3.2.1.73: licheninase
This is an abbreviated version!
For detailed information about licheninase, go to the full flat file.
Word Map on EC 3.2.1.73
-
3.2.1.73
-
cellulases
-
cellulolytic
-
trichoderma
-
knee
-
reesei
-
cellobiohydrolase
-
exoglucanase
-
thermocellum
-
avicel
-
carboxymethyl
-
lignocellulosic
-
cellulosic
-
arthroscopic
-
saccharification
-
beta-glucosidase
-
carboxymethylcellulose
-
cellulose-binding
-
straw
-
microcrystalline
-
glutenins
-
cellulosome
-
bagasse
-
cellotriose
-
lichenan
-
xyloglucans
-
cellulomonas
-
cellotetraose
-
xylanases
-
3.2.1.4
-
hemicellulases
-
cmcase
-
patellar
-
endo-beta-1,4-glucanase
-
patellofemoral
-
succinogenes
-
endoxylanase
-
dockerins
-
humicola
-
fpase
-
fibrobacter
-
cellulose-degrading
-
lysholm
-
lignocellulolytic
-
mannanase
-
cellodextrins
-
meniscal
-
cellobiase
-
thermobifida
-
xylanolytic
-
brewing
-
synthesis
-
endocellulase
-
agriculture
-
biofuel production
-
degradation
-
food industry
-
analysis
-
industry
-
nutrition
- 3.2.1.73
- cellulases
-
cellulolytic
- trichoderma
- knee
- reesei
- cellobiohydrolase
- exoglucanase
- thermocellum
- avicel
-
carboxymethyl
-
lignocellulosic
-
cellulosic
-
arthroscopic
-
saccharification
- beta-glucosidase
- carboxymethylcellulose
-
cellulose-binding
- straw
-
microcrystalline
-
glutenins
- cellulosome
- bagasse
- cellotriose
- lichenan
- xyloglucans
- cellulomonas
- cellotetraose
- xylanases
-
3.2.1.4
-
hemicellulases
- cmcase
-
patellar
- endo-beta-1,4-glucanase
-
patellofemoral
- succinogenes
- endoxylanase
-
dockerins
- humicola
-
fpase
- fibrobacter
-
cellulose-degrading
-
lysholm
-
lignocellulolytic
- mannanase
- cellodextrins
- meniscal
- cellobiase
- thermobifida
-
xylanolytic
- brewing
- synthesis
- endocellulase
- agriculture
- biofuel production
- degradation
- food industry
- analysis
- industry
- nutrition
Reaction
Synonyms
(1,3)(1,4)-beta-D-glucan-4-glucanohydrolase, (1->3,1->4)-beta-glucanase isoenzyme EII, 1,3-1,4-beta-D-glucan 4-glucanohydrolase, 1,3-1,4-beta-D-glucan glucanohydrolase, 1,3-1,4-beta-D-glucan-4-glucano hydrolase, 1,3-1,4-beta-D-glucanase, 1,3-1,4-beta-glucanase, 1,3;1,4-beta-glucan 4-glucanohydrolase, 1,3;1,4-beta-glucan endohydrolase, Af-EGL7, Afu6g01800, Beg1, beta-(1,3-1,4)-glucanase, beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase, beta-1,3-1,4 glucanase, beta-1,3-1,4-D-glucanase, beta-1,3-1,4-glucanase, beta-1,3;1,4-glucanase, beta-1-3, 1-4 glucan 4-glucanohydrolase, beta-glucanase, BG1, Bg1314, Bga1, bgc, bgi, Bgl, bgl5-1, BglA, BglA13, BglA16, BglA51, BglBB, bglBC1, BGlc8H, BglM2, BglS, BglT, BglTO, Bglu16A, bifunctional xylanase/endoglucanase, BLB369, BLB369 endo-beta-1,3-1,4-glucanase, Blc8H, BP_Cel9A, Cel5F, CP7 beta-1,3-1,4-glucanase, CtGlu16A, Cthe_0211, CtLic16A, CtLic26A, E-LICHN, EG1, EGL, EII, endo-(1,3)(1,4)-beta-glucanase, endo-(1,3;1,4)-beta-glucanase, endo-beta-1,3-1,4 glucanase, endo-beta-1,3-1,4-glucanase, endo-beta-1,3;1,4-glucan-D-glycosyl hydrolase, endo-beta-glucanase, endoglucanase, endotype beta-1,3-1,4-glucanase, Fisuc_2961, Fsbeta-glucanase, FSU_0226, Gcs2, GH7 endo-1,4-beta-glucanase, GHF16 TFsbeta-glucanase, GHF17 barley 1,3-1,4-beta-D-glucanase, Glc16A, GLU-1, GLU-3, glu369, Gluc5_26A, GluIII, GluUS570, glycoside hydrolase family 9 endoglucanase, GyrA, H(A16-M), lam1, LamA, laminarinase, Lic16A, Lic8H, LicA, LicB, Lichenase, lichenase-2, LicKM, licM, LicMB, LicS, McLic1, mHG, Mixed linkage beta-glucanase, More, NFEg16A, PbBglu16A, PlicA, PtLic16A, Ra0505, RuCelA, TaGlu34, TC2, TC5, TF-glu, TF-glucanase, theme C glycoside hydrolase family 9 endo-beta-glucanase, TM1752, US8_01508, XynIII, XynZ, ZgLamA
ECTree
3.2.1.73 licheninaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.2.1.73 - licheninase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
2,4-dinitrophenol + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
-
-
?
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
3,4-dinitrophenol + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
-
-
?
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucopyranoside
-
-
-
?
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
-
-
-
-
?
4-methylumbelliferyl-(1,3)-beta-D-glucooligosaccharides + H2O
4-methylumbelliferol + beta-D-oligosaccharides
-
-
-
-
?
4-methylumbelliferyl-beta-D-Gal-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
?
-
Gal substrate has a 1.3fold higher kcat/KM-value than Glc substrate
-
-
r
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-3)-beta-D-Glc
-
-
-
-
?
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
-
-
?
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
?
-
Gal substrate has a 1.3fold higher kcat/KM-value than Glc substrate
-
-
r
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
-
-
?
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
?
-
1% of the activity with carboxymethyl-cellulose
-
-
?
4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-2-deoxy-beta-D-erythro-pentopyranoside + H2O
?
-
2-deoxy analog is better substrate than corresponding 2-hydroxy substrate
-
-
?
4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-arabinopyranoside + H2O
?
-
2-deoxy analog is better substrate than corresponding 2-hydroxy substrate
-
-
?
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + F-
-
-
-
-
?
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
-
-
-
-
?
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-glucopyranoside
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
-
-
-
-
?
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-xylopyranoside
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Xyl + F-
-
-
-
-
?
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
-
-
-
-
?
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-glucopyranoside
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
-
-
-
-
?
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-xylopyranoside
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Xyl + F-
-
-
-
-
?
alpha-laminaribiosyl fluoride + methyl beta-D-Glc-(1-3)-beta-D-Glc
methyl beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + F-
-
-
-
-
?
alpha-laminaribiosyl fluoride + methyl beta-D-Glc-(1-4)-beta-D-Glc
methyl beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
-
-
-
-
?
barley beta-glucan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose + ?
-
-
-
-
?
barley beta-glucan + H2O
beta-D-glucose + cellobiose + ?
enzyme NFEg16A efficiently hydrolyzes the substrate at a high concentration of 15 mg/mL, and releases glucose and cellobiose as its main end products
-
-
?
barley beta-glucan + H2O
Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
cellohexaose + H2O
cellobiose + cellotriose
-
no release of D-glucose
-
?
chitosan + H2O
?
81.3% of the activity with barley beta-D-glucan
-
-
?
Glcbeta(1-3)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glc + H2O
glucose + Glcbeta(1-3)Glcbeta(1-4)Glcbeta(1-4)Glc
-
-
-
-
?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-3)Glcbeta(1-4)Glcbeta(1-4)Glc-OMe + H2O
?
-
-
-
-
?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-3)Glc + H2O
?
-
-
-
-
?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta-O-4-methylumbeliferone + H2O
?
-
-
-
-
?
glucan tetrasaccharide + H2O
D-glucose + glucan trisaccharide
containing two beta-1,4-linkages separated by one beta-1,3-linkage, i.e. G4G3G4G
containing one beta-1,4-linkage separated by one beta-1,3-linkage, i.e. G4G3G, which is not further degraded
-
?
laminaritriose + H2O
D-glucose + laminaribiose
the smallest oligosaccharide that can be degraded by the enzyme
-
-
?
lichenan + H2O
cellobiose + Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
oat beta-glucan + H2O
beta-glucan oligosaccharides
-
92% of the activity with barley beta-glucan
-
-
?
avicel + H2O
?
-
50% of the activity with carboxymethyl-cellulose
-
-
?
barley beta-glucan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
-
-
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
-
-
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
?
best substrate, 1% w/v substrate concentration, best substrate
-
-
?
barley beta-glucan + H2O
?
best substrate, 1% w/v substrate concentration, best substrate
-
-
?
barley beta-glucan + H2O
?
best substrate, 1% w/v substrate concentration, best substrate
-
-
?
barley beta-glucan + H2O
?
Aspergillus fumigatus CBS 101355
best substrate, 1% w/v substrate concentration, best substrate
-
-
?
barley beta-glucan + H2O
?
Aspergillus fumigatus FGSC A1100
best substrate, 1% w/v substrate concentration, best substrate
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
63% of the activity with oat gum
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
best substrate
-
-
?
barley beta-glucan + H2O
?
best substrate
-
-
?
barley beta-glucan + H2O
?
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
Rasamsonia emersonii CBS 841.70
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
-
the main final hydrolysis products from barley beta-glucan are the trisaccharide and the tetrasaccharide, which is typical for true bacterial lichenases
-
-
?
barley beta-glucan + H2O
?
-
-
the enzyme produces glucosyl beta-1,3 glucosyl beta-1,4 glucose as the major end product, glucosyl beta-1,4 glucosyl beta-1,3 glucose is not detected
-
?
barley beta-glucan + H2O
?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
the enzyme produces glucosyl beta-1,3 glucosyl beta-1,4 glucose as the major end product, glucosyl beta-1,4 glucosyl beta-1,3 glucose is not detected
-
?
barley beta-glucan + H2O
?
endo-beta-glucanase BP_Cel9A hydrolyzes beta-1,3-1,4-linked barley beta-glucan, best substrate
-
-
?
barley beta-glucan + H2O
beta-glucan oligosaccharides
Bacillus sp. (in: Bacteria) KCCM 90078
-
-
-
-
?
barley beta-glucan + H2O
beta-glucan oligosaccharides
-
-
-
-
?
barley beta-glucan + H2O
beta-glucan oligosaccharides
-
-
-
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
-
-
oligosaccharides (mainly trisaccharide and tetrasaccharide) followed by disaccharide (cellobiose) and glucose are formed as the major products of hydrolysis after a prolonged incubation of 4 h
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
-
-
oligosaccharides (mainly trisaccharide and tetrasaccharide) followed by disaccharide (cellobiose) and glucose are formed as the major products of hydrolysis after a prolonged incubation of 4 h
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
-
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
-
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
-
final products
-
?
barley beta-glucan + H2O
Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
-
final products
-
?
barley-beta-glucan + H2O
?
KM079629
best substrate, azo-barley-glucan as the substrate
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
from oat and barley
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
from oat and barley
-
-
?
beta-1,3-1,4-glucan + H2O
?
-
from Hordeum vulgare, best substrate
-
-
?
beta-1,3-1,4-glucan + H2O
?
source of substrate: barley
-
-
?
beta-1,3/1,4-glucan + H2O
?
best substrate is 1,3/1,4-beta-glucan from Hordeum vulgare, and almost equally active from Avena sativa
-
-
?
beta-1,3/1,4-glucan + H2O
?
best substrate is 1,3/1,4-beta-glucan from Hordeum vulgare, and almost equally active from Avena sativa
-
-
?
beta-D-glucan + H2O
?
source: barley, best substrate
hydrolysis products from barley beta-glucan are 6.8 micromol/ml glucose and 16.3 micromol/ml cellobiose
-
?
beta-D-glucan + H2O
?
-
the two extremely different folds adopted by GHF16 and GHF17 enzymes, beta-jellyroll and (beta/alpha)8, respectively, accommodate mixed beta-1,3 and beta-1,4 beta-D-glucans or lichenan
-
-
?
carboxymethyl cellulose + H2O
?
1% w/v substrate concentration, low activity
-
-
?
carboxymethyl cellulose + H2O
?
1% w/v substrate concentration, low activity
-
-
?
carboxymethyl cellulose + H2O
?
1% w/v substrate concentration, low activity
-
-
?
carboxymethyl cellulose + H2O
?
Aspergillus fumigatus CBS 101355
1% w/v substrate concentration, low activity
-
-
?
carboxymethyl cellulose + H2O
?
Aspergillus fumigatus FGSC A1100
1% w/v substrate concentration, low activity
-
-
?
carboxymethyl cellulose + H2O
?
9.8% of the activity with beta-D-glucan
-
-
?
carboxymethyl cellulose + H2O
?
32.2% of the activity with barley beta-D-glucan
-
-
?
carboxymethyl cellulose + H2O
?
22.4% activity compared to barley beta-glucan
-
-
?
carboxymethyl-cellulose + H2O
?
-
a negligible amount of hydrolysis of carboxymethyl-cellulose is observed
-
-
?
carboxymethyl-cellulose + H2O
?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
a negligible amount of hydrolysis of carboxymethyl-cellulose is observed
-
-
?
carboxymethylcellulose + H2O
?
52% of the activity with oat gum
-
-
?
carboxymethylcellulose + H2O
?
-
18% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
cellopentaose + H2O
cellobiose + D-glucose
-
with N-terminal deletion mutant, products are cellotriose and cellobiose
-
?
cellopentaose + H2O
cellobiose + D-glucose
-
with N-terminal deletion mutant, products are cellotriose and cellobiose
-
?
cellulose + H2O
?
-
7% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
cellulose + H2O
?
filter paper
main products are cellobiose and cellotriose
-
?
Glc-beta(1,4)-Glc-beta(1,4)-Glc-beta(1,3)-Glc + H2O
cellobiose + laminaribiose
-
with N-terminal deletion mutant, products are cellotriose and D-glucose
-
?
Glc-beta(1,4)-Glc-beta(1,4)-Glc-beta(1,3)-Glc + H2O
cellobiose + laminaribiose
-
with N-terminal deletion mutant, products are cellotriose and D-glucose
-
?
laminarin + H2O
?
-
70% of the activity with carboxymethyl-cellulose
-
-
?
laminarin + H2O
?
-
20.5% activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
Paenibacillus barengoltzii CAU904
-
20.5% activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
4.1% of the activity with barley beta-D-glucan
-
-
?
laminarin + H2O
?
0.12% activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
the wild-type enzyme displays a bent topology adapted to the binding of helical-shaped laminarin
-
-
?
lichenan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
-
-
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
lichenan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
-
-
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
lichenan + H2O
?
-
500% of the activity with carboxymethyl-cellulose
-
-
?
lichenan + H2O
?
72% of the activity with beta-D-glucan
hydrolysis products from lichenan are 9.1 micromol/ml glucose and 9.9 micromol/ml cellobiose, and 0.45 micromol/ml cellotetraose
-
?
lichenan + H2O
?
-
the two extremely different folds adopted by GHF16 and GHF17 enzymes, beta-jellyroll and (beta/alpha)8, respectively, accommodate mixed beta-1,3 and beta-1,4 beta-D-glucans or lichenan
-
-
?
lichenan + H2O
?
-
85% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
lichenan + H2O
?
a beta-1,3/1,4-glucan from Cetraria islandica, half as active as barley or oat beta-1,3/1,4-glucans
-
-
?
lichenan + H2O
?
a beta-1,3/1,4-glucan from Cetraria islandica, half as active as barley or oat beta-1,3/1,4-glucans
-
-
?
lichenan + H2O
?
68.8% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
14.5% of the activity with barley beta-D-glucan
-
-
?
lichenan + H2O
?
136.4% activity compared to barley beta-glucan
-
-
?
lichenan + H2O
?
-
68.2% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
Thermoascus aurantiacus CAU830
-
68.2% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
-
-
the enzyme produces glucosyl beta-1,3 glucosyl beta-1,4 glucose as the major end product, glucosyl beta-1,4 glucosyl beta-1,3 glucose is not detected
-
?
lichenan + H2O
?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
the enzyme produces glucosyl beta-1,3 glucosyl beta-1,4 glucose as the major end product, glucosyl beta-1,4 glucosyl beta-1,3 glucose is not detected
-
?
lichenan + H2O
?
67% activity compared to barley beta-glucan
-
-
?
lichenan + H2O
beta-D-Glc-(1->3)-beta-D-Glc-(1->4)-beta-D-Glc + ?
beta-D-Glc-(1->4)-beta-D-Glc-(1->3)-beta-D-Glc is not detected as product
-
-
?
lichenan + H2O
beta-D-Glc-(1->3)-beta-D-Glc-(1->4)-beta-D-Glc + ?
beta-D-Glc-(1->4)-beta-D-Glc-(1->3)-beta-D-Glc is not detected as product
-
-
?
lichenan + H2O
cellobiose + Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
-
final products
-
?
lichenan + H2O
cellobiose + Glc-beta(1,4)-Glc-beta(1,3)-Glc-beta(1,4)-Glc + Glc-beta(1,3)-Glc-beta(1,4)-Glc-OH
-
final products
-
?
lichenan + H2O
cellotriose + ?
95.2% activity compared to barley beta-glucan
oligosaccharides, mainly trisaccharide
-
?
lichenan + H2O
cellotriose + ?
95.2% activity compared to barley beta-glucan
oligosaccharides, mainly trisaccharide
-
?
lichenan + H2O
cellotriose + cellotetraose + ?
-
93.5% activity compared to barley beta-glucan
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
lichenan + H2O
cellotriose + cellotetraose + ?
-
93.5% activity compared to barley beta-glucan
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
lichenin + H2O
?
-
49.8% activity compared to barley beta-glucan
-
-
?
lichenin + H2O
?
-
50% of the activity with barley beta-glucan
-
-
?
lichenin + H2O
?
Paenibacillus barengoltzii CAU904
-
49.8% activity compared to barley beta-glucan
-
-
?
lichenin + H2O
?
Paenibacillus barengoltzii CAU904
-
50% of the activity with barley beta-glucan
-
-
?
oat beta-glucan + H2O
?
-
92.3% activity compared to barley beta-glucan
-
-
?
oat beta-glucan + H2O
?
-
92.4% of the activity with barley beta-glucan
-
-
?
oat beta-glucan + H2O
?
Thermoascus aurantiacus CAU830
-
92.4% of the activity with barley beta-glucan
-
-
?
sugarcane exploded bagasse + H2O
?
1% w/v substrate concentration, sugarcane exploded bagasse biomass (SEB). SEB is a highly heterogeneous material that consists of 47.5% cellulose, 9.0% hemicellulose, and 34.3% lignin
-
-
?
sugarcane exploded bagasse + H2O
?
1% w/v substrate concentration, sugarcane exploded bagasse biomass (SEB). SEB is a highly heterogeneous material that consists of 47.5% cellulose, 9.0% hemicellulose, and 34.3% lignin
-
-
?
sugarcane exploded bagasse + H2O
?
1% w/v substrate concentration, sugarcane exploded bagasse biomass (SEB). SEB is a highly heterogeneous material that consists of 47.5% cellulose, 9.0% hemicellulose, and 34.3% lignin
-
-
?
sugarcane exploded bagasse + H2O
?
Aspergillus fumigatus CBS 101355
1% w/v substrate concentration, sugarcane exploded bagasse biomass (SEB). SEB is a highly heterogeneous material that consists of 47.5% cellulose, 9.0% hemicellulose, and 34.3% lignin
-
-
?
sugarcane exploded bagasse + H2O
?
Aspergillus fumigatus FGSC A1100
1% w/v substrate concentration, sugarcane exploded bagasse biomass (SEB). SEB is a highly heterogeneous material that consists of 47.5% cellulose, 9.0% hemicellulose, and 34.3% lignin
-
-
?
xylan + H2O
?
-
500% of the activity with carboxymethyl-cellulose
-
-
?
xyloglucan + H2O
?
high activity, xyloglucan from tamarind seed, 1% w/v substrate concentration
-
-
?
xyloglucan + H2O
?
high activity, xyloglucan from tamarind seed, 1% w/v substrate concentration
-
-
?
xyloglucan + H2O
?
high activity, xyloglucan from tamarind seed, 1% w/v substrate concentration
-
-
?
xyloglucan + H2O
?
Aspergillus fumigatus CBS 101355
high activity, xyloglucan from tamarind seed, 1% w/v substrate concentration
-
-
?
xyloglucan + H2O
?
Aspergillus fumigatus FGSC A1100
high activity, xyloglucan from tamarind seed, 1% w/v substrate concentration
-
-
?
xyloglucan + H2O
?
40% activity compared to barley beta-glucan
-
-
?
barley beta-glucan + H2O
additional information
-
-
-
pentose, triose, tetarose and a high molecular weight polysaccharide with 1,3 linkage
-
?
barley beta-glucan + H2O
additional information
-
-
-
pentose, triose, tetrose and a high molecular weight polysaccharide with 1,3 linkage
-
?
barley beta-glucan + H2O
additional information
-
-
-
pentose, triose, tetarose and a high molecular weight polysaccharide with 1,3 linkage
-
?
barley beta-glucan + H2O
additional information
-
-
-
pentose, triose, tetrose and a high molecular weight polysaccharide with 1,3 linkage
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from oat
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
main products are triose and tetraose
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
oligosaccharides are formed as the major products, no glucose
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from oat
oligosaccharides are formed as the major products, no glucose
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
-
?
carboxymethyl beta-glucan + H2O
additional information
-
-
carboxymethyl beta-glucan from barley
trisaccharide, 53%, tetrasaccharide, 25%
?
lichenin + H2O
additional information
-
-
-
main products are triose and tetraose
?
lichenin + H2O
additional information
-
-
lichenin from Cetralia islandica and from Usnea barbata
-
-
?
additional information
?
-
-
no activity against beta-1,4- or beta-1,3 homopolymers of gluco- or manno-configured polysaccharides
-
-
?
additional information
?
-
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
?
additional information
?
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
?
additional information
?
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Acetivibrio thermocellus DSM 1237
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
?
additional information
?
-
Acetivibrio thermocellus DSM 1237
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus DSM 1237
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Acetivibrio thermocellus NBRC 103400
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus NBRC 103400
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Acetivibrio thermocellus NCIMB 10682
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus NCIMB 10682
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Acetivibrio thermocellus NRRL B-4536
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus NRRL B-4536
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Acetivibrio thermocellus VPI 7372
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Acetivibrio thermocellus VPI 7372
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
?
additional information
?
-
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
-
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
Aspergillus fumigatus CBS 101355
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
Aspergillus fumigatus FGSC A1100
the enzyme exhibits higher activity toward beta-glucan than toward xyloglucan and carboxymethyl cellulose suggesting that the enzyme corresponds to a beta-1,3-1,4-glucanase. No activity with Avicel and beechwood xylan
-
-
?
additional information
?
-
-
does not hydrolyze carboxymethyl-cellulose or avicel cellulose
-
-
?
additional information
?
-
-
the enzyme is a conformation-retaining and is only active toward glucan containing beta-1,3-1,4-linkages. No activity with laminarin and carboxymethyl cellulose
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
does not hydrolyze carboxymethyl-cellulose or avicel cellulose
-
-
?
additional information
?
-
-
the enzyme is a conformation-retaining and is only active toward glucan containing beta-1,3-1,4-linkages. No activity with laminarin and carboxymethyl cellulose
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Aspergillus terreus ASKU 10
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans
-
-
?
additional information
?
-
native and recombinant enzymes are both inactive on laminarin, cellulose, xylan, or mannan
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans
-
-
?
additional information
?
-
native and recombinant enzymes are both inactive on laminarin, cellulose, xylan, or mannan
-
-
?
additional information
?
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
?
additional information
?
-
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
antifungal enzyme activity assay
-
-
?
additional information
?
-
antifungal enzyme activity assay
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
activity against 1% carboxymethylcellulose is not observed
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose and laminarin, isozymes EG1 and EG2 exhibit no activity for pure beta-1,3 bond and for pure beta-1,4 glucan forms
-
-
?
additional information
?
-
-
enzyme exhibits strict specificity for beta-1,3-1,4-D-glucans
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Bacillus licheniformis EGW039 / CGMCC 0635
-
activity against 1% carboxymethylcellulose is not observed
-
-
?
additional information
?
-
Bacillus licheniformis EGW039 / CGMCC 0635
-
no activity on cellulose
-
-
?
additional information
?
-
-
enzyme exhibits strict specificity for beta-1,3-1,4-D-glucans
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose and laminarin, isozymes EG1 and EG2 exhibit no activity for pure beta-1,3 bond and for pure beta-1,4 glucan forms
-
-
?
additional information
?
-
no substrates: laminarin and carboxymethylcellulose
-
-
?
additional information
?
-
-
no substrates: laminarin and carboxymethylcellulose
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Bacillus pumilus US570
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Bacillus pumilus US570
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
no hydrolysis of carboxymethylpachyman
-
-
?
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans
-
-
?
additional information
?
-
thin layer product identification
-
-
?
additional information
?
-
beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans
-
-
?
additional information
?
-
thin layer product identification
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Bacillus sp. N137
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Bacillus sp. N137
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
no activity against carboxymethylcellulose, xylan, laminarin, dextrin
-
-
?
additional information
?
-
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
?
additional information
?
-
-
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
?
additional information
?
-
-
no activity against carboxymethylcellulose, xylan, laminarin, dextrin
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Bacillus subtilis NCIB 8565
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Bacillus subtilis NCIB 8565
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
no activity with carboxymethyl cellulose, xylan, laminarin, and soluble starch, substrate specificity, overview
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
no activity with carboxymethyl cellulose, xylan, laminarin, and soluble starch, substrate specificity, overview
-
-
?
additional information
?
-
enzyme displays low activity on avicel, cellobiose, filter paper, p-nitrophenyl beta-D-cellobioside, and p-nitrophenyl beta-D-glucoside, and no activity against microcrystalline cellulose or salicin
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
carboxymethylcellulose and starch are no substrates
-
-
?
additional information
?
-
poor substrates: laminarin, oat spelt xylan. No substrate: avicel
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
carboxymethylcellulose and arabinoxylan are no substrates
-
-
?
additional information
?
-
-
carboxymethylcellulose, arabinoxylan, laminarin, and starch are no substrates
-
-
?
additional information
?
-
-
no hydrolysis of carboxymethylpachyman
-
-
?
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
also active with laminarin, poor activity with Avicel, rice straw, and xylan, no activity with 4-nitrophenyl-beta-D-hexoside derivatives, substrate specificity, overview
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
the enzyme shows strict substrate specificity for barley beta-glucan, oat beta-glucan and lichenan, but is not active with other tested polysaccharides and synthetic 4-nitrophenyl derivates
-
-
?
additional information
?
-
-
the enzyme shows strict substrate specificity for barley beta-glucan, oat beta-glucan and lichenan, but is not active with other tested polysaccharides and synthetic 4-nitrophenyl derivates
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
the enzyme shows strict substrate specificity for barley beta-glucan, oat beta-glucan and lichenan, but is not active with other tested polysaccharides and synthetic 4-nitrophenyl derivates
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Niallia circulans ATCC 21367
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
Niallia circulans ATCC 21367
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
purified recombinant EGL2 protein hydrolyzes beta-1,3/1,4-glucans, but not beta-1,3/1,6-linked or beta-1,3-linked glucopolysaccharides, e.g. laminarin from Laminaria digitata or Eisenia bicyclis, or curdlan from Alcaligenes faecalis, nor carboxymethylcellulose
-
-
?
additional information
?
-
-
purified recombinant EGL2 protein hydrolyzes beta-1,3/1,4-glucans, but not beta-1,3/1,6-linked or beta-1,3-linked glucopolysaccharides, e.g. laminarin from Laminaria digitata or Eisenia bicyclis, or curdlan from Alcaligenes faecalis, nor carboxymethylcellulose
-
-
?
additional information
?
-
purified recombinant EGL1 protein hydrolyzes beta-1,3/1,4-glucans, but not beta-1,3/1,6-linked or beta-1,3-linked glucopolysaccharides, e.g. laminarin from Laminaria digitata or Eisenia bicyclis, or curdlan from Alcaligenes faecalis, nor carboxymethylcellulose
-
-
?
additional information
?
-
strictly specific for beta-1,3-1,4-glucans. No substrates are: Avicel, carboxymethyl-cellulose, cellulose, filter paper, beta-1,3-glucan, laminarin, and birchwood xylan
-
-
?
additional information
?
-
-
strictly specific for beta-1,3-1,4-glucans. No substrates are: Avicel, carboxymethyl-cellulose, cellulose, filter paper, beta-1,3-glucan, laminarin, and birchwood xylan
-
-
?
additional information
?
-
-
beta-1,3-1,4-glucanase strictly cleaves the beta-1,4-D-glucosidic bonds adjacent to beta-1,3-linkages in mixed linked beta-glucans
-
-
?
additional information
?
-
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
?
additional information
?
-
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
-
-
?
additional information
?
-
-
beta-glucanase does not act toward avicel, carboxymethylcellulose, cellulose, filter paper, beta-1,3-glucan, hydroxyethyl-cellulose, laminarin, starch, pullulan, birchwood xylan, locust bean gum, cellobiose, and xylobiose. No activity for p-nitrophenyl-beta-D-glucopyranoside, p-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-fucopyranoside, p-nitrophenyl-beta-D-galactopyranoside, and p-nitrophenyl-beta-D-mannopyranoside
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview
-
-
?
additional information
?
-
-
beta-glucanase does not act toward avicel, carboxymethylcellulose, cellulose, filter paper, beta-1,3-glucan, hydroxyethyl-cellulose, laminarin, starch, pullulan, birchwood xylan, locust bean gum, cellobiose, and xylobiose. No activity for p-nitrophenyl-beta-D-glucopyranoside, p-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-fucopyranoside, p-nitrophenyl-beta-D-galactopyranoside, and p-nitrophenyl-beta-D-mannopyranoside
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
?
additional information
?
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
-
no detectable hydrolysis activity is observed towards xylan, pullulan, soluble starch, carboxymethyl cellulose, and artificially synthesized 4-nitrophenyl-glycosides
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
Paenibacillus barengoltzii CAU904
-
no detectable hydrolysis activity is observed towards xylan, pullulan, soluble starch, carboxymethyl cellulose, and artificially synthesized 4-nitrophenyl-glycosides
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
additional information
?
-
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
-
-
?
additional information
?
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lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
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additional information
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beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
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additional information
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the enzyme specifically catalyzes the hydrolysis of beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in 1,3-1,4-beta-glucan
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additional information
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enzyme substrate specificity, overview. No activity with laminarin, carboxymethyl cellulose, xylan and soluble starch
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additional information
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enzyme hydrolyzes mixed-linked beta-1,3-1,4-glucans and chitosan as well as carboxymethyl cellulose, showing activities of EC 3.2.1.6 and EC 3.2.1.74
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additional information
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the enzyme specifically catalyzes the hydrolysis of beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in 1,3-1,4-beta-glucan
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additional information
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enzyme substrate specificity, overview. No activity with laminarin, carboxymethyl cellulose, xylan and soluble starch
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additional information
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no activity with carboxymethyl cellulose, laminarin, xylan, scleroglucan, and starch, substrate specificity, overview. The enzyme is inactive toward alpha-1,4, alpha-1,6, beta-1,4 and beta-1,6 linkages
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additional information
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beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
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additional information
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beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
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additional information
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no activity with carboxymethyl cellulose, laminarin, xylan, scleroglucan, and starch, substrate specificity, overview. The enzyme is inactive toward alpha-1,4, alpha-1,6, beta-1,4 and beta-1,6 linkages
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additional information
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beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
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additional information
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Rasamsonia emersonii CBS 841.70
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beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
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additional information
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thin layer chromatography product analysis, overview. Poor activity with laminarin, no activity with birchwood xylan, carboxymethyl cellulose, pullulan, soluble starch, locust bean gum, cellulose, Avicel, beta-1,3-glucan, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-D-galactopyranoside, substrate specificity, overview
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additional information
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beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
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?
additional information
?
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beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
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additional information
?
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beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
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additional information
?
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thin layer chromatography product analysis, overview. Poor activity with laminarin, no activity with birchwood xylan, carboxymethyl cellulose, pullulan, soluble starch, locust bean gum, cellulose, Avicel, beta-1,3-glucan, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-D-galactopyranoside, substrate specificity, overview
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additional information
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the enzyme shows only residual activity against 1,3-beta-glucan (laminarin) or no activity at all against 1,4-beta-glucan (cellulose), chitin, xylan, or manan
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additional information
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beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
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additional information
?
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lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
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?
additional information
?
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beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
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additional information
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Rhodothermus marinus ITI378
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
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additional information
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Rhodothermus marinus ITI378
beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
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?
additional information
?
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lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
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?
additional information
?
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beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
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?
additional information
?
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lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
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?
additional information
?
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beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
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additional information
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carboxymethylcellulose and arabinoxylan are no substrates
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additional information
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does not hydrolyze laminaripentaose and cellopentaose
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additional information
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reported fungal eta-1,3-1,4-glucanases exhibit strict substrate specificity toward barley beta-glucan, oat beta-glucan and lichenan, of which the structures are all beta-(1,4)-linked glucose interrupted with beta-(1,3)-linkages. beta-1,3-1,4-Glucanases (lichenases) specifically hydrolyze the beta-1,4 glycosidic linkages adjacent to beta-1,3 bonds, yielding disaccharides, trisaccharides and tetrasaccharides as the major products. Enzyme TaGlu34 hydrolyzes barley beta-glucan and lichanan to produce mainly disaccharide and trisaccharide without formation of tetrasaccharide. Production of glucan oligosaccharides from oat bran by TaGlu34
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additional information
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no activity towards other tested polysaccharides including laminarin, CMC, birchwood xylan, pullulan, soluble starch and locust bean gum, and 4-nitrophenyl derivates such as 4-nitrophenyl-beta-xylopyranoside, 4-nitrophenyl-beta-galactopyranoside, 4-nitrophenyl alpha-galactopyranoside, 4-nitrophenyl beta-glucopyranoside and 4-nitrophenyl-alpha-glucopyranoside
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additional information
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Thermoascus aurantiacus CAU830
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reported fungal eta-1,3-1,4-glucanases exhibit strict substrate specificity toward barley beta-glucan, oat beta-glucan and lichenan, of which the structures are all beta-(1,4)-linked glucose interrupted with beta-(1,3)-linkages. beta-1,3-1,4-Glucanases (lichenases) specifically hydrolyze the beta-1,4 glycosidic linkages adjacent to beta-1,3 bonds, yielding disaccharides, trisaccharides and tetrasaccharides as the major products. Enzyme TaGlu34 hydrolyzes barley beta-glucan and lichanan to produce mainly disaccharide and trisaccharide without formation of tetrasaccharide. Production of glucan oligosaccharides from oat bran by TaGlu34
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additional information
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Thermoascus aurantiacus CAU830
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no activity towards other tested polysaccharides including laminarin, CMC, birchwood xylan, pullulan, soluble starch and locust bean gum, and 4-nitrophenyl derivates such as 4-nitrophenyl-beta-xylopyranoside, 4-nitrophenyl-beta-galactopyranoside, 4-nitrophenyl alpha-galactopyranoside, 4-nitrophenyl beta-glucopyranoside and 4-nitrophenyl-alpha-glucopyranoside
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additional information
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Thermomonospora sp.
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no activity towards avicel, laminarin, gum arabic, p-nitrophenyl glucoside, and p-nitrophenyl xylopyranoside
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additional information
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does not display any activity on crystalline cellulose or laminarin
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additional information
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no activity with crystalline cellulose, carbocymethyl cellulose, Avicel, curdlan, starch, pustulan, birchwood xylan or laminarin
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additional information
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no activity with crystalline cellulose, carbocymethyl cellulose, Avicel, curdlan, starch, pustulan, birchwood xylan or laminarin
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additional information
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Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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does not display any activity on crystalline cellulose or laminarin
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additional information
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the purified enzyme fraction shows no activity on laminarin and xylan
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additional information
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the purified enzyme fraction shows no activity on laminarin and xylan
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additional information
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beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
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?
additional information
?
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beta-1,3-1,4-glucanases or lichenases hydrolyze beta-glucans containing beta-1,3 and beta-1,4 linkages, such as cereal beta-glucans and lichenan
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additional information
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the enzyme is active with beta-D-glucans containing (1->3)- and (1->4)-bonds (EC 3.2.1.73, licheninase) and with beta-D-glucans containing only (1->4)-bonds (EC 3.2.1.4, cellulase). It shows an exclusive endoacting mechanism. No activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-cellobioside, avicel, curdlan, laminarin, cellulose, carboxymethyl cellulose, and xylan
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additional information
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no activitiy using beta-1,3-glucan, laminarin, or Avicel as substrates
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additional information
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enzyme NFEg16A does not show clear activity against nature product of laminarin and carboxymethylcellulose-Na, but shows activity on barley beta-glucan, which might indicate that it is a true beta-1,3-1,4-glucanase (EC 3.2.1.73)
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additional information
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the enzyme specifically cleaves beta-1,4-linkages next to beta-1,3-linkages and is active on linear 1,3-beta-D-glucans with 3-6 monomers and on a glucan tetrasaccharide containing two beta-1,4-linkages separated by one beta-1,3-linkage. Enzyme-substrate complex structure analysis using wild-type and mutant enzymes with glucan oligomers, binding structure and substrate recognition, overview
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