * 21900-22300, recombinant enzyme, SDS-PAGE
?
x * 21900 or x * 22100 or x * 22300, mass spectrometry of recombinant protein with variability in the amino terminus, x * 26900, SDS-PAGE
?
-
x * 21900-22300, recombinant enzyme, SDS-PAGE
-
?
-
x * 21300, SDS-PAGE
-
?
-
x * 24700, SDS-PAGE
-
?
-
x * 23600, SDS-PAGE
-
?
-
x * 82000, SDS-PAGE
-
?
-
x * 119642, calculated
?
-
x * 26000, mutant hybrid enzyme, SDS-PAGE
?
-
x * 29000, the enzyme also exists as a 20000 Da enzyme form, SDS-PAGE
?
-
x * 20000, the enzyme also exists as a 29000 Da enzyme form, SDS-PAGE
?
-
x * 18600, SDS-PAGE
-
?
-
x * 32000, xylanase I, SDS-PAGE
?
-
x * 23000, xylanase II, SDS-PAGE
?
-
x * 21000-22000, native wild-type enzyme, SDS-PAGE, x * 25000, recombinant wild-type enzyme, SDS-PAGE
?
B2CNY5
x * 21000, recombinant enzyme, SDS-PAGE
?
-
x * 20000-21000, recombinant wild-type enzyme, SDS-PAGE, x * 26000, mutant hybrid enzyme, SDS-PAGE
?
B2CNY5
x * 21000, recombinant His-tagged mature enzyme without N-terminal signal sequence, SDS-PAGE
?
-
x * 21000, Xyn2, SDS-PAGE
?
-
x * 20000-21000, recombinant wild-type enzyme, SDS-PAGE, x * 26000, mutant hybrid enzyme, SDS-PAGE
-
?
-
x * 21000, recombinant enzyme, SDS-PAGE
-
?
-
x * 30100, isozyme EX1, SDS-PAGE, x * 20100, isozyme EX2, SDS-PAGE
?
-
x * 30100, isozyme EX1, SDS-PAGE, x * 20100, isozyme EX2, SDS-PAGE
-
?
-
x * 71300, calculated, x * 80000, SDS-PAGE
?
x * 55000, wild-type, x * 28000, mutant XylA, x * 40000, mutant XylB, x * 26000, mutant XylC, SDS-PAGE
?
multimodular enzyme consisting of a catalytic domain and two tandem carbohydrate-binding modules (CBM36)
?
x * 60600, about, sequence calculation
dimer
-
2 * 27500, SDS-PAGE
dimer
-
2 * 27500, SDS-PAGE
-
dimer
-
2 * 49800, xylanase II
monomer
Acacia verek
-
1 * 60000, SDS-PAGE
monomer
1 * 63000, SDS-PAGE, recombinant EGXA
monomer
-
1 * 27000, isoform xyl I, 1 * 17700, isoform xylII, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
-
monomer
-
1 * 48000, SDS-PAGE
monomer
-
x * 32000, SDS-PAGE
monomer
-
1 * 24000, SDS-PAGE
monomer
-
1 * 24000, SDS-PAGE
-
monomer
-
1 * 56000, SDS-PAGE
monomer
-
1 * 50000, enzyme component II from strain W2, SDS-PAGE
monomer
-
1 * 49500, enzyme component II from strain W1, SDS-PAGE
monomer
-
1 * 56000, SDS-PAGE
-
monomer
1 * 20000, SDS-PAGE and HPLC
monomer
-
1 * 20000, SDS-PAGE and HPLC
-
monomer
-
1 * 42000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
-
monomer
1 * 49000, SDS-PAGE
monomer
-
1 * 49000, SDS-PAGE
-
monomer
-
1 * 65000, xylanase A, SDS-PAGE
monomer
-
1 * 29900, xylanase B, SDS-PAGE
monomer
-
1 * 23000, SDS-PAGE
monomer
-
1 * 23000, SDS-PAGE
-
monomer
-
1 * 22400, SDS-PAGE
monomer
-
1 * 22400, SDS-PAGE
-
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
-
monomer
-
1 * 70000, SDS-PAGE, 1 * 69300, LabChip microfluidic system
monomer
1 * 43500, SDS-PAGE
monomer
-
1 * 43500, SDS-PAGE
-
monomer
-
1 * 22900, isozyme Ia, SDS-PAGE, 1 * 20700, isozyme Ib, SDS-PAGE, 1 * 18600, isozyme Ic, SDS-PAGE, 1 * 31300, isozyme IIa, SDS-PAGE, 1 * 25400, isozyme IIb, SDS-PAGE, 1 * 38500, isozyme IIc, SDS-PAGE, 1 * 34300, isozyme IId, SDS-PAGE
monomer
-
1 * 22900, isozyme Ia, SDS-PAGE, 1 * 20700, isozyme Ib, SDS-PAGE, 1 * 18600, isozyme Ic, SDS-PAGE, 1 * 31300, isozyme IIa, SDS-PAGE, 1 * 25400, isozyme IIb, SDS-PAGE, 1 * 38500, isozyme IIc, SDS-PAGE, 1 * 34300, isozyme IId, SDS-PAGE
-
monomer
-
1 * 38000, SDS-PAGE
monomer
-
1 * 38000, SDS-PAGE
-
monomer
1 * 31600, SDS-PAGE
monomer
-
1 * 31600, SDS-PAGE
-
monomer
-
1 * 23900, xylanase I, SDS-PAGE, 1 * 33100, xylanase II, SDS-PAGE
monomer
-
1 * 54200, xylanase III
monomer
-
1 * 58800, gel filtration
monomer
-
1 * 58800, gel filtration
-
monomer
-
1 * 21000, SDS-PAGE
monomer
1 * 47000, SDS-PAGE
monomer
-
1 * 45500, SDS-PAGE
monomer
-
1 * 45500, SDS-PAGE
-
monomer
-
1 * 44000, SDS-PAGE
monomer
-
1 * 50000, xylanase X-I, SDS-PAGE
monomer
-
1 * 25000, xylanase X-II-A and X-II-B, SDS-PAGE
monomer
-
1 * 26400, SDS-PAGE
monomer
-
1 * 26400, SDS-PAGE
-
monomer
-
1 * 44000, SDS-PAGE
-
monomer
-
1 * 50000, xylanase X-I, SDS-PAGE
-
monomer
-
1 * 25000, xylanase X-II-A and X-II-B, SDS-PAGE
-
monomer
1 * 46000, SDS-PAGE
monomer
-
1 x * 12000, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 32000, SDS-PAGE
-
monomer
Thermochaetoides thermophila
1 * 29300, sequence analysis, 1 * 30000, SDS-PAGE
monomer
Thermochaetoides thermophila NIBGE 1
-
1 * 29300, sequence analysis, 1 * 30000, SDS-PAGE
-
monomer
-
1 * 44000, xylanase A, SDS-PAGE
monomer
-
1 * 44000, xylanase C, SDS-PAGE
monomer
-
1* 72000, xylanase B, SDS-PAGE
monomer
-
1 * 25000, SDS-PAGE
monomer
-
1 * 24000, SDS-PAGE
monomer
-
1 * 27500, SDS-PAGE
monomer
-
1 * 21500, SDS-PAGE
monomer
-
1 * 22000, wild-type enzyme, SDS-PAGE, 1 * 24000, mutant enzyme, SDS-PAGE
monomer
-
1 * 27500, SDS-PAGE
-
monomer
1 * 41100, SDS-PAGE
additional information
homology modeling, enzyme XYL1p has the overall fold typical to family 11 xylanases, comparison of XYL1 structure with other homologous acidophilic, neutrophilic and alkalophilic xylanases, overview
additional information
secondary structure comparisons, overview
additional information
-
secondary structure comparisons, overview
-
additional information
-
secondary structure comparisons, overview
-
additional information
-
enzyme N-terminal structure analysis and homology modelling, overview
additional information
-
enzyme N-terminal structure analysis and homology modelling, overview
-
additional information
-
two protein bands are detected by SDS-PAGE: 18400 Da and 19600 Da
additional information
structure homology modelling of wild-type and mutant enzymes, overview
additional information
-
bi-modular enzyme comprising a GH10 catalytic module and a family 15 carbohydrate-binding module, crystallization data
additional information
Mxyn10 contains a catalytic domain from positions 36 to 339 and a carbohydrate-binding module at the C-terminus. Glu163 and Glu271 are the most likely residues located in the catalytic site of Mxyn10
additional information
-
secondary structure analysis, enzyme contains 10-15% alpha-helices at pH 6.0 and 35°C, portion of alpha-helix is pH-dependent
additional information
Halalkalibacterium halodurans
the enzyme has the common eightfold TIM-barrel structure of family 10 xylanases, however, unlike non-alkaline active xylanases, it has a highly negatively charged surface and a deeper active site cleft, structure comparisons, overview
additional information
Halalkalibacterium halodurans S7
-
the enzyme has the common eightfold TIM-barrel structure of family 10 xylanases, however, unlike non-alkaline active xylanases, it has a highly negatively charged surface and a deeper active site cleft, structure comparisons, overview
-
additional information
tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
additional information
tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
additional information
-
tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
additional information
the enzyme possesses an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (position 165) catalyst and the other acts as a nucleophile (position 273)
additional information
the enzyme possesses an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (position 165) catalyst and the other acts as a nucleophile (position 273)
additional information
-
the enzyme possesses an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (position 165) catalyst and the other acts as a nucleophile (position 273)
additional information
-
the enzyme possesses an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (position 165) catalyst and the other acts as a nucleophile (position 273)
-
additional information
-
tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
-
additional information
catalytic residues are Glu78 and Glu172
additional information
Bcx possesses a beta-jellyroll fold that places its N- and C-termini in salt bridge contact. Mutant enzyme structure determination and analysis by X-ray diffraction and by NMR spectroscopy, overview. Overall conformation of Bcx changes very little in response to circular permutation, with effects largely being limited to increased local mobility near the new and the linked old termini and to a decrease in global stability against thermal denaturation
additional information
-
Bcx possesses a beta-jellyroll fold that places its N- and C-termini in salt bridge contact. Mutant enzyme structure determination and analysis by X-ray diffraction and by NMR spectroscopy, overview. Overall conformation of Bcx changes very little in response to circular permutation, with effects largely being limited to increased local mobility near the new and the linked old termini and to a decrease in global stability against thermal denaturation
additional information
-
XynBE18 structure-function relationship, homology modeling and molecular dynamic simulation, overview
additional information
-
XynB structure homology molecular modelling, overview
additional information
-
Xyn3 homology modelling
additional information
-
Xyn3 homology modelling
-
additional information
-
PhX33 contains predominant alpha-and, while PhX22 contains predominantly beta-sheets
additional information
-
PhX33 contains predominant alpha-and, while PhX22 contains predominantly beta-sheets
-
additional information
XynA19 contains a complete GH10 catalytic domain of GH 10 from Ile38 to Ala381, structure homology modeling of the recombinant enzyme, overview
additional information
-
(beta/alpha)8 barrel with 2 catalytic functions, the acid/base and the nucleophile, at the C-terminal side
additional information
-
enzyme N-terminal structure analysis and homology modelling, overview
additional information
structure homology modelling, XylG folds to form an (alpha/beta)8-barrel with two catalytic residues of an acid/base Glu181 and a nucleophile Glu289. The formation of a disulfide bond between Cys321 and Cys327 is predicted by homology modeling
additional information
-
structure homology modelling, XylG folds to form an (alpha/beta)8-barrel with two catalytic residues of an acid/base Glu181 and a nucleophile Glu289. The formation of a disulfide bond between Cys321 and Cys327 is predicted by homology modeling
-
additional information
the enzyme XynD consists of 387 amino acid residues with an N-terminal catalytic module, a linker rich in Ser and Thr residues, and a C-terminal family 1 carbohydrate-binding module
additional information
-
the enzyme XynD consists of 387 amino acid residues with an N-terminal catalytic module, a linker rich in Ser and Thr residues, and a C-terminal family 1 carbohydrate-binding module
additional information
-
the enzyme XynD consists of 387 amino acid residues with an N-terminal catalytic module, a linker rich in Ser and Thr residues, and a C-terminal family 1 carbohydrate-binding module
-
additional information
enzyme three-dimensional structure analysis
additional information
-
enzyme three-dimensional structure analysis
additional information
-
enzyme three-dimensional structure analysis
-
additional information
-
enzyme three-dimensional structure analysis
-
additional information
-
a 38000 Da enzyme form and a 48000 Da enzyme form are detected by SDS-PAGE. The 38000 Da enzyme form does not contain the cellulose-binding domain
additional information
-
a 38000 Da enzyme form and a 48000 Da enzyme form are detected by SDS-PAGE. The 38000 Da enzyme form does not contain the cellulose-binding domain
-
additional information
-
enzyme N-terminal structure analysis and homology modelling, overview
additional information
Thermomonospora sp.
-
the enzyme is composed of 38% alpha-helix and 10% beta-sheet
additional information
-
modeled structure of full-length XYN10A xylanase, overview
additional information
-
enzyme folds into a (beta/alpha)8-barrel structure, and has characteristic clusters of aromatic residues together with a lack of exposed hydrophobic residues, crystallization data
additional information
-
enzyme folds into a (beta/alpha)8-barrel structure, and has characteristic clusters of aromatic residues together with a lack of exposed hydrophobic residues, crystallization data
-
additional information
domain composition, the enzyme contains an N-termminal domain D1 which is the xylan-binding domain XBD, it is homologous to noncatalytic thermostabilizing domains of other xylanases, D1 is followed by the catalytic D2 domain, and 2 cellulose-binding domains D3 and D4, the latter linked via a proline-threonine-rich sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
E225A
mutation in catalytic residue, crystallization data
E337A
capture of the substrate xylohexaose in the inactivated site
E225A
-
mutation in catalytic residue, crystallization data
-
D60N
-
site-directed mutagenesis, the mutant shows an increased pH optimum and over 90% reduced specific activity compared to the wild-type enzyme
D60N/E141A
-
site-directed mutagenesis, the mutant shows an increased pH optimum and over 90% reduced specific activity compared to the wild-type enzyme
D60N/Y35W
-
site-directed mutagenesis, the mutant shows an increased pH optimum and over 90% reduced specific activity compared to the wild-type enzyme
E141A
-
site-directed mutagenesis, the mutant shows an increased pH optimum, slightly reduced thermostability, 50% increase in specific activity at pH 4.0, and an overall increased catalytic efficiency compared to the wild-type enzyme
Y35W
-
site-directed mutagenesis, the mutant shows an increased pH optimum and 64% reduced specific activity compared to the wild-type enzyme
Y35W/E141A
-
site-directed mutagenesis, the mutant shows an increased pH optimum and 46% reduced specific activity compared to the wild-type enzyme
A60D
increase in thermostability and in optimum temperature
Q47P/S159R
increase in thermostability and in optimum temperature
S68R
increase in thermostability and in optimum temperature
T16A/T39I/L176Q
increase in thermostabilityand in optimum temperature
D48N/T64S
shift in pH optimum from 2.0 to 5.0
T64S
shift in pH optimum from 2.0 to 3.8
D48N/T64S
-
shift in pH optimum from 2.0 to 5.0
-
T64S
-
shift in pH optimum from 2.0 to 3.8
-
D11F/R122D
-
no inhibition by Triticum aestivum xylanase inhibitor-I
G12
-
no inhibition by Triticum aestivum xylanase inhibitor-I
G12K
-
decreased sensitivity to Triticum aestivum xylanase inhibitor-I
G12W
-
no inhibition by Triticum aestivum xylanase inhibitor-I
G23A/G24P/S26T
-
the mutation increases the enzyme's thermostability
N35D
-
increased sensitivity to Triticum aestivum xylanase inhibitor-I
Q127E
-
specific activity is lower than 5% compared to the wild type enzyme
Q127K
-
no inhibition by Triticum aestivum xylanase inhibitor-I
Q127L
-
specific activity is lower than 5% compared to the wild type enzyme
R112H
-
wild type comparable sensitivity to TAXI-I
R112Y
-
no inhibition by Triticum aestivum xylanase inhibitor-I
T11Y/N12H/N13D/F15Y/F16F
-
the mutation increases the enzyme's thermostability
T205C/A52C
the optimum temperature of the mutant enzyme is improved from 45°C to 60°C, and it retains greater than 90.0% activity (wild-type enzyme retains only 50.0% activity) after treatment at 50°C for 85 min. The optimum pH of mutant xylanase is similar to wild-type enzyme (pH 5.0). The pH stability span (5.0-7.0) of the wild-type enzyme is increased to 3.0-9.0 for the mutant enzyme
T30E/N32G/S33P
-
the mutation increases the enzyme's thermostability
V3A/I4V/T6S/Q8E
-
the mutation increases the enzyme's thermostability
W9Y
-
mutant enzyme is insensitive for Triticum aestivum xylanase inhibitor-II
W9Y/N35D
-
increased sensitivity to Triticum aestivum xylanase inhibitor-I and insensitive for Triticum aestivum xylanase inhibitor-II
Y174W
-
increased sensitivity to Triticum aestivum xylanase inhibitor-I
G23A/G24P/S26T
-
the mutation increases the enzyme's thermostability
-
T11Y/N12H/N13D/F15Y/F16F
-
the mutation increases the enzyme's thermostability
-
T30E/N32G/S33P
-
the mutation increases the enzyme's thermostability
-
V3A/I4V/T6S/Q8E
-
the mutation increases the enzyme's thermostability
-
D11F/R122D
the mutant shows highly decreased sensitivity to inhibitor Triticum aestivum xylanase inhibitor compared to wild-type enzyme
F48C
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
G23R
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
Q175K
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
T10H
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
T44C
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
T44Y
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
T87D
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
W9H
construction of a XynA mutant with increased pH stability, Computational design-based molecular engineering, overview
Y94C
-
mutation increases the half-inactivation temperature by 2-3°C over that of the wild type enzyme
F181Y
-
isoform xylanase 10A, enzymic activity similar to wild-type
G295E
-
isoform xylanase 10C, enzymic activity similar to wild-type
Y340A
-
isoform xylanase 10C, enzymic activity reduced by more than 90%
Y434F
-
isoform xylanase 10C, enzymic activity similar to wild-type
Y87A
-
isoform xylanase 10A, reduced enzymic activity
N62D
-
XylB mutant with inhibition specificity similar to the wild type enzyme and lower pH optimum
N65D
-
XylA mutant with inhibition specificity similar to the wild type enzyme and lower pH optimum
Q144N
-
XylA mutant with inhibition specificity similar to the wild type enzyme
V151T
-
XylA mutant with increased inhibition sensitivity
E159A/E265A
-
crystals are isomorphous to wild-type crystals
G201L
increase in melting temperature by 8.5 degrees
N38Y/F52W/G56Y/G201L
increase in melting temperature by 14 degrees
D101N
site-directed mutagenesis, deleterious mutation
D101N/G103F/R132A/R136A
site-directed mutagenesis, the mutant is expressed in inclusion bodies
F48Y
site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme
F48Y/R49A/T50V/T147L
site-directed mutagenesis, the half-life of the mutant is 4fold increased compared to the wild-type enzyme
F48Y/T147L
site-directed mutagenesis, the half-life of the mutant is 7.5fold increased compared to the wild-type enzyme
F48Y/T50V
site-directed mutagenesis, the half-life of the mutant is increased compared to the wild-type enzyme
F48Y/T50V/T147L
site-directed mutagenesis, the half-life of the mutant is 15fold increased compared to the wild-type enzyme
G103F
site-directed mutagenesis, the mutation introduced a bulky hydrophobic residue causing a clash with the neighbouring residues that results in destabilization
R132A
site-directed mutagenesis, deleterious mutation
R136A
site-directed mutagenesis, deleterious mutation
R49A
site-directed mutagenesis, deleterious mutation
T147L
site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme
T50V
site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme
T50V/T147L
site-directed mutagenesis, the half-life of the mutant is increased compared to the wild-type enzyme
Y69F
the barrier for conversion of the 4C1 chair to the more-stable 2,5B boat in the wild-type enzyme-substrate complex is significantly lower than it is for the mutant. The mutation reduces the degree of oxacarbenium-ion character in the proximal xylose ring of the enzyme-substrate complex
E129A/E236A
-
the naturally occuring enzyme mutant XynBE18 shows also beta-1,3-1,4-glucan hydrolase activity, EC 3.2.1.6. Recombinant XynBE18 shows specificity toward oat spelt xylan and birchwood xylan and barley beta-1,3-1,4-glucan and lichenin, no activity with carboxymethylcellulose or Avicel, overview
DELTAD130
-
retains specific activity comparable to the wild-type
F14Y
-
retains specific activity comparable to the wild-type
K131S/K132S
-
site-directed mutagenesis, with or without deletion mutation DELTAP130, the mutant without deletion shows no sensitivity to inhibitor XIP-1, like the wild-type enzyme, but shows increased activity compared to the wild-type, the mutant with deletion mutation is sensitive to inhibitor XIP-1
Q121R
-
shows a marked 33% increase in specific activity, mainly due to a 2fold increase in kcat. It does not alter the hydrolysis product profile of wheat arabinoxylan, shows highest increase in activity on low substituted xylan
R7T
-
retains specific activity comparable to the wild-type
S129G
-
sensitivity to the xylanase inhibitor protein, XIP-I
S129G/DELTAD130
-
lowest Ki compared to tested natural enzymes
S129G/S44D
-
low specific activity
S129G/S44N
-
sensitivity to the xylanase inhibitor protein, XIP-I
S44A
-
loses both pH-dependence profile and activity, reduces activity mainly due to a reduction in kcat whereas the apparent affinity remains unchanged
S44D
-
shows only slight alteration in Km and Vmax, reduces activity mainly due to a reduction in kcat whereas the apparent affinity remains unchanged. It shifts the activity to acidic pHs by ca. 1 unit, decreasing the optimum pH to 4.5. It has a broader pH profile retaining ca. 60% of its maximum activity at pH 3.0 as compared to the wild-type
S44N
-
shows only slight alteration in Km and Vmax, reduces activity mainly due to a reduction in kcat whereas the apparent affinity remains unchanged. It shifts the activity to alkaline pHs by ca. 0.5 unit with a pH optimum of 5.5
D144A
crystallization data
E78Q
crystallization data
D144A
-
crystallization data
-
E78Q
-
crystallization data
-
E128H
-
inhibits the breakdown of the glycosyl-enzyme intermediate. Restoration of the breakdown activity of the mutant by adding exogenous nucleophiles, such as sodium azide, results in a mutant that acts as a switching enzyme with azide
G23A/G24P/S26T
-
the mutation increases the enzyme's thermostability
T11Y/N12H/N13D/F15Y/F16F
-
the mutation increases the enzyme's thermostability
T30E/N32G/S33P
-
the mutation increases the enzyme's thermostability
V3A/I4V/T6S/Q8E
-
the mutation increases the enzyme's thermostability
E128H
-
inhibits the breakdown of the glycosyl-enzyme intermediate. Restoration of the breakdown activity of the mutant by adding exogenous nucleophiles, such as sodium azide, results in a mutant that acts as a switching enzyme with azide
-
D65P
98% of wild-type activity, decrease in melting temperature
D65P/N66G
102% of wild-type activity, increase in melting temperature
N44H
101%% of wild-type activity, decrease in melting temperature
N63L
85% of wild-type activity, decrease in melting temperature
N66G
100% of wild-type activity, decrease in melting temperature
S102N
100%% of wild-type activity, increase in melting temperature
S35C
101% % of wild-type activity, decrease in melting temperature
S35C/N44H/Y61M/T62C/N63L/D65P/N66G/T101P/S102N
114% of wild-type activity, 20 degrees increase in melting temperature
S35C/T62C
97%% of wild-type activity, increase in melting temperature
T101P
99%% of wild-type activity
T62C
86%% of wild-type activity, decrease in melting temperature
Y61M
94% of wild-type activity, decrease in melting temperature
Y61M/N63L
109% of wild-type activity, decrease in melting temperature
N44H
-
101%% of wild-type activity, decrease in melting temperature
-
N63L
-
85% of wild-type activity, decrease in melting temperature
-
S35C
-
101% % of wild-type activity, decrease in melting temperature
-
T62C
-
86%% of wild-type activity, decrease in melting temperature
-
Y61M
-
94% of wild-type activity, decrease in melting temperature
-
H209N
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 8.0-10.0, similar to wild-type
N257D
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 5.0-10.0
Q158R
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 5.0-10.0,
H209N
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 8.0-10.0, similar to wild-type
-
N257D
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 5.0-10.0
-
Q158R
-
mutant shows increased thermostability relative to the wild type at 70°C and 75°C and is stable in the pH range 5.0-10.0,
-
G217L
-
increases activity and alkaline pH stability to some extent
G23A/G24P/S26T
-
the mutation increases the enzyme's thermostability
G25P
-
mainly leads to increase in alkaline pH stability without improving the specific activity
I91T
-
results in the main contribution to catalytic activity rather than alkaline pH stability
T11Y/N12H/N13D/F15Y/F16F
-
the mutation increases the enzyme's thermostability
T21A
-
mainly leads to increase in alkaline pH stability without improving the specific activity
T21A/G25P/V87P/J91T/G217L
-
mutant 2TfxA98, with approximately 12fold increased kcat/Km and 4.5fold decreased Km compared with its parent. Mutant 2TfxA98 inherits its thermostability from parent TfxA and enhances its alkaline pH stability through DNA shuffling. 2Tfx98 has significantly improved catalytic activities in performing the xylan hydrolysis. It is most active at 75°C, almost the same as the parental TfxA, but 2TfxA98 produces 1.9 times more reducing sugar than TfxA at 75°C of pH 9.0
T30E/N32G/S33P
-
the mutation increases the enzyme's thermostability
V3A/I4V/T6S/Q8E
-
the mutation increases the enzyme's thermostability
V87P
-
significantly improves both the activity and alkaline pH stability
A54T
-
when exposed to 80°C for 90 min the mutant displays a low stability and retains only 10% of its activity. It is extremely alkali tolerant. After 90 min at pH 10 it retains 93% of its activity. It has catalytic activity almost comparable to the wild-type
D72G
-
decreased activity
K30E/W40R/T57A/K80R
-
thermostable mutant, when exposed to 80°C for 90 min it displays 75% retention of its total activity. The mutant loses nearly 60% of its activity under extremely alkaline conditions (after 90 min at pH 10). It has a much lower activity as compared to the wild-type
L18P/A193S/H201Y
-
low activity
F180Q/H144C/N92C
increased resistance towards thermal inactivation at alkaline pH
H144C/N92C
increased resistance towards thermal inactivation at alkaline pH
H22K/F180Q/H144C/N92C
increased resistance towards thermal inactivation at alkaline pH
K58R
site-directed mutagenesis, slight increase of thermostability at 55°C from half-life 5 min, wild-type, to 10-20 min, increased pH-stability compared to the wild-type enzyme
K58R/A160R
site-directed mutagenesis, no alteration of thermal or pH-stability
K58R/A160R/N97R
site-directed mutagenesis, no alteration of thermal or pH-stability
K58R/A160R/N97R/N67R
site-directed mutagenesis, no alteration of thermal or pH-stability
K58R/A160R/N97R/N67R/T26R
site-directed mutagenesis, no alteration of thermal or pH-stability
K58R/A160R/N97R/N67R/T26R/A132R
site-directed mutagenesis, no alteration of thermal or pH-stability
N11D
-
site-directed mutagenesis, increase of half-life to about 100 min at 65°C
N38E
-
site-directed mutagenesis, increase of half-life to about 100 min at 65°C
N97R/F93W/H144K
increased resistance towards thermal inactivation at alkaline pH
Q162H
-
site-directed mutagenesis, mutation at the C-terminus of the alpha-helix has a stabilizing effect at 55°C, not at 65°C
Q162Y
-
site-directed mutagenesis, mutation at the C-terminus of the alpha-helix has a stabilizing effect at 55°C, not at 65°C
Q286A/N340Y
LC132960
substantial improvement of thermostability
S110C/N154C
-
site-directed mutagenesis, introduction of a disulfide bridge in the alpha-helix of the enzyme leads to increase of the half-life at 65°C from less than 1 min to 14 min
S110C/N154C/Q162H
-
site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview
S110C/N154C/Q162H/N11D
-
site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview
S110C/N154C/Q162H/N11D/N38D
-
site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview
S110C/N154C/Q162Y
-
site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview
S110C/N154C/Q162Y/N11D
-
site-directed mutagenesis, mutations lead to increased thermal and pH stability, overview
S186R
site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate compared to the wild-type enzyme
S186R/N67R
site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate compared to the wild-type enzyme
S186R/N67R/T26R
site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate, reduced stability at 60°C and unaltered at 65°C in presence of substrate, compared to the wild-type enzyme
S186R/N67R/T26R/Q34R
site-directed mutagenesis, highly reduced thermal stability at 50°C in absence of substrate, unaltered stability at 60°C and slightly increased at 65°C in presence of substrate, compared to the wild-type enzyme
S186R/N67R/T26R/Q34R/N69R
site-directed mutagenesis, reduced thermal stability at 50°C in absence of substrate, increased stability at 60°C and 65°C in presence of substrate, compared to the wild-type enzyme
S186R/N67R/T26R/Q34R/S40R
site-directed mutagenesis, highly reduced thermal stability at 50°C in absence of substrate, highly increased stability at 60°C and increased 65°C in presence of substrate, compared to the wild-type enzyme
N14H
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
N30V
thermostabilizing mutation
Q10S
thermostabilizing mutation
Q34C
thermostabilizing mutation
Q34H
thermostabilizing mutation
Q34L
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
S194H
thermostabilizing mutation
S25E
thermostabilizing mutation
S35E
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
S71T
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
S9P/T13F/N14H/Y18F/Q34L/S35E/S71T
hyperthermostable mutant Xyn11TS, retains full activity after incubation at 90°C for 60 min, catalytic activity is broadly similar to the wild-type
T13Y
thermostabilizing mutation
T4L
thermostabilizing mutation
Y18F
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
E142H
-
complete loss of activity
E244A
-
1% of wild-type activity
E244H
-
complete loss of activity
K231R/K223R/K227R
-
145% of wild-type activity
K73R/K185R
-
133% of wild-type activity
K73R/K185R/K231R/K223R/K227R
-
146% of wild-type activity
T28C/T60C
-
171% of wild-type activity, 2-3fold increases in bagasse hydrolysis at pH 9.0 and 60°C compared to the wild-type
T28C/T60C/T48F/L59F
-
134% of wild-type activity
T28C/T60C/T77C/E249C
-
158% of wild-type activity, 2-3fold increases in bagasse hydrolysis at pH 9.0 and 60°C compared to the wild-type
V5N/V6N/K7R/K223R/K227R
-
130% of wild-type activity
V5N/V6N/K7R/K223R/K227R/T28C/T60C
-
154% of wild-type activity
S100C/N150C
-
increased thermostability of about 5°C compared to the wild type enzyme
S100C/N150C
-
increased thermostability of about 5°C compared to the wild type enzyme
-
V169A/I170F/D171N
Halalkalibacterium halodurans
site-directed mutagenesis, the mutant shows a pH optimum of pH 7.0, incontrast to the wild-type enzyme which has an optimum at pH 9.0-9.5
V169A/I170F/D171N
Halalkalibacterium halodurans S7
-
site-directed mutagenesis, the mutant shows a pH optimum of pH 7.0, incontrast to the wild-type enzyme which has an optimum at pH 9.0-9.5
-
biofuel production
potential application in the field of biomass pretreatment and biofuel production
biofuel production
-
potential application in the field of biomass pretreatment and biofuel production
-
D281N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. The TtGH8 D281N-beta-1,4-xylohexaose complex structure reveals that, the -1 subsite sugar is in a completely ring-flipped, southern hemisphere 1C4 chair conformation. Although this allows access to a hexasaccharide complex structure, the ring-flipped -1 sugar is unlikely to be representative of a catalytically relevant conformation since its position neither allows protonation of the leaving group by Glu73 nor is there a potential reactive water. In the 1C4 chair conformation the now axial (and down) O2 occupies the position that should instead be occupied by the nucleophilic water
D281N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. The TtGH8 D281N-beta-1,4-xylohexaose complex structure reveals that, the -1 subsite sugar is in a completely ring-flipped, southern hemisphere 1C4 chair conformation. Although this allows access to a hexasaccharide complex structure, the ring-flipped -1 sugar is unlikely to be representative of a catalytically relevant conformation since its position neither allows protonation of the leaving group by Glu73 nor is there a potential reactive water. In the 1C4 chair conformation the now axial (and down) O2 occupies the position that should instead be occupied by the nucleophilic water
-
D281N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. The TtGH8 D281N-beta-1,4-xylohexaose complex structure reveals that, the -1 subsite sugar is in a completely ring-flipped, southern hemisphere 1C4 chair conformation. Although this allows access to a hexasaccharide complex structure, the ring-flipped -1 sugar is unlikely to be representative of a catalytically relevant conformation since its position neither allows protonation of the leaving group by Glu73 nor is there a potential reactive water. In the 1C4 chair conformation the now axial (and down) O2 occupies the position that should instead be occupied by the nucleophilic water
-
Q1C/Q24C
introduction of disulfide bridge, leading to increase in temperature optimum at pH 6.5 by about 10 degrees to 75°C, increased resistance to thermal inactivation and increased melting temperature. At pH 8 and 70°C, the disulfide bridge increases the enzyme half-life 20fold in the presence of substrate
Q1C/Q24C
-
introduction of disulfide bridge, leading to increase in temperature optimum at pH 6.5 by about 10 degrees to 75°C, increased resistance to thermal inactivation and increased melting temperature. At pH 8 and 70°C, the disulfide bridge increases the enzyme half-life 20fold in the presence of substrate
-
S9P
locks the conformation of a surface loop, catalytic activity is broadly similar to the wild-type
S9P
thermostabilizing mutation
T13F
increases hydrophobic interactions
T13F
thermostabilizing mutation, catalytic activity is broadly similar to the wild-type
additional information
generation of two constructs of XynC, one with its cellulose binding domain and the catalytic domain, pXynC-BC, and the other with only the catalytic domain, pXynC-C. The specific activities of XynC with and without the non-catalytic domains are similar
additional information
generation of two constructs of XynC, one with its cellulose binding domain and the catalytic domain, pXynC-BC, and the other with only the catalytic domain, pXynC-C. The specific activities of XynC with and without the non-catalytic domains are similar
additional information
generation of two constructs of XynZ: pXynZ-BDC, which includes the dockerin domain, and pXynZ-C, which does not. For XynZ, the specific activity of the enzyme without the non-catalytic domains is about 5fold greater than that of the intact enzyme. The overall increase in activity is 9fold higher for XynZ-C versus XynZ-BDC
additional information
generation of two constructs of XynZ: pXynZ-BDC, which includes the dockerin domain, and pXynZ-C, which does not. For XynZ, the specific activity of the enzyme without the non-catalytic domains is about 5fold greater than that of the intact enzyme. The overall increase in activity is 9fold higher for XynZ-C versus XynZ-BDC
additional information
truncated derivatives XynAGN16L (truncation of GH 10 domain at N-terminus) and XynAGN16Lpd (truncation of GH 10 domain at N-terminus and polysaccharide deacetylases domain) show similar features, including catalytic activities at 0°C, thermolabilities at temperatures of more than 50°C, and similar substrate specificity. However, the polysaccharide deacetylases domain improves the affinity and catalytic efficiency towards xylans
additional information
-
truncated derivatives XynAGN16L (truncation of GH 10 domain at N-terminus) and XynAGN16Lpd (truncation of GH 10 domain at N-terminus and polysaccharide deacetylases domain) show similar features, including catalytic activities at 0°C, thermolabilities at temperatures of more than 50°C, and similar substrate specificity. However, the polysaccharide deacetylases domain improves the affinity and catalytic efficiency towards xylans
-
additional information
-
construction of an N-terminal replacement mutant
additional information
-
construction of an N-terminal replacement mutant
-
additional information
DELTAXBD, consists of the catalytic domain only and corresponds to ALa1-Pro222 of XynJ. Mutants DELTAXBDR5 and DELTAXBDK51R/R5 show about 50% activity of that of DELTAXBD and have optima of pH 9.0 and 9.5, respectively. Reinforcing the characteristic salt bridge in the catalytic cleft and introducing excess Arg residues on the protein surface shift the optimum pH of the wild-type enzyme from 8.5 to 9.5. Mutant DELTAXBDK51R exhibit almost the same temperature profile and temperature optimum as DELTAXBD. The temperature optima of mutants DELTAXBDR5 and DELTAXBDK51R/R5 are both 60°C. Mutants show lower specific activity than DELTAXBD at 37-60°C, but they show apparently higher activity at 65°C. Introduction of excess Arg residues on the protein surface increase the thermostability of DELTAXBD
additional information
-
the fusion of the 1642-bp laccase (CorA) with either the 555-bp xylanase (XynA) or the thermostable variant (XynAG3) are performed by insertion of the xylanase into a surface loop of the laccase. The resulting chimeric constructs of 2197 bp contain a central region composed of the XynA or XynAG3 sequence flanked by the regions of the CorA encoding the N-terminal residues 1216 (forming the 5' region of the chimera) and the C-terminal region comprising residues 217513 of CorA. As a consequence, the final construct results in two linkage points between the laccase and xylanase domains
additional information
generation of a bifunctional enzyme consisting of a GH11 endo-1,4-beta-xylanase fused to a GH43 beta-xylosidase, both from Bacillus subtilis. The substrate cleavage rate is altered by the molecular fusion improving at least 3fold the xylose production using specific substrates as beechwood xylan and hemicelluloses from pretreated biomass. The chimeric enzyme shows higher thermotolerance with a positive shift of the optimum temperature from 35°C to 50°C for xylosidase activity
additional information
fusion of enzyme with a carbohydrate-binding module from Clostridium thermocellum which exhibits high affinity to xylan. The molecular fusion does not alter the pH and temperature dependence, but leads to an increase of 65% in the catalytic efficiency. As supplement in the commercial cocktail Accellerase1 1500, the chimeric enzyme improves the reducing sugar release by 17% from pretreated sugarcane bagasse
additional information
-
fusion of enzyme with a carbohydrate-binding module from Clostridium thermocellum which exhibits high affinity to xylan. The molecular fusion does not alter the pH and temperature dependence, but leads to an increase of 65% in the catalytic efficiency. As supplement in the commercial cocktail Accellerase1 1500, the chimeric enzyme improves the reducing sugar release by 17% from pretreated sugarcane bagasse
additional information
construction of a fusion protein with the carbohydrate-binding doamin of xylanase XynZ from Clostridium thermocellum. The fusion does not alter the pH and temperature dependence, but increases the catalytic activity by 65%
additional information
-
construction of a fusion protein with the carbohydrate-binding doamin of xylanase XynZ from Clostridium thermocellum. The fusion does not alter the pH and temperature dependence, but increases the catalytic activity by 65%
additional information
-
generation of a bifunctional enzyme consisting of a GH11 endo-1,4-beta-xylanase fused to a GH43 beta-xylosidase, both from Bacillus subtilis. The substrate cleavage rate is altered by the molecular fusion improving at least 3fold the xylose production using specific substrates as beechwood xylan and hemicelluloses from pretreated biomass. The chimeric enzyme shows higher thermotolerance with a positive shift of the optimum temperature from 35°C to 50°C for xylosidase activity
-
additional information
-
fusion of enzyme with a carbohydrate-binding module from Clostridium thermocellum which exhibits high affinity to xylan. The molecular fusion does not alter the pH and temperature dependence, but leads to an increase of 65% in the catalytic efficiency. As supplement in the commercial cocktail Accellerase1 1500, the chimeric enzyme improves the reducing sugar release by 17% from pretreated sugarcane bagasse
-
additional information
-
construction of a fusion protein with the carbohydrate-binding doamin of xylanase XynZ from Clostridium thermocellum. The fusion does not alter the pH and temperature dependence, but increases the catalytic activity by 65%
-
additional information
the disruption of xyn11A causes only a moderate decrease, about 30%, in the level of extracellular endo-beta-1-4-xylanase activity
additional information
-
the disruption of xyn11A causes only a moderate decrease, about 30%, in the level of extracellular endo-beta-1-4-xylanase activity
additional information
-
the disruption of xyn11A causes only a moderate decrease, about 30%, in the level of extracellular endo-beta-1-4-xylanase activity
-
additional information
construction of a deletion mutant lacking the C-terminal ricin-type beta-trefoil lectin domain-like part. Mutant shows a decrease in binding capacities to lignin and insoluble polysaccharides
additional information
construction of a library of circular permutants, generated by random circular permutation of Bcx, random DNase cleavage of the circularized Bcx gene, to introduce new termini in loop regions while linking its native termini directly or via one or two glycines, qualitative analysis, overview. Several permutations place key catalytic residues at or near the new termini with minimal deleterious effects on activity, up to 4fold increased activity. Mutant structure determination and analysis by X-ray diffraction and by NMR spectroscopy. Detailed stability and activity studies on three selected permutants, cpN35G2', cpY94G2', and cpY174G2', overview
additional information
-
construction of a library of circular permutants, generated by random circular permutation of Bcx, random DNase cleavage of the circularized Bcx gene, to introduce new termini in loop regions while linking its native termini directly or via one or two glycines, qualitative analysis, overview. Several permutations place key catalytic residues at or near the new termini with minimal deleterious effects on activity, up to 4fold increased activity. Mutant structure determination and analysis by X-ray diffraction and by NMR spectroscopy. Detailed stability and activity studies on three selected permutants, cpN35G2', cpY94G2', and cpY174G2', overview
additional information
removal of the CBMs from Xyn10A strongly reduces the ability of plant cell wall hydrolysis
additional information
-
removal of the CBMs from Xyn10A strongly reduces the ability of plant cell wall hydrolysis
additional information
generation of a truncationmutant lacking the N-terminal domain, the mutant is catalytically inactive
additional information
-
generation of a truncationmutant lacking the N-terminal domain, the mutant is catalytically inactive
additional information
-
removal of the CBMs from Xyn10A strongly reduces the ability of plant cell wall hydrolysis
-
additional information
-
a DELTAxyn5 mutant, as well as a xyn5DELTASLH mutant, lacking the SLH domain, grow poorly and produce minimal amounts of Xyn1 and Xyn3 on water-insoluble xylan. The xyn5DELTASLH mutant is secreted to the culture medium
additional information
-
generation of XynB mutans variants, e.g. deletion mutant DELTAP130, displaying increased catalytic efficiency towards wheat arabinoxylan and xylo-oligosaccharides and identified specific determinants in PgXynB thumb region responsible for resistance to the wheat xylanase inhibitor XIP-I
additional information
enzyme knockout mutant, strain is as virulent as wild-type in infecting the rice host
additional information
silencing of the endoxylanase by double-stranded RNA targeting, by RNA interference, RNAi, of the carbohydratebinding module, CBM, region results in an average decrease in infection of 60%
additional information
-
silencing of the endoxylanase by double-stranded RNA targeting, by RNA interference, RNAi, of the carbohydratebinding module, CBM, region results in an average decrease in infection of 60%
additional information
-
preparation of a robust immobilized biocatalyst of beta-1,4-endoxylanase C-terminally His-tagged Xys1 by surface coating with polymers for production of xylooligosaccharides from different xylan sources. Surface coating of dextran-modified Ag-G-Xys1-L and Ag-G-Xys1-H biocatalysts with cationic polymer (PEI) by chemical modifications via ionic exchange. The optimized biocatalyst is 550fold more stable than one-point covalent immobilized C-terminally His-tagged Xys1 at 70°C, pH 7.0. Hydrolysis of beechwood, wheat straw and corncob xylans is 93% in 4 h, 44% in 5 h and 100% in 1 h, respectively. Maximum values of xylooligosaccharides are found for beechwood at 20.6 mg/ml, wheat at 12.5 mg/ml, and corncob at 30.4 mg/ml. The optimized biocatalyst is reused for 15 reaction cycles without affecting its catalytic activity. Method optmization and evaluation, overview
additional information
preparation of a robust immobilized biocatalyst of beta-1,4-endoxylanase C-terminally His-tagged Xys1 by surface coating with polymers for production of xylooligosaccharides from different xylan sources. Surface coating of dextran-modified Ag-G-Xys1-L and Ag-G-Xys1-H biocatalysts with cationic polymer (PEI) by chemical modifications via ionic exchange. The optimized biocatalyst is 550fold more stable than one-point covalent immobilized C-terminally His-tagged Xys1 at 70°C, pH 7.0. Hydrolysis of beechwood, wheat straw and corncob xylans is 93% in 4 h, 44% in 5 h and 100% in 1 h, respectively. Maximum values of xylooligosaccharides are found for beechwood at 20.6 mg/ml, wheat at 12.5 mg/ml, and corncob at 30.4 mg/ml. The optimized biocatalyst is reused for 15 reaction cycles without affecting its catalytic activity. Method optmization and evaluation, overview
additional information
-
preparation of a robust immobilized biocatalyst of beta-1,4-endoxylanase C-terminally His-tagged Xys1 by surface coating with polymers for production of xylooligosaccharides from different xylan sources. Surface coating of dextran-modified Ag-G-Xys1-L and Ag-G-Xys1-H biocatalysts with cationic polymer (PEI) by chemical modifications via ionic exchange. The optimized biocatalyst is 550fold more stable than one-point covalent immobilized C-terminally His-tagged Xys1 at 70°C, pH 7.0. Hydrolysis of beechwood, wheat straw and corncob xylans is 93% in 4 h, 44% in 5 h and 100% in 1 h, respectively. Maximum values of xylooligosaccharides are found for beechwood at 20.6 mg/ml, wheat at 12.5 mg/ml, and corncob at 30.4 mg/ml. The optimized biocatalyst is reused for 15 reaction cycles without affecting its catalytic activity. Method optmization and evaluation, overview
-
additional information
-
obtained switching mutant N127S-E128H, rate of hydrolysis is apparently zero in the absence of sodium azide, accumulates the glycosyl-enzyme intermediate, breakdown rate of glycosyl-enzyme intermediate is dramatically accelerated by two orders of magnitude in the presence of 300 mM sodium azide
additional information
-
substituting of Streptomyces olivaceovirdis SoxB 33 N-terminal amino acid residues with the corresponding residues of the thermophilic xylanase TfxA from Thermomonospora fusca strain ATCC 27730 significantly enhances the enzyme thermostability, overview
additional information
-
obtained switching mutant N127S-E128H, rate of hydrolysis is apparently zero in the absence of sodium azide, accumulates the glycosyl-enzyme intermediate, breakdown rate of glycosyl-enzyme intermediate is dramatically accelerated by two orders of magnitude in the presence of 300 mM sodium azide
-
additional information
recombinant protein expressed in Pichia pastoris without signal peptide exhibits better physicochemical properties than those of the native enzyme including higher optimal temperature of 60°C, and specific activity, but lower optimal pH 4.0
additional information
truncated versions xynAS27cd (CBM-linker-truncated version) and xynAS27cdl (CBM-truncated version) show less pH and thermal stability, and less affinity and hydrolytic activity to insoluble substrate than the intact one
additional information
the catalytic domain is identified and truncated to remove the original signal peptide and linker region and to include an N-terminal hexahistidine tag and 3C protease cleavage site
additional information
-
the catalytic domain is identified and truncated to remove the original signal peptide and linker region and to include an N-terminal hexahistidine tag and 3C protease cleavage site
additional information
-
the catalytic domain is identified and truncated to remove the original signal peptide and linker region and to include an N-terminal hexahistidine tag and 3C protease cleavage site
-
additional information
-
the catalytic domain is identified and truncated to remove the original signal peptide and linker region and to include an N-terminal hexahistidine tag and 3C protease cleavage site
-
additional information
substitution of 31 N-terminal amino acids by thecorresponding region of 22 amino acid residues of the Bacillus subtilis xylanase A
additional information
-
substitution of 31 N-terminal amino acids by thecorresponding region of 22 amino acid residues of the Bacillus subtilis xylanase A
additional information
-
construction of an N-terminal replacement mutant
additional information
-
random mutagenesis leads to mutant M7 with improved kinetic and thermodynamic properties
additional information
fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus
additional information
-
the C-terminal carbohydrate binding module has only a slight effect, whereas a polyhistidine tag increases the thermostability of XYN10A
additional information
-
improving the thermostability of Trichoderma reesei xylanase 2 by introducing the thermostabilizing domain A2 from Thermotoga maritima XynA into the N-terminal region of the Xyn2 protein
additional information
construction of several mutant with increased number of arginines on the protein surface showing unaltered thermal stability but narrowed pH optimum, mutation of arginines to Ser/Thr causes a pH profile shift
additional information
-
construction of several mutant with increased number of arginines on the protein surface showing unaltered thermal stability but narrowed pH optimum, mutation of arginines to Ser/Thr causes a pH profile shift
additional information
-
increase in thermal stability in the mutants leads to increased pH stability as well, but also to reduced activity at both acidic and alkaline pH levels
additional information
-
improving the thermostability of Trichoderma reesei xylanase 2 by introducing the thermostabilizing domain A2 from Thermotoga maritima XynA into the N-terminal region of the Xyn2 protein
additional information
LC132960
the addition of a xylan-binding domain to the C-terminus of Xyn III improves its hydrolytic activity on insoluble xylan
additional information
-
the addition of a xylan-binding domain to the C-terminus of Xyn III improves its hydrolytic activity on insoluble xylan
additional information
-
improving the thermostability of Trichoderma reesei xylanase 2 by introducing the thermostabilizing domain A2 from Thermotoga maritima XynA into the N-terminal region of the Xyn2 protein
-
additional information
construction of truncated mutants, lacking the carbohydrate binding module CBM, which functions to selectively bind insoluble xylan and increase the rate of hydrolysis. Xyl1A corresponds to the GH11 domain coding sequence, Xyl1B corresponds to the GH11 and the CBM1 domain coding sequences, and Xyl1C corresponds to the two CBM coding sequences
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0 - 45
Pomacea insularus
-
pH 6.9, 10 min, stable
0 - 50
-
the retention of 50% of its maximum activity is observed at 0°C, retains 65% of its activity after 1-4 h incubation at 50°C
10
purified recombinant enzyme, pH 6.5, 40% remaining activity
110
-
60% of XylF2 activity is retained at 110°C
20
purified recombinant enzyme, pH 6.5, 65% remaining activity
20 - 50
purified recombinant enzyme, stable
20 - 60
-
more than 50% of the optimal xylanase activity is retained when the temperature is increased from 20 to 60°C after 240 min, at 40°C the xylanase maintains 93% of the optimal activity after a 240 min reaction, the enzyme retains 78.12% and 41.64% of the maximum activity at 50 and 60°C, respectively. at temperatures up to 60°C, xylanase activity decreases sharply with time
20 - 80
the enzyme remains completely stable from 20 to 50°C, while about 90 and 70% of the activity is retained at 60 and 70°C after 30 min. The melting temperature is 80°C
25
-
stable up to for at least 10 min, rapid inactivation above, isozymes A and B
30 - 45
-
3 h, completely stable
30 - 55
at temperatures below 30°C and above 55°C, enzyme activity is less than 50% of that at the optimal temperature
30 - 70
purified enzyme, 1 h, 65% activity remaining at 70°C, completely stable at 30-60°C, overview
4 - 50
-
1 h, pH 6.3, stable
40 - 50
-
purified extracellular enzyme, 2 h, over 80% activity remaining
40 - 60
-
purified isozyme EX1, stable at temperatures below 40°C, retains 50% activity after incubation at 50°C for 30 h, but it loses its activity rapidly at 60°C for 1 h
43
-
pH 6.0, 24 h, about 20% loss of activity
45 - 60
purified enzyme, pH 7.0, 60 min, 80% activity remaining
48
-
pH 5.5-5.6, half-life: 40 h
5 - 25
purified recombinant enzyme, 3 h, over 90% activity remaining
50 - 100
-
high thermal stability for 7 days, half-life of the xylanase at 100°C is 60 min
50 - 65
-
the half-lives of xylanase at 50°C and 65°C are approximately 200 and 50 min, respectively
50 - 80
retains more than 65% of the maximum activity
50 - 85
-
remains stable at 50°C for 20 min and at 85°C for 7 min
55 - 85
-
30 min, enzyme retains more than 70% of its initial activity
55.2
melting temperature of apoenzyme
56
-
9 h, more than 90% of maximal activity remains
57.3
apoenzyme with xylan
58.9
wild-type, melting temperature
60 - 65
-
marginally stable at temperatures above 60°C, with half-life of about 0.5 min at 65°C
60.1
apoenzyme with xylohexaose
64.6
mutant D65P/N66G, melting temperature
70 - 75
-
purified enzyme, 60 min, completely stable
70 - 90
Halalkalibacterium halodurans
-
stable up to 70°C, 2% and 16% of the original activity are retained after incubation at 80°C and 90°C, respectively
70.4
-
melting temperature, mutant N257D
70.9
-
melting temperature, wild-type and mutant Q158R
71.3
-
melting temperature, mutant H209N
74
melting temperature, mutant Q1C/Q24C
74.5
mutant S35C/T62C, melting temperature
81
-
half-life of xylanase A is 90 min, half-life of xylanase B is 2 min 30 s, half-life of xylanase C is 8 min
100
-
partially purified extracellular xylanase, inactivation after 120 min
100
30 min, 28% residual activity
100
Halalkalibacterium halodurans
-
3 h, no loss of activity
100
-
1 h, purified Xyl16-3, 50% remaining activity
100
-
half-life of 47 min at 100°C
100
-
pH 7.0, 10 min, about 40% loss of activity. pH 5.5, 10 min, complete inactivation
100
-
10 min, retains 50% of its activity at pH 6.1, retains 58% of its activity at pH 6.4, completly inactivated at pH 5.8
100
Thermomonospora sp.
-
half-life 15 min
100
15% remaining activity of recombinant N-terminal + catalytic domains
20 - 70
purified recombinant enzyme, 30 min, completely stable at 20-50°C, 90% activity is retained at 60°C, and 70% at 70°C, inactivation at 80°C
30
-
stable for up to 72 h
30
3 h, 50% loss of activity
30
purified recombinant enzyme, 3 h, loss of 50% activity
30
-
7 days, 55% loss of activity
30
-
stable at 30°C for 60 min, with more than 95% of the activity remaining
30
-
purified recombinant PgXynB is stable at 30 °C, pH 4.5 for 240 min, with more than 85% of the activity remaining
30
stable at 30°C for 60 min, with more than 95% of the activity remaining
30
Thermochaetoides thermophila
purified recombinant enzyme expressed from gene with intron, half-life is 1959 min
30
xylan as substrate, remains stable after treatment for 1 h
30 - 50
purified native, 30% activity remaining
30 - 50
purified native, stable at
30 - 50
-
purified enzyme, highly stable at
30 - 50
purified recombinant enzyme, pH 6.5, over 80% remaining activity, above 50°C the enzyme activity decreases rapidly after 10 min preincubation
30 - 50
purified recombinant RuCelA, 1 h, stable
35
1 h, 50% loss of activity
35
purified recombinant enzyme, 1 h, loss of 50% activity
35
-
pH 5.0, 10 min, stable at or below
37
1 h, more than 96% residual activity
37
-
pH 6.0, 24 h, stable
40
mutant T64S, 30 min, 77% resiudal activity
40
-
15 min, significant inactivation
40
-
purified native enzyme, pH 7.0, 120 min, 80% activity remaining
40
-
X-I and X-II are 100% stable after 1 h at 40°C
40
-
pH 5.0 or pH 8.5, 30 min, enzyme retains more than 85% of its activity
40
-
pH 6.0, 10 min, enzyme component I from strain W1, stable up to
40
20-30 min, complete inactivation
40
purified recombinant enzyme, 20-30 min, complete inactivation
40
C-terminal truncated mutant, loss of activity above 40°C
40
-
1 h, xylanase A is stable, 25% loss of activity of xylanase B
40
remains stable up to 40°C, loses its activity at 80°C
40
purified recombinant extracellular deglycosylated enzyme, 6 h, over 80% activity remains
40
purified recombinant enzyme, pH 6.0, 90 min, stable up to
40
-
1 h, inactivation above
40
purified recombinant enzyme, pH 6.5, 24 h, completely stable
40
-
4 h, 65% loss of activity
40
Thermochaetoides thermophila
purified recombinant enzyme expressed from gene with intron, half-life is 959 min
40
-
1 h, 20000 Da enzyme form is stable
40
-
2.2 h at 40°C and 2 min at 50°C
40
-
20 h, 10% loss of activity of xylanase I, xylanase II is stable
40
xylan as substrate, remains stable after treatment for 1 h
45
recombinant EGXA and wild-type EGX lose activity quickly when Cl- is at a low concentration. In the presence of 50 mM Cl-, the rtEGXAs activity loss is only 15% after 5 h incubation at 45°C. Wild-type EGX loses activity at a faster speed than the recombinant EGXA, in both 0.5 mM Cl- and 50 mM Cl-. Cellulose-binding domain increases thermal stability of the recombinant enzyme
45
1 h, the wild-type enzyme almost completely loses its activity
45
-
37.5% loss of activity after 90 min, stable up to 30 min
45
purified recombinant enzyme, 2 h, stable
45
-
1 h, 5% loss of activity
45
-
instable above, loss of secondary structure and activity
45
-
complete loss of activity within 5 min, isozymes A and B
45
purified recombinant extracellular deglycosylated enzyme, 70% activity remains after 30 min, 17% after 3 h, and 6% after 5 h
45
-
half-life of both isozymes is about 210 min
45
-
purified enzyme, 1 h, 91% activity remaining
45
purified recombinant enzyme, pH 6.0, 90 min, loss of 50% activity
45
Thermochaetoides thermophila
purified recombinant enzyme expressed from gene with intron, 10 min, 100% activity remaining
45
-
30 min, stable up to
45
-
pH 5.0, 4.5 h, 50% loss of activity
45
-
rapid loss of activity above
45 - 55
-
slight decrease in xylanase activity between 45°C (93.4%) and 55°C (97.7%). Enzyme activity is rapidly reduced to 59.3% when the temperature is at 60°C, and there is negligible activity (5.4%) above 80°C
45 - 55
purified recombinant enzyme, pH 5.0, stable for 120 min
50
-
half-life 120 h
50
-
pH 5, half-life: 16 min
50
30 min, 60% residual activity
50
purified extracellular enzyme, stable up to
50
-
xylanase I, half-life 22.5 min, xylanase II, half-life 17.5 min
50
-
stable for at least 90 min
50
-
purified native enzyme, pH 5.0-7.0, 86% residual activity after 45 min, the crude enzyme retains only 6% of the initial activity
50
-
87.5% loss of activity after 90 min
50
purified recombinant enzyme, half-life is 30 min
50
-
after 1 h 85.9% activity remaining, after 3 h 65.4% activity remaining
50
-
stable for several days
50
-
X-I retains more than 90% of hydrolytic activity after 1 h of heating at 50°C
50
is stable at temperatures up to 50°C. At 55°C, more than half of the activity is lost, and no activity remains at 60°C
50
-
partially purified extracellular xylanase, completely stable for 30 min, loss of 50% activity after 120 min
50
-
30 min, 50% loss of activity
50
-
pH 6.0, 10 min, enzyme component I from strain W2, stable up to
50
-
purified native enzyme, stable
50
the half-life of the recombinant protein at 50°C is 65 min whereas it is approximately 25 min at 60°C. The enzyme is not stable at 70°C and it loses almost all of its activity even 5 min after incubation
50
-
1 h, 24% loss of activity
50
30 min, 50% residual activity
50
stable below for at least 1 h
50
-
10 min, complete loss of activity
50
1 h, more than 40% resiudal activity
50
-
pH 6.7, 30 min, stable
50
-
pH 5-10, stable for 24 h, both isoforms xylanase IA and xylanase IIIA
50
-
10 min, 5% loss of activity
50
-
pH 5.4, 0.1 M NaCl, half-life: 7 min
50
recombinant His-tagged enzyme, 30 min, over 90% activity remaining
50
-
half-life of both isozymes is about 80 min
50
-
purified enzyme, 1 h, 70% activity remaining
50
-
isoform xynB, stable up to
50
purified recombinant enzyme, pH 6.0, 90 min, loss of 70% activity
50
purified enzyme, 2 h, stable
50
5 min, 40% residual activity
50
1 h, 90% residual activity
50
-
1 h, 60% residual activity
50
-
pH 6.0, 24 h, about 80% loss of activity
50
-
Xyl1-Xyl3 are stable for 16 h
50
purified recombinant enzyme, 1 h, 95% remaining activity, rapid decrease in activity above 60°C
50
5 min, 25% residual activity
50
-
isozyme III is stable below
50
-
12 weeks, more than 50% residual activity
50
-
90 min, 70% residual activity
50
Thermochaetoides thermophila
purified recombinant enzyme expressed from gene with intron, half-life is 176 min
50
Thermochaetoides thermophila
-
stable for 24 h, xylanase I, xylanase II
50
-
pH 7-8, stable for 7 days
50
stable for at least 4 h
50
-
24 h, 50% residual activity
50
-
pH 6.5, 51 h, 100% residual activity
50
t1/2: 173 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
50
t1/2: 693 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
50
-
pH 5.0, 24 h, 80% remaining activity
50
-
1 h, 29000 Da enzyme form is stable
50
-
20 h, 27% loss of activity of xylanase I and II
50
B2CNY5
over 85% activity remaining after 30 min
50
-
purified enzyme, 30 min, loss of less that 10% activity
50
B2CNY5
purified recombinant enzyme, 30 min, 94% activity remaining
50
xylan as substrate, remains stable after treatment for 1 h
50 - 60
-
the enzyme activity remains stable after 16 h at 50°C. At 60°C, the enzyme shows less than 40% activity after 3 h
50 - 60
remains stable at 50°C after incubation for 30 min at pH 7.8. More than 40% of the activity is retained after treating the enzyme at 60°C for 5 min
50 - 60
-
purified EX2, 48 h, 50% activity remaining
55
-
purified enzyme is stable for 44 h
55
-
isoform xyl I, half-life 27.3 min, xyl II, half-life above 90 min
55
1 h, mutant enzyme T205C/A52C retains more than 80% of its initial activity
55
-
pH 6.8, 15 min, stable up to
55
-
pH 5.3, stable for 3 days
55
-
30 min, 70% loss of activity, recombinant enzyme
55
-
sharp decline in activity above at pH 6.0
55
-
fully stable up to, 30 min, pH 5.0
55
purified recombinant enzyme, 60 min, 70% activity remaining
55
4 h, 65% residual activity
55
-
half-life of both isozymes is 50 min
55
-
half-life of the catalytic domain XYLA-A1 is 20 min, half-life of the catalytic domain XYLA-C2 is 50 min
55
-
10 min, stable up to
55
-
pH 5.5, 30 min, stable
55
-
isozymes I and II are stable below
55
-
10 days, about 90% residual activity
55
-
30 min, stable up to
55
-
10 days, about 90% residual activity
55
-
pH 10, stable for 5 h
55
LC132960
30 min, almost complete loss of activity for wild-type, 9% residual activity for mutant Q286A/N340Y
55
2 h, 90% residual activity
60
-
half-life 2 h
60
-
purified enzyme is stable for 1 h
60
purified recombinant XynA4, 1 h, pH 7.0, over 90% activity remaining, half-life is 394 min
60
purified native, inactivation
60
-
30 min, 40% residual activity
60
-
xylanase I, half-life 1.5 min, xylanase II, half-life 1.5 min
60
-
half-life of 115 min
60
-
X-II retains more than 90% of hydrolytic activity after 1 h of heating at 60°C
60
-
partially purified extracellular xylanase, loss of 10% activity after 60 min, loss of 55% activity after 120 min
60
-
complete inactivation in 15 min
60
purified recombinant enzyme, 1 h, over 50% activity remaining
60
-
pH 5.3, 93% loss of activity after 1 day
60
-
pH 6.0, 10 min, enzyme component II from strain W1 and W2, stable up to
60
-
purified enzyme, 5 h, 95% activity remaining
60
-
50% final residual activity in presence of 0.5 M trehalose as well as 8fold increased half-life of XylII and 2.5fold of XylI, inactivation in absence of trehalose
60
-
the wild type enzyme completely loses activity after preincubation at 60°C
60
glycosylated recombinant enzyme, 30 h, 50% remaining activity. Unglycosylated native enzyme, 12 h, 50% activity remaining
60
purified recombinant enzyme, 60 min, pH 3.0, 98% remaining activity
60
purified recombinant enzyme, 80% activity remaining
60
-
loss of 78% activity after 30 min at pH 5.0
60
-
45 min, xylanase 2 completely loses activity, xylanase 1 retains 50% of its activity
60
-
pH 5.0, 10 min, stable up to
60
purified recombinant enzyme, 60 min, 30% activity remaining
60
-
retains approximately 97% of its relative activity following incubation for 4 h
60
1 h, 80% residual activity
60
-
isozyme IIb shows a half-life of 94.5 min, isozyme IId of 85.6 min, isozyme Ia of 164.3 min
60
-
purified extracellular enzyme, 2 h, loss of 80% activity, half-life is 20 min
60
-
purified enzyme, 1 h, 50% activity remaining
60
-
isoforms xynA, xynC, stable for 30 min
60
purified recombinant enzyme, pH 6.0, 90 min, inactivation
60
-
purified PhX20, half-life is 10 min
60
purified enzyme, half-life is 180 min
60
1 h, 16% residual activity
60
-
half-lives: Xyl1 10 min, Xyl2 30 min, Xyl3 70 min
60
purified recombinant enzyme, pH 6.5, 60 min, stable
60
-
97 h, retains full activity
60
-
retains full activity for 97 h
60
Thermochaetoides thermophila
purified recombinant enzyme expressed from gene with intron, half-life is 72 min
60
Thermochaetoides thermophila
120 min, enzyme retains about 85% of its initial activity, xylanase ativity
60
Thermochaetoides thermophila
120 min, enzyme retains more than 80% of its initial activity, endoglucanase activity
60
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, 90% activity remaining after 120 min
60
-
4 days, 10% loss of activity
60
-
stable for more than 48 h
60
-
3 h, no loss of activity
60
-
4 h, 50% residual activity
60
96 h, 80% residual activity
60
-
pH 5-9, stable for 5 h
60
t1/2: 16 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
60
t1/2: 347 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
60
-
recombinant mutant hybrid enzyme, 30 min, over 85% activity remaining
60
-
20 h, 84% loss of activity of xylanase I, 76% loss of activity of xylanase II
60
B2CNY5
over 65% activity remaining after 30 min
60
-
purified enzyme, 30 min, loss of about 70% activity
60
-
recombinant mutant hybrid enzyme, 30 min, over 85% activity remaining
60
LC132960
30 min, 51% residual activity, mutant Q286A/N340Y
60
-
10 min, complete loss of activity
60
Xyn11 in its apo form, is not subject to thermal inactivation up to 60°C
60
purified recombinant RuCelA, 1 h, 60% activity remaining
60
xylan as substrate, remains 60% activity after treatment for 1 h
60 - 70
-
purified recombinant XynS14s, 12 h, completely stable
60 - 70
Halalkalibacterium halodurans
-
stable up to 60°C, retains 30% of original activity after incubation at 70°C
60 - 70
thermostability of the recombinant catalytic domain is decreased to 60°C in absence and increased to 70°C in presence of the recombinant N-terminal thermostabilizing domain D1
65
purified recombinant XynA4, half-life is 17 min
65
-
1 h, 50% residual activity
65
1 h, pH 10, 100% residual activity
65
-
pH 7.0, 10 h, stable, pH 9.0, half-life is 6 h
65
-
1 h, 43% residual activity
65
20 min, wild-type, 70% loss of activity, mutant N38Y/F52W/G56Y/G201L, about 10% loss of activity
65
-
purified native enzyme, half-life is 415.12 min
65
MK331807
1 h, no loss of activity
65
purified recombinant enzyme, 1 h, 70% remaining activity
65
-
recombinant His-tagged enzyme, 30 min, completely stable up to
65
Thermothelomyces fergusii
-
1 h, 61% residual activity
65
-
1 h, 90% residual activity
65
-
6 h, 80% residual activity
65
-
30 min, 90% loss of activity
65
-
half-lives: wild-type enzyme below 1 min, S110C/N154C 14 min, S110C/N154C/Q162H and S110C/N154C/Q162Y 63 min, S110C/N154C/Q162H/N11D 107 min, S110C/N154C/Q162Y/N11D 97 min, S110C/N154C/Q162H/N11D/N38D 112 min
65
-
30 min, complete inactivation
66
-
half-life: 3 min
66
melting temperature, wild-type
70
2 h, 87% activity of mutant Xyn-BDC is remaining, 42% of mutant Xyn-BDC
70
2 h, mutant Xyn-C loses all activity, while mutant XynC-BC retains 70% activity
70
purified recombinant XynA4, half-life is 3 min
70
1 h, complete loss of activity for wild-type, 46% residual activity for mutant T16A/T39I/L176Q, 33% for mutant A60D, 25.8% for mutant S68R, 23.8% for mutant Q47P/S159R
70
10 min, complete loss of activity
70
-
the recombinant enzyme is stable below 70°C, enzyme activity is rapidly lost above 70°C, the residual activity of the recombinant BlxA is 76% at 70°C and pH 6.0 after 2 min
70
-
partially purified extracellular xylanase, loss of 80% activity after 120 min
70
-
complete inactivation after 1 day
70
-
pH 6.0, 4 h, 20% loss of activity in presence of xylan, 80% loss of activity without xylan
70
-
4 h, in presence of xylan, 20% loss of activity
70
-
4 h, 20% activity remaining
70
-
purified enzyme, 5 h, 82% activity remaining
70
-
35% final residual activity in presence of 0.5 M trehalose as well as 2fold increased half-lives of XylII and XylI, inactivation in absence of trehalose
70
glycosylated recombinant enzyme, 1 h, 90% remaining activity
70
-
the thermostable variant XynAG3 loses 90% of its activity after 10 min, and after 30 min no activity is observed. The chimeric CotA-XynAG3 retains 60% activity after 10 min and about 20% activity after 120 min. The half-lives of the chimeric enzymes XynAG3 and CotA-XynAG3 are 2.2 and 21 min
70
3 h, immobilized enzyme retains 45.3% of its activity, soluble enzyme retains 16.3% of its activity
70
-
pH 6.0, half-life: 4 min in absence of added protein, 30 min, in presence of 0.5 mg/ml bovine serum albumin
70
-
pH 7.0, half-life is 14.5 h
70
-
pH 5.0, 10 min, inactivated
70
purified recombinant enzyme, 60 min, 10% activity remaining
70
-
isozyme Ia shows a half-life of 16.7 min, isozyme IId of 15.6 min
70
purified enzyme, pH 7.0, 60 min, 55% activity remaining
70
recombinant His-tagged enzyme, half-life is 174.8 min
70
-
purified native enzyme, half-life is 102.8 min
70
-
24 h, more than 70% residual activity
70
-
purified enzyme, 15 min, 68% activity remaining
70
-
isoforms xynA, xynB, xynC, complete inactivation in 30 min
70
XYN10G, about 90% of activity remaining after 1 h, 37°C
70
-
purified PhX33, half-life is 15 min
70
-
pH 5.5, 5 min, xylanase X-a, X-b-I and X-b-II, stable up to
70
1 h, 56% residual activity (small enzyme form RrXyn11A S), 1 h, 65% residual activity (larger enzyme form RrXyn11A L)
70
purified enzyme, half-life is 120 min
70
purified heavier protein band (42.8 kDa), retains more than 40% after a 1 h incubation at 70°C. Retains 35% of its activity after a 1 h incubation at 87°C
70
MK331807
1 h, 15% loss of activity
70
-
30 min, complete inactivation
70
purified recombinant enzyme, 1 h, 45% remaining activity
70
purified recombinant enzyme, 180 min, no loss of activity
70
-
1 h, complete loss of activity
70
-
24 h, retains full activity
70
-
retains full activity for 24 h
70
-
both recombinant TfxA and mutant 2TfxA98 are stable at 70°C during 30 min incubation, although the mutant is slightly less stable than the parent at 70°C after 30 min of incubation
70
Thermochaetoides thermophila
purified recombinant enzyme expressed from gene with intron, half-life is 39.4 min
70
Thermochaetoides thermophila
60 min, enzyme retains 66.2% of its initial activity, xylanase ativity
70
Thermochaetoides thermophila
60 min, enzyme retains 74.3% of its initial activity, endoglucanase activity
70
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, half-life of endoxylanase activity is 100 min, 40% activity remaining after 120 min
70
-
10 min, xylanase A, stable
70
80 min, 60% remaining activity, native and recombinant enzyme
70
-
mutant enzyme retains over 50% activity after 2 h
70
-
30 min, stable up to. 120 min, 67% residual activity
70
80 min, 60% residual activity
70
wild-type at pH 8.0, half-life 11 min in presence of substrate, 33 min in absence of substrate, respectively. Mutant Q1C/Q24C at pH 8.0, half-life 229 min in presence of substrate, 315 min in absence of substrate, respectively. Mutant Q1C/Q24C at pH 9.0, half-life 112 min in presence of substrate, 169 min in absence of substrate, respectively
70
t1/2: 15 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
70
t1/2: 231 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
70
purified recombinant enzyme, 30 min, 60% activity remaining
70
-
20 h, complete inactivation
70
-
10 min: inactivation of mutant S110C/N154C, 50-60% remaining activity of mutants S110C/N154C/Q162H/N11D, S110C/N154C/Q162Y/N11D, and S110C/N154C/Q162H/N11D/N38D
70
-
purified enzyme, 30 min, loss of over 90% activity
70
-
purified recombinant enzyme, loss of 60% activity after 30 min
70
purified recombinant RuCelA, 1 h, almost no activity remaining
70
xylan as substrate, almost loses its activity after treatment for 1 h
75
-
pH 6.8, 15 min, nearly all activity is destroyed
75
-
15 min, inactivation
75
-
pH 7.0, half-life is 20 min
75
30 min, stable up to 75°C
75
recombinant His-tagged enzyme, half-life is 137.9 min
75
2 h, 75% resiudal activity
75
-
1 h, xylanase A and C are stable, xylanase B retains 85% of its activity
75
-
30 min, 80% loss of activity
80
-
XynS14 expressed from Pichia pastoris shows 50% remaining activity after 2 h, the enzyme expressed from Escherichia coli shows 30% remaining activity. In the presence of sorbitol at 90% and glycerol at 50%, the enzyme retains approximately 70% and 80% activity, respectively, at 80°C for 4 h
80
-
15 min, complete inactivation
80
-
15 min, xylanase IA and Ib are rapidly inactivated above, xylanase II is completly inactivated
80
-
22% activity remaining
80
-
partially purified extracellular xylanase, loss of 85% activity after 120 min
80
-
15 min, complete loss of activity
80
glycosylated recombinant enzyme, 1 h, 86% remaining activity
80
purified recombinant enzyme, 5 min, pH 3.0, 25% remaining activity
80
purified recombinant Xyl10C, 60 min, completely stablem half-life is 45 h
80
-
pH 6.0, half-life is 20 min in presence of 0.5 mg/ml bovine serum albumin
80
Halalkalibacterium halodurans
wild-type, half-life 35 min, recombinant glycosylated enzyme, half-life 45 min
80
-
all isozymes are inactivated within 10 min
80
purified enzyme, pH 7.0, 60 min, 10% activity remaining
80
-
purified enzyme, 60 min, 80% activity remaining
80
purified enzyme, inactivation
80
purified recombinant enzyme, 10 min, loss of 80% activity
80
Thermochaetoides thermophila
retains 35% enzyme activity. The enzyme shows half lives of 1100, 330, 86, 70, 19.3 and 11.4 min at 30, 40, 50, 60, 70 and 80°C, respectively
80
Thermochaetoides thermophila
purified recombinant enzyme expressed from gene with intron, half-life is 18.7 min
80
Thermochaetoides thermophila
60 min, enzyme retains 61.3% of its initial activity, endoglucanase activity
80
Thermochaetoides thermophila
60 min, enzyme retains about 50% of its initial activity, xylanase ativity
80
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, half-life of endoxylanase activity is 40 min, 10% activity remaining after 80 min, inactivation after 120 min
80
-
enzyme begins to denature at around 80°C
80
Thermomonospora sp.
-
half-life 86 min
80
40 min, 60% remaining activity, native and recombinant enzyme
80
-
loses 90% activity after 10 min at 80°C
80
40 min, 60% residual activity
80
t1/2: 12 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
80
t1/2: 63 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
80
-
recombinant His-tagged enzyme, 30 min, 50% activity remaining
80
-
24% remaining activity
80
8 h, enzyme remains stable
80.5
melting temperature
80.5
mutant S35C/N44H/Y61M/T62C/N63L/D65P/N66G/T101P/S102N, melting temperature
85
purified recombinant Xyl10C, half-life is 3 h
85
recombinant His-tagged enzyme, 30 min, over 60% activity remaining, half-life is 68.2 min
85
-
purified enzyme, 60 min, 40% activity remaining
85
12% remaining activity of recombinant catalytic domain
90
-
half-life is 1.5 h in presence of xylan
90
-
pH 5.0, 10 min, 40% residual activity
90
-
X-I presents 50% activity at 90°C, and X-II presents 80% activity at the same temperature
90
-
partially purified extracellular xylanase, loss of 90% activity after 120 min
90
purified recombinant Xyl10C, 10 min, 87% remaining activity
90
Halalkalibacterium halodurans
-
half-life 60 h
90
purified enzyme, pH 7.0, 60 min, 5% activity remaining
90
-
purified enzyme, half-life is 30 min, 20% activity remaining after 60 min
90
-
50% maximal activity is measured after 85 min at 90°C, 23% residual activity after 3 h at 90°C
90
purified recombinant enzyme, 20 min, inactivation
90
30 min, more than 10% residual activity, recombinant protein, both with and without His-tag
90
Thermochaetoides thermophila
40 min, enzyme retains about 28% of its initial activity, endoglucanase activity
90
Thermochaetoides thermophila
60 min, enzyme retains about 30% of its initial activity, xylanase ativity
90
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, half-life of endoxylanase activity is 30 min, inactivation after 80 min
90
Thermomonospora sp.
-
half-life 30 min
90
-
30 min, complete inactivation
90
t1/2: 12 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, endoglucanase activity
90
t1/2: 20 min, fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus, xylanase activity
95
-
5 min, enzyme form X-a retains 65% of the original activity, enzyme form X-b-I retains 65% of the original activity, enzyme form X-b-II retains 65% of the original activity
95
-
t1/2: 5 min, xylanase a
95
-
recombinant His-tagged enzyme, 30 min, 10% activity remaining
95
60% remaining activity of recombinant N-terminal + catalytic domains
additional information
thermostablitiy increases by 30-50% when 2 M sorbitol is added
additional information
-
thermostablitiy increases by 30-50% when 2 M sorbitol is added
additional information
-
K+ stabilizes against thermal inactivation
additional information
-
trehalose stabilizes both isozymes at 60°C and 70°C and increases the enzyme activity, thermal deactivation kinetics of enzyme forms XylI and XylII
additional information
-
very low thermostability of isozymes A and B
additional information
-
half-lives of the 7 isozymes at different temperatures, isozyme Ia is the most stable, overview
additional information
thermal denaturation measurements, circular dichroism, overview
additional information
-
thermal denaturation measurements, circular dichroism, overview
additional information
Tm of wild-type and mutant enzymes
additional information
the absence of the xylan-binding domain results in a decrement of 40% in thermostability
additional information
psychrophilic enzyme with high activity at low temperatures and low thermal stability
additional information
-
the C-terminal carbohydrate binding module has only a slight effect, whereas a polyhistidine tag increases the thermostability of XYN10A
additional information
-
features that account for the high thermostability of enzyme are clusters of aromatic residues together with a lack of exposed hydrophobic residues
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
agriculture
-
unprocessed Xyn2, supplemented to a xylan-containing diet for weaned pigs, results an average body-weight gain increased by 16.9% with added Xyn2 at a concentration of 500 U/kg diet
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
analysis
enzyme coupled assay procedure, using substrate 4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] and release of 4-nitrophenol by beta-xylosidase
analysis
enzyme coupled assay procedure, using substrate 4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] and release of 4-nitrophenol by beta-xylosidase
analysis
enzyme coupled assay procedure, using substrate 4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] and release of 4-nitrophenol by beta-xylosidase
biofuel production
-
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently
biofuel production
-
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently
biofuel production
-
pre-treatment for ethanol formation from lignin-cellulose fibres more efficiently
biofuel production
RuCelA can produce xylo-oligosaccharides and cell-oligosaccharides in the continuous saccharification of pretreated rice straw, which can be further degraded into fermentable sugars. Therefor, the bifunctional RuCelA distinguishes itself as an ideal candidate for industrial application
biofuel production
the enzyme is a candidate for the utilization of agro-industrial waste for fuel production
biofuel production
potential applications on biofuels and paper industries
biofuel production
the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone
biofuel production
-
potential applications on biofuels and paper industries
-
biofuel production
-
the enzyme is a candidate for the utilization of agro-industrial waste for fuel production
-
biotechnology
-
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
-
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
biotechnology
increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
degradation
-
the substrate binding site of Xyn11A probably contains six subsites. Aromatic residues Tyr165, Trp9, Tyr69, Tyr80, Tyr65, Tyr88 and Tyr173 play an important role in the six subsites of Xyn11A
degradation
enzyme is able to degrade pulp and release substantial chromophoric materials and lignin derived compounds indicating its effective utility in pulp bleaching
degradation
Abf51A shows greater synergistic effect in combination with xylanase (2.92fold) on wheat arabinoxylan degradation than other reported enzymes, the amounts of arabinose, xylose, and xylobiose are all increased in comparison to that by the enzymes acting individually
degradation
Halalkalibacterium halodurans
agroresidues subjected to alkali and microwave irradiation for 6 min in order to expose the polysaccharide component to enzymatic hydrolysis lead to increased relase of sugars. The maximum sugar content is detected in the hydrolysate of microwave-irradiated wheat bran (6.20 mg/g substrate) followed by wheat straw (4.9 mg/g substrate)
degradation
-
co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles
degradation
during degradation of bagasse, hemicellulose content, especially arabinan, and the cellulose crystallinity of bagasse affects the synergism of degrading enzymes cellulase and xylanase. Higher synergism (above 3.4) is observed for glucan conversion, at low levels of arabinan (0.9%), during the hydrolysis of peracetic acid pretreated bagasse. In contrast, 1-ethyl-3-methylimidazolium acetate pretreated bagasse shows lower cellulose crystallinity and achieves higher synergism (over 1.9) for xylan conversion. The combination of Thermobidfida endoglucanase Cel6A and xylanase Xyn11A results in higher synergism for glucan conversion than the combination of Cel6A with Clostridium thermocellum XynZ-C
degradation
during degradation of bagasse, hemicellulose content, especially arabinan, and the cellulose crystallinity of bagasse affects the synergism of degrading enzymes cellulase and xylanase. Higher synergism (above 3.4) is observed for glucan conversion, at low levels of arabinan (0.9%), during the hydrolysis of peracetic acid pretreated bagasse. In contrast, 1-ethyl-3-methylimidazolium acetate pretreated bagasse shows lower cellulose crystallinity and achieves higher synergism (over 1.9) for xylan conversion. The combination of Thermobidfida endoglucanase Cel6A and xylanase Xyn11A results in higher synergism for glucan conversion than the combination of Cel6A with Clostridium thermocellum XynZ-C
degradation
hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilizedon commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed
degradation
-
immobilization of enzyme within calcium alginate beads using entrapment technique. Temperature (50°C) and pH (7.0) optima of immobilized enzyme remain same, but enzyme-substrate reaction time increases from 5.0 to 30.0 min as compared to free enzyme. The diffusion limit of high molecular weight xylan (corncob) causes a decline in Vmax of immobilized enzyme from 4773 to 203.7 U/min, whereas the Km value increases from 0.5074 to 0.5722 mg/ml. Immobilized endo-beta-1,4-xylanase is stable even at high temperatures and retains 18 and 9% residual activity at 70°C and 80°C, respectively. The immobilized enzyme also exhibits sufficient recycling efficiency up to five reaction cycles
degradation
immobilizazion of enzyme on various supports. Most active immobilized enzyme is achieved when Xyl2 is covalently bound to low functionalized agarose matrices, poorer activity is observed for Xyl2 immobilized on highly functionalized agarose or on nickel-affinity resin
degradation
pretreatments with alkali or acid significantly increase the relative release of pentose sugars, especially in alkali-pretreated canola meal (about 44%) and mustard bran (about 72%). The amounts of pentosan (g/100 g) in acid- and alkali-pretreated canola meal are 7.50 and 8.21 and in corresponding mustard bran are 8.67 and 10.39, respectively. These pretreated substrates produced a pentose content (g/100 g) of 2.10 in 18 h and 2.95 in 24 h, respectively, during hydrolysis. The main oligosaccharides in the hydrolyzates of alkali-pretreated substrates are xylo-glucuronic acid and xylobiose
degradation
-
the combination of Axy43A and Paenibacillus curdlanolyticus B-6 endo-xylanase Xyn10C greatly improves the efficiency of xylose and arabinose production from the highly substituted rye arabinoxylan
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
-
crude thermostable cellulases and xylanase hydrolyze phosphoric acid-swollen wheat straw, avicel and untreated xylan up to 74, 71 and 90 %, respectively
degradation
-
degradation of alpha-amylase-treated wheat bran by xylanase solubilises about 20% of the fibre residue, i.e. 10% of the original bran. Amylase, protease and xylanase treatments alter the composition of the original bran, removing starch (100%), a portion of the non-starch glucan (39%), xylan (57%), arabinan (61%), ash (62%) and other components including protein (52%). Pre-extraction of enzymatically-hydrolysable starch and xylan reduces the release of furfural. Steam explosion of the lignocellulosic residue followed by cellulase treatment and conversion to ethanol at a high substrate concentration (19%) gives an ethanol titre ofabout 25 g/l or a yield of 93% of the theoretical maximum
degradation
-
enzymatic treatment of kraft pulp with xylanase and laccase decreases the amount of chlorine needed for bleaching. Pretreatment of pulp followed by a chemical treatment with 3% NaOCl gives the same results as with chemicals at 7% NaOCl, resulting in 42% reduction in chlorine consumption
degradation
-
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase
degradation
-
maximum saccharification is obtained from treatment of cane bagasse by partially purified xylanase from Thermomyces lanuginosus A72 and Thermomyces lanuginosus YMN72 after 24 hrs of incubation. The maximum production of ethanol and xylitol is obtained after 48 and 24 h fermentation giving 22.48 g/l and 13.54 g/l, respectively, in enzyme broth of Thermomyces lanuginosus YMN72 using Candida tropicalis EMCC2
degradation
KU366607
optimization of xylanase production using agro-industrial substrates. Pretreated rice straw yields 126.9 mg/g maximum fermentable sugars
degradation
-
treatment of Eucalyptus kraft pulp with culture supernatant at 10 IU per gram pulp to enhance bleaching of kraft pulp results in a 10.5% reduction in Kappa number (indicating the amount of chemicals needed for bleaching pulps) and has a positive effect on the brightness of the resulting handsheets
degradation
-
using enzymatic extract from Myceliophthora thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively
degradation
-
application in enzymatic hydrolysis for sugars production from lignocellulosic biomass. On empty fruit bunch as a feedstock, the total sugars conversion is 3.8%, and the conversion after alkaline pretreatment is approximately 16fold improved (61.1%)
degradation
-
application of enzyme for biobleaching of Eucalyptus kraft pulp, the xylanase increases the brightness of the pulp by 14.5% and reduces the kappa number by 24.5%
degradation
-
enzyme can be used for hydrolysis of pretreated agro-wastes. Sugarcane juice substituted medium yields maximum (52.19%) reducing sugar, followed by bioethanol production (4.19 g/l) at 72 h of incubation
degradation
when a fusion protein with the carbohydrate-binding domain of xylanase XynZ from Clostridium thermocellum supplements the commercial cocktail Accellerase1 1500, reducing sugar release is improved by 17% from pretreated sugarcane bagasse
degradation
-
the substrate binding site of Xyn11A probably contains six subsites. Aromatic residues Tyr165, Trp9, Tyr69, Tyr80, Tyr65, Tyr88 and Tyr173 play an important role in the six subsites of Xyn11A
-
degradation
-
during degradation of bagasse, hemicellulose content, especially arabinan, and the cellulose crystallinity of bagasse affects the synergism of degrading enzymes cellulase and xylanase. Higher synergism (above 3.4) is observed for glucan conversion, at low levels of arabinan (0.9%), during the hydrolysis of peracetic acid pretreated bagasse. In contrast, 1-ethyl-3-methylimidazolium acetate pretreated bagasse shows lower cellulose crystallinity and achieves higher synergism (over 1.9) for xylan conversion. The combination of Thermobidfida endoglucanase Cel6A and xylanase Xyn11A results in higher synergism for glucan conversion than the combination of Cel6A with Clostridium thermocellum XynZ-C
-
degradation
-
when a fusion protein with the carbohydrate-binding domain of xylanase XynZ from Clostridium thermocellum supplements the commercial cocktail Accellerase1 1500, reducing sugar release is improved by 17% from pretreated sugarcane bagasse
-
degradation
-
application of enzyme for biobleaching of Eucalyptus kraft pulp, the xylanase increases the brightness of the pulp by 14.5% and reduces the kappa number by 24.5%
-
degradation
-
enzyme is able to degrade pulp and release substantial chromophoric materials and lignin derived compounds indicating its effective utility in pulp bleaching
-
degradation
-
immobilization of enzyme within calcium alginate beads using entrapment technique. Temperature (50°C) and pH (7.0) optima of immobilized enzyme remain same, but enzyme-substrate reaction time increases from 5.0 to 30.0 min as compared to free enzyme. The diffusion limit of high molecular weight xylan (corncob) causes a decline in Vmax of immobilized enzyme from 4773 to 203.7 U/min, whereas the Km value increases from 0.5074 to 0.5722 mg/ml. Immobilized endo-beta-1,4-xylanase is stable even at high temperatures and retains 18 and 9% residual activity at 70°C and 80°C, respectively. The immobilized enzyme also exhibits sufficient recycling efficiency up to five reaction cycles
-
degradation
-
immobilizazion of enzyme on various supports. Most active immobilized enzyme is achieved when Xyl2 is covalently bound to low functionalized agarose matrices, poorer activity is observed for Xyl2 immobilized on highly functionalized agarose or on nickel-affinity resin
-
degradation
-
optimization of xylanase production using agro-industrial substrates. Pretreated rice straw yields 126.9 mg/g maximum fermentable sugars
-
degradation
-
co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles
-
degradation
-
using enzymatic extract from Myceliophthora thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively
-
degradation
-
enzyme can be used for hydrolysis of pretreated agro-wastes. Sugarcane juice substituted medium yields maximum (52.19%) reducing sugar, followed by bioethanol production (4.19 g/l) at 72 h of incubation
-
degradation
-
enzymatic treatment of kraft pulp with xylanase and laccase decreases the amount of chlorine needed for bleaching. Pretreatment of pulp followed by a chemical treatment with 3% NaOCl gives the same results as with chemicals at 7% NaOCl, resulting in 42% reduction in chlorine consumption
-
degradation
-
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase
-
degradation
-
the combination of Axy43A and Paenibacillus curdlanolyticus B-6 endo-xylanase Xyn10C greatly improves the efficiency of xylose and arabinose production from the highly substituted rye arabinoxylan
-
degradation
Halalkalibacterium halodurans TSEV1
-
agroresidues subjected to alkali and microwave irradiation for 6 min in order to expose the polysaccharide component to enzymatic hydrolysis lead to increased relase of sugars. The maximum sugar content is detected in the hydrolysate of microwave-irradiated wheat bran (6.20 mg/g substrate) followed by wheat straw (4.9 mg/g substrate)
-
degradation
-
crude thermostable cellulases and xylanase hydrolyze phosphoric acid-swollen wheat straw, avicel and untreated xylan up to 74, 71 and 90 %, respectively
-
degradation
-
application in enzymatic hydrolysis for sugars production from lignocellulosic biomass. On empty fruit bunch as a feedstock, the total sugars conversion is 3.8%, and the conversion after alkaline pretreatment is approximately 16fold improved (61.1%)
-
food industry
-
changes in arabinoxylan during the breadmaking process are to a large extent caused by endogenous endoxylanases, whereas the contribution of microbial endoxylanases to these changes are very low. Endogenous endoxylanases affect the arabinoxylan population only during the fermentation phase and not during the mixing phase of breadmaking. Endoxylanases can, on the one hand, positively affect bread volume by solubilization of water unextractable arabinoxylan, but they can, on the other hand, also lead to unwanted stickiness
food industry
contribution of microbial endoxylanases to changes in arabinoxylan during the breadmaking process are very low. Microbial endoxylanases end up in flour as contaminant and affect its functional properties
food industry
contribution of microbial endoxylanases to changes in arabinoxylan during the breadmaking process are very low. Microbial endoxylanases end up in flour as contaminant and affect its functional properties
food industry
-
high levels of endoxylanase activity in wheat flour should be avoided as they can cause uncontrolled degradation of arabinoxylan during bread dough processing, glutenstarch separation, or refrigerated dough storage
food industry
high levels of endoxylanase activity in wheat flour should be avoided as they can cause uncontrolled degradation of arabinoxylan during bread dough processing, glutenstarch separation, or refrigerated dough storage
food industry
high levels of endoxylanase activity in wheat flour should be avoided as they can cause uncontrolled degradation of arabinoxylan during bread dough processing, glutenstarch separation, or refrigerated dough storage
food industry
improvement of cereal-based industrial processing by endoxylanase enzymes insensitive towards inhibitors
food industry
-
wheat flour-associated endoxylanases are not active during dough mixing but exert their main effect during the fermentation phase of bread making. Wheat flour-associated endoxylanases can alter part of the arabinoxylan in dough, thereby changing their functionality in bread making and potentially affecting dough and end product properties
food industry
-
endogenous endoxylanase activity during fermentation and storing can have negative effects on dough, the enzyme effect depends on the wheat variety's enzyme content and inhibitor content
food industry
-
extraction of pectins from apple pomace with monoactive preparation of endoxylanase and endocellulase. Endoxylanase application results in the highest extraction efficiency of pectins (19.8%). The obtained polymer was characterised by a very high molecular mass, high level of neutral sugars (mainly arabinose, galactose and glucose), and very high degree of pectin methylation (73.4). The simultaneous application of both enzymatic preparations results in their cooperation, leading to a decrease of both the extraction efficiency and the molecular mass of pectin. This pectin is distinguished by the highest GalA (74.7%) and rhamnose contents
food industry
-
extraction of pectins from apple pomace with monoactive preparation of endoxylanase and endcellulase. Pectin extracted with endocellulase has 1.5fold lower molecular mass but contains significantly more galacturonic acid (70.5%) of a high degree of methylation (66.3%). The simultaneous application of both enzymatic preparations results in their cooperation, leading to a decrease of both the extraction efficiency and the molecular mass of pectin. This pectin displays the highest galacturonic acid (74.7%) and rhamnose contents
food industry
use of enzyme as an additive in the bread making process leads to a decrease in firmness, stiffness and consistency, and improvements in specific volume and reducing sugar content
food industry
-
application of the extremely thermo- and alkali-stable enzyme for preparation of prebiotic xylooligosaccharides
food industry
-
fruit juice clarification potential of GC25 xylanase at mild conditions. Pediococcus acidilactici strain GC25 xylanase causes a high increase in reducing sugar content after 30 min incubation at 40°C
food industry
MK331807
the ability of the enzym to produce xylobiose from agricultural and forestry residues proves that it is an excellent candidate enzyme in prebiotic and alternative sweetener industries
food industry
the enzyme is important for industrial applications such as pretreatment of poultry cereals, bio-bleaching of wood pulp and degradation of plant biomass
food industry
xylooligosaccharide derived from enzymatic hydrolysis of biopolymers is of considerable importance in preparing nutritional health oligosaccharides useful in food and pharmaceutical industries. To create added value products from hardwood xylan, xylanase (XynB) and alpha-glucuronidase (AguA) from Thermotoga maritima were co-produced in Escherichia coli through dual-promoter and bicistronic constructs
food industry
-
the enzyme is important for industrial applications such as pretreatment of poultry cereals, bio-bleaching of wood pulp and degradation of plant biomass
-
food industry
-
application of the extremely thermo- and alkali-stable enzyme for preparation of prebiotic xylooligosaccharides
-
food industry
-
fruit juice clarification potential of GC25 xylanase at mild conditions. Pediococcus acidilactici strain GC25 xylanase causes a high increase in reducing sugar content after 30 min incubation at 40°C
-
food industry
-
xylooligosaccharide derived from enzymatic hydrolysis of biopolymers is of considerable importance in preparing nutritional health oligosaccharides useful in food and pharmaceutical industries. To create added value products from hardwood xylan, xylanase (XynB) and alpha-glucuronidase (AguA) from Thermotoga maritima were co-produced in Escherichia coli through dual-promoter and bicistronic constructs
-
food industry
-
the enzyme is important for industrial applications such as pretreatment of poultry cereals, bio-bleaching of wood pulp and degradation of plant biomass
-
industry
-
used for pulp bleaching
industry
-
application as a pre-bleaching aid of apparent importance for pulp and paper industries
industry
-
DNA shuffling improves the catalytic activity and alkaline pH stability of Thermobifida fusca xylanase A toward the hydrolysis of xylan evolved enzyme 2TfxA98 can meet the requirements of biobleaching by its stability and activation under conditions of alkaline and high temperatures
industry
favorable properties of XynAS9, such as high activity over a wide temperature range, good thermal and pH stability, and less complex hydrolysis products, make this xylanase promising for various applications in the animal feed and biofuel industries
industry
high production yields of the modular xylanase Xyl30 by solid-state fermentation and its biochemical features make it a good candidate for use in industrial applications
industry
Thermochaetoides thermophila
is thermostable in alkaline buffer favoring its suitability to bio-bleaching of kraft pulp. Xylanases that are more active in pH range of 6.0-10.0 can act as promising agents in paper and pulp industry. Productivity profiles of xylanase in Escherichia coli recombinant are more than 4fold of that produced from Trichoderma reesei RUTC-30, 5fold of that produced by the donor and significantly higher than the values reported on other Escherichia coli, and Saccharomyces cerevisiae recombinants
industry
-
oligoglycosides have excellent properties as both surfactants and biodegradability enhancers, whereby Xyn1 is probably useful for such synthesis, since Xyn1 has high transglycosylation activity
industry
-
possible employment in some industrial processes, which require activity in acid pH, wide-ranging pH stability, and absence of cellulase activity
industry
purified recombinant Xyn10A is a useful candidate for producing xylooligosaccharides as thickeners, fat substitutes, and antifreeze food additives in the food industry
industry
the broad temperature profile of the enzyme makes it a potential candidate for its use in the pulp and paper industry
industry
the MS514-Xyn11 enzyme can be useful as an additive to mixtures designed to hydrolyze biomass as well as in applications for which it is desirable to maintain cellulose structure
industry
-
the suitable temperature range for industrial application of xylanase from Alternaria mali ND-16 is 50-55°C
industry
-
Thermomyces lanuginosus SSBP has potential applications due to its high productivity of xylanase and its efficiency in pulp bleaching
industry
-
variants with improved thermal and alkaline stability are ideal candidates for DNA shuffling experiments to produce a robust xylanase for industrial application
industry
-
xylanase has potential in bleach boosting and reducing the consumption elemental chlorine-free bleaching sequence. Effects produced are dependent on the enzyme and pulp type used. No correlation between the xylanase-induced brightness gains and possible savings of chlorine dioxide. Use of xylanases for pulp bleaching can boost pulp brightness or alternatively decrease the amounts of bleaching chemicals consumed, which in turn may result in respective reductions of the absorbable organic halogens and chloride levels of the bleach wastewaters and alleviate the environmental impact of the industry
industry
-
xylanase has potential in bleach boosting and reducing the consumption elemental chlorine-free bleaching sequence. Effects produced are dependent on the enzyme and pulp type used. No correlation between the xylanase-induced brightness gains and possible savings of chlorine dioxide. Use of xylanases for pulp bleaching can boost pulp brightness or alternatively decrease the amounts of bleaching chemicals consumed, which in turn may result in respective reductions of the absorbable organic halogens and chloride levels of the bleach wastewaters and alleviate the environmental impact of the industry
industry
Xyn10 can be an important candidate for protease-resistant mechanistic research and has potential applications in the food industry, cotton scouring, and improving animal nutrition
industry
XynAS27 may be a compelling tool for the food industry because it generates xylobiose (85% w/w) as the main product of xylan hydrolysis
industry
-
XynBS27 has several advantageous properties such as high specific activity, good activity over broad pH range, excellent pH stability, and being suitable for xylobiose production. These significant characteristics suggest that XynBS27 may be a good candidate in industrial application
industry
-
the enzyme is a potentially strong candidate for industrial and commercial application in pulp bleaching
industry
-
the xylanase from Bacillus sp. JB 99 is highly compatible for paper and pulp industry
industry
-
xylanase is an important industrial enzyme used in the pulp and paper industry
industry
XYN10G5 a good candidate for application in the animal feed industry
industry
Thermochaetoides thermophila
the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
industry
the fusion enzyme (EG-M-Xyn) of endoglucanase (cellulase) from Teleogryllus emma and xylanase from Thermomyces lanuginosus has great potential in generating fermentable sugars from renewable agro-residues for biofuel and fine chemical industry. Application of the fusion enzyme (EG-M-Xyn)in combination with Ctec2 (commercial enzyme) in the saccharification leads to a 10-20% net increase in fermentable sugars liberated from pretreated rice straw in comparison to the Ctec2 alone
industry
Thermochaetoides thermophila IMI 039719
-
the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
-
industry
Thermochaetoides thermophila DSM 1495
-
the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
-
industry
-
used for pulp bleaching
-
industry
-
xylanase is an important industrial enzyme used in the pulp and paper industry
-
industry
-
the suitable temperature range for industrial application of xylanase from Alternaria mali ND-16 is 50-55°C
-
industry
Thermochaetoides thermophila NIBGE 1
-
is thermostable in alkaline buffer favoring its suitability to bio-bleaching of kraft pulp. Xylanases that are more active in pH range of 6.0-10.0 can act as promising agents in paper and pulp industry. Productivity profiles of xylanase in Escherichia coli recombinant are more than 4fold of that produced from Trichoderma reesei RUTC-30, 5fold of that produced by the donor and significantly higher than the values reported on other Escherichia coli, and Saccharomyces cerevisiae recombinants
-
industry
-
high production yields of the modular xylanase Xyl30 by solid-state fermentation and its biochemical features make it a good candidate for use in industrial applications
-
industry
-
the broad temperature profile of the enzyme makes it a potential candidate for its use in the pulp and paper industry
-
industry
-
the MS514-Xyn11 enzyme can be useful as an additive to mixtures designed to hydrolyze biomass as well as in applications for which it is desirable to maintain cellulose structure
-
industry
Thermochaetoides thermophila CBS 144.50
-
the enzyme is a promising candidate for industrial lignocellulosic biomass conversion. Generation of soluble oligosaccharides from lignocellulose is a critical step in bioethanol production. The enzyme produces cello-oligosaccharides and xylo-oligosaccharides from the continuous enzymatic saccharification of sodium carboxymethyl cellulose and xylan, respectively
-
industry
-
purified recombinant Xyn10A is a useful candidate for producing xylooligosaccharides as thickeners, fat substitutes, and antifreeze food additives in the food industry
-
industry
-
the enzyme is a potentially strong candidate for industrial and commercial application in pulp bleaching
-
industry
-
the xylanase from Bacillus sp. JB 99 is highly compatible for paper and pulp industry
-
nutrition
-
possible usage as feed additive for animals in order to diminish health problems and enhance proliferation of beneficial microflora
nutrition
-
use in bio-pulping applications
nutrition
-
application of enzyme in bread making at low dosages of 0.297 International Xylanase Units/g shows its suitability to increase loaf volume by 8.0% compared with the control bread. Enzyme increases loaf softness by 19.6% while reducing bread staling by 20.4% up to 4 days of storage
nutrition
-
application of enzyme in bread making at low dosages of 0.297 International Xylanase Units/g shows its suitability to increase loaf volume by 8.0% compared with the control bread. Enzyme increases loaf softness by 19.6% while reducing bread staling by 20.4% up to 4 days of storage
-
paper production
-
biobleaching of eucalyptus kraft pulp
paper production
-
potential use in biopulping processes
paper production
-
bleaching of pulp
paper production
-
use in the pulp and paper industry, efficiency of the enzyme application to the kraft Eucalyptus pulp
paper production
-
enzyme can be used in pulp-bleaching processes to remove hemicellulose and release lignin from the pulp, leading to reduction of chloride required for conventional chemical bleaching
paper production
-
enzyme has biodelignification potential and can be used in bleaching of kraft pulps, method development, overview
paper production
-
use in pre-bleaching and bio-pulping applications
paper production
-
use in treatment of paper pulps
paper production
-
use in the pulp and paper industry for bleaching purposes
paper production
-
used for paper bleaching
paper production
-
used for paper bleaching
paper production
since XynA is thermostable and has no cellulase activity it can be potentially used for pretreatment of paper pulp before bleaching
paper production
-
xylanase is an important industrial enzyme used in the pulp and paper industry
paper production
potential applications on biofuels and paper industries
paper production
-
potential applications on biofuels and paper industries
-
paper production
-
potential use in biopulping processes
-
paper production
-
use in the pulp and paper industry, efficiency of the enzyme application to the kraft Eucalyptus pulp
-
paper production
-
enzyme can be used in pulp-bleaching processes to remove hemicellulose and release lignin from the pulp, leading to reduction of chloride required for conventional chemical bleaching
-
paper production
-
since XynA is thermostable and has no cellulase activity it can be potentially used for pretreatment of paper pulp before bleaching
-
paper production
-
used for paper bleaching
-
paper production
-
xylanase is an important industrial enzyme used in the pulp and paper industry
-
paper production
-
biobleaching of eucalyptus kraft pulp
-
paper production
-
use in the pulp and paper industry for bleaching purposes
-
paper production
-
used for paper bleaching
-
paper production
-
enzyme has biodelignification potential and can be used in bleaching of kraft pulps, method development, overview
-
paper production
-
bleaching of pulp
-
synthesis
Halalkalibacterium halodurans
-
optimum levels of wheat bran (15-20 g/l), lactose (1.0-1.5 g/l), tryptone (2-2.5 g/l) and NaCl (7.0-8.0 g/l) support a 6.75fold increase in xylanase production
synthesis
production of enzyme in Pichia pastoris with codon optimization. The activity of dual-copy enzyme is maximized at 15158 U/ml after 120 h of shaking
synthesis
Halalkalibacterium halodurans
-
yield of enzyme is enhanced more than four fold in the presence of 1% corn husk and 0.5% peptone or feather hydrolysate at pH 11 and 37°C
synthesis
recombinant expression of endo-beta-1,4-xylanase in Pichia pastoris. Codon optimization leads to 59% increase in activity. Coexpression of the Vitreoscilla hemoglobin (VHb) gene leads to higher biomass, cell viability, and xylanase activity. The maximum xylanase activity reaches 58792 U/ml when the induction temperature is 22°C
synthesis
-
alkali-pretreated roots of Taraxacum kok-saghyz (rubber dandelion), incubated with crude enzyme extracts from Thermomyces lanuginosus STm yield more natural rubber (90 mg/g dry root) than the protocols, Eskew process (24 mg/g) and commercial-enzyme-combination process (45 mg/g). The crude enzyme treatment at 91.6% rubber purity approaches the purity of the commercial-enzyme-combination process at 94.1% purity
synthesis
optimization of recombinant enzyme production in 1-liter flasks. Initial cell density is the most important parameter. Under optimized conditions, 1498 mg xylanase per liter can be achieved
synthesis
-
Bacillus licheniformis strain DM5 is attributed for the production of prebiotic and anti-inflammatory XOS from agrowaste
synthesis
-
production of enzyme in Pichia pastoris with codon optimization. The activity of dual-copy enzyme is maximized at 15158 U/ml after 120 h of shaking
-
synthesis
-
alkali-pretreated roots of Taraxacum kok-saghyz (rubber dandelion), incubated with crude enzyme extracts from Thermomyces lanuginosus STm yield more natural rubber (90 mg/g dry root) than the protocols, Eskew process (24 mg/g) and commercial-enzyme-combination process (45 mg/g). The crude enzyme treatment at 91.6% rubber purity approaches the purity of the commercial-enzyme-combination process at 94.1% purity
-
synthesis
Halalkalibacterium halodurans TSPV1
-
optimum levels of wheat bran (15-20 g/l), lactose (1.0-1.5 g/l), tryptone (2-2.5 g/l) and NaCl (7.0-8.0 g/l) support a 6.75fold increase in xylanase production
-
synthesis
Halalkalibacterium halodurans PPKS-2
-
yield of enzyme is enhanced more than four fold in the presence of 1% corn husk and 0.5% peptone or feather hydrolysate at pH 11 and 37°C
-
synthesis
-
Bacillus licheniformis strain DM5 is attributed for the production of prebiotic and anti-inflammatory XOS from agrowaste
-
additional information
Cellulomonas flavigena CDBB-531 secrets a bifunctional cellulase/xylanase
additional information
-
Cellulomonas flavigena CDBB-531 secrets a bifunctional cellulase/xylanase
additional information
Penicillium citrinum XynB is close to xylanases from other Penicillium spp. and also to enzymes from black aspergilli
additional information
-
Penicillium citrinum XynB is close to xylanases from other Penicillium spp. and also to enzymes from black aspergilli
additional information
-
simultaneous production of endoxylanase and oligosaccharides
additional information
the Bacillus sp. KT12 xylanolytic enzyme is a suitable enzyme for the synthesis of polyphenyl beta-oligoxylosides
additional information
-
the hybrid xylanase, whose parents are Thermomonospora fusca xylanase A and Aspergillus niger xylanase A, inherits some hydrolytic properties from its parents, and it is an endo-acting xylanase. X4 may be the minimum oligomer hydrolyzed by it
additional information
-
the hybrid xylanase, whose parents are Thermomonospora fusca xylanase A and Aspergillus niger xylanase A, inherits some hydrolytic properties from its parents, and it is an endo-acting xylanase. X4 may be the minimum oligomer hydrolyzed by it
additional information
the enzyme can be used for various biotechnological applications such as for prebiotic xylooligosaccharides and bioethanol production from pretreated agrowaste biomass
additional information
-
Cellulomonas flavigena CDBB-531 secrets a bifunctional cellulase/xylanase
-
additional information
-
the enzyme can be used for various biotechnological applications such as for prebiotic xylooligosaccharides and bioethanol production from pretreated agrowaste biomass
-
additional information
-
the Bacillus sp. KT12 xylanolytic enzyme is a suitable enzyme for the synthesis of polyphenyl beta-oligoxylosides
-
additional information
-
the enzyme can be used for various biotechnological applications such as for prebiotic xylooligosaccharides and bioethanol production from pretreated agrowaste biomass
-
additional information
-
the enzyme can be used for various biotechnological applications such as for prebiotic xylooligosaccharides and bioethanol production from pretreated agrowaste biomass
-
additional information
-
Penicillium citrinum XynB is close to xylanases from other Penicillium spp. and also to enzymes from black aspergilli
-
additional information
-
the enzyme can be used for various biotechnological applications such as for prebiotic xylooligosaccharides and bioethanol production from pretreated agrowaste biomass
-
additional information
-
the enzyme can be used for various biotechnological applications such as for prebiotic xylooligosaccharides and bioethanol production from pretreated agrowaste biomass
-
additional information
-
the enzyme can be used for various biotechnological applications such as for prebiotic xylooligosaccharides and bioethanol production from pretreated agrowaste biomass
-