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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
-
-
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
mode of action
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
Mucor rouxians
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
reaction mechanism depends on the substrate, i.e. hydrolysis or transglycosylation, overview
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
residue Trp622 is important in substrate binding rather than in determination of pH optimum, and probably does not interact with the catalytic base
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
structure-function relationship, ligand binding
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
mode of action
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
residue Trp622 is important in substrate binding rather than in determination of pH optimum, and probably does not interact with the catalytic base
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
-
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3-alpha-maltosylglucose + H2O
?
-
-
-
-
?
4 glucose
glucooligosaccharide + 3 H2O
4-alpha-nigerosyl-glucose + H2O
?
-
-
-
-
?
4-methylumbelliferyl-alpha-D-glucoside + H2O
?
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
4-nitrophenyl alpha-D-glucopyranoside + H2O
D-glucose + 4-nitrophenol
-
-
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
4-nitrophenyl D-glucose
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
6-alpha-maltosylglucose + H2O
?
-
-
-
-
?
alpha-alpha-trehalose + H2O
alpha-D-glucose
-
-
-
-
?
alpha-cyclodextrin + H2O
?
alpha-cyclodextrin + H2O
alpha-cyclodextrin + beta-D-glucose
alpha-cyclodextrin + H2O
glucose + ?
alpha-D-glucopyranosyl fluoride + H2O
?
-
-
-
-
?
alpha-limit dextrin + H2O
?
-
-
-
-
?
amylodextrin + H2O
?
-
amylodextrin DP-15
-
-
?
amylopectin + H2O
amylopectin + beta-D-glucose
amylopectin + H2O
beta-D-glucose + ?
amylopectin + H2O
D-glucose + ?
amylose + H2O
amylose + beta-D-glucose
amylose + H2O
beta-D-glucose + ?
amylose + H2O
D-glucose + ?
amylose + H2O
glucose + ?
amylose A + H2O
?
-
-
-
?
amylose B + H2O
?
-
-
-
?
amylose DP 18 + H2O
beta-D-glucose + amylose DP 17
-
-
-
-
?
beta-cyclodextrin + H2O
?
beta-cyclodextrin + H2O
beta-cyclodextrin + beta-D-glucose
-
-
-
-
?
cassava starch + H2O
beta-D-glucose + ?
-
-
-
-
?
curcumin + beta-D-glucose
curcuminyl bis-alpha-D-glucoside + 6-O-curcuminyl bis-D-glucose + curcuminyl bis-beta-D-glucoside
-
i.e. 1E,6E-1,7-di(4-hydroxy-3-methoxy-phenyl)-1,6-heptadiene-3,5-dione
-
-
?
curcumin + D-mannitol
1-O-curcuminyl bis-D-mannitol
-
i.e. 1E,6E-1,7-di(4-hydroxy-3-methoxy-phenyl)-1,6-heptadiene-3,5-dione
-
-
?
curcumin + D-mannose
curcuminyl bis-alpha-D-mannoside + curcuminyl bis-maltoside + 6-O-curcuminyl bis-maltose + 6''-O-curcuminyl bis-maltose
-
i.e. 1E,6E-1,7-di(4-hydroxy-3-methoxy-phenyl)-1,6-heptadiene-3,5-dione
-
-
?
curcumin + sucrose
1-O-curcuminyl bis-sucrose + 6''-O-curcuminyl bis-sucrose + 6-O-curcuminyl bis-sucrose
-
i.e. 1E,6E-1,7-di(4-hydroxy-3-methoxy-phenyl)-1,6-heptadiene-3,5-dione
-
-
?
curcumin-bis-alpha-D-glucoside + H2O
curcumin + beta-D-glucose
-
the enzyme also performs glucosylation of curcumin-bis-alpha-D-glucoside in the reverse reaction
-
-
r
D-glucooligomer + H2O
D-glucose
-
-
-
-
?
D-malto-oligosaccharides + H2O
?
-
low activity
-
-
?
dextrin + 6 H2O
7 beta-D-glucose
dextrin + 6 H2O
7 D-glucose
dextrin + H2O
dextrin + beta-D-glucose
-
-
-
-
?
eugenol + beta-D-glucose
eugenyl alpha-D-glucoside + 6-O-eugenyl D-glucose + eugenyl beta-D-glucoside
-
i.e. 4-allyl-2-methoxy phenol
-
-
?
eugenol + D-mannitol
1-O-eugenyl mannitol
-
i.e. 4-allyl-2-methoxy phenol
-
-
?
eugenol + D-mannose
eugenyl alpha-D-mannoside
-
i.e. 4-allyl-2-methoxy phenol
-
-
?
eugenol + maltose
eugenyl maltoside + 6-O-eugenyl maltose + 6''-O-eugenyl maltose
-
-
-
-
?
eugenol + sucrose
1-O-eugenyl sucrose + 6-O-eugenyl sucrose + 6''-O-eugenyl sucrose
-
i.e. 4-allyl-2-methoxy phenol
-
-
?
gamma-cyclodextrin + H2O
gamma-cyclodextrin + beta-D-glucose
-
-
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
glycogen + H2O
beta-D-glucose + glycogen
-
-
-
-
?
glycogen + H2O
D-glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
glycogen + H2O
glycogen + beta-D-glucose
guaiacol-alpha-D-glucoside + H2O
guaiacol + beta-D-glucose
-
the enzyme also performs glucosylation of guaiacol-alpha-D-glucoside in the reverse reaction
-
-
r
isomaltoheptaose + H2O
?
-
-
-
-
?
isomaltoheptaose + H2O
beta-D-glucose
-
-
-
-
?
isomaltohexaose + H2O
?
-
-
-
-
?
isomaltohexaose + H2O
beta-D-glucose
-
-
-
-
?
isomaltopentaose + H2O
beta-D-glucose
-
-
-
-
?
isomaltose
isomaltooligosaccharide
isomaltose + H2O
beta-D-glucose
isomaltose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
isomaltotetraose + H2O
beta-D-glucose
-
-
-
-
?
isomaltotriose + H2O
? + beta-D-glucose
-
-
-
-
?
isomaltotriose + H2O
beta-D-glucose
-
-
-
-
?
kojibiose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
maize starch + H2O
beta-D-glucose + ?
-
-
-
-
?
maltodextrin + H2O
?
-
corn maltodextrin
-
-
?
maltodextrin + H2O
beta-D-glucose + ?
-
-
-
-
?
maltodextrin + H2O
beta-glucose + ?
-
-
-
?
maltodextrin + H2O
D-glucose + ?
-
from corn mash
-
-
?
maltodextrin + H2O
maltodextrin + beta-D-glucose
-
during incubation 5-(hydroxymethyl)-2-furfuraldehyde is released, resulting in a glycated enzyme
-
-
?
maltoheptaose + 6 H2O
7 beta-D-glucose
maltoheptaose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltoheptaose + H2O
maltohexaose + D-glucose
maltohexaose + 5 H2O
6 beta-D-glucose
maltohexaose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
maltononaose + H2O
maltooctaose + beta-D-glucose
-
-
-
-
?
maltooctaose + H2O
maltoheptaose + beta-D-glucose
-
-
-
-
?
maltooligomers + H2O
? + beta-D-glucose
substrate specificity
-
-
r
maltooligosaccharide + H2O
beta-D-glucose
maltooligosaccharides + H2O
maltooligosaccharides + beta-D-glucose
maltopentadecaose + H2O
maltotetradecaose + beta-D-glucose
-
low activity
-
-
?
maltopentaose + 4 H2O
5 beta-D-glucose
maltopentaose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
maltose + H2O
2 beta-D-glucose
maltose + H2O
2 D-glucose
maltose + H2O
beta-D-glucose + D-glucose
maltose + H2O
D-glucose + ?
maltotetraose + 3 H2O
4 beta-D-glucose
-
-
-
?
maltotetraose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
maltotetraose + H2O
maltotriose + D-glucose
-
-
-
?
maltotriose + 2 H2O
3 beta-D-glucose
maltotriose + H2O
3 D-glucose
AAE85601
-
-
-
?
maltotriose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltotriose + H2O
maltose + beta-D-glucose
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + glucose
methyl-alpha-D-glucoside + H2O
methanol + alpha-D-glucose
nigerose + H2O
2 alpha-D-glucose
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
pectin + H2O
pectin + beta-D-glucose
-
-
-
-
?
phenyl alpha-glucoside + H2O
?
-
-
-
-
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
potato starch + H2O
beta-D-glucose + ?
-
-
-
-
?
pullulan + H2O
beta-D-glucose + ?
-
182% of activity with soluble starch
-
-
?
pullulan + H2O
beta-D-glucose + pullulan
-
-
-
-
?
pullulan + H2O
pullulan + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
raw potato starch + H2O
?
-
-
-
?
rice starch + H2O
beta-D-glucose + ?
-
-
-
-
?
short-chain amylose + H2O
beta-D-glucose + short-chain amylose
-
-
-
-
?
soluble potato starch + H2O
?
soluble starch + H2O
beta-D-glucose + ?
soluble starch + H2O
beta-D-glucose + soluble starch
starch + H2O
beta-D-glucose + ?
starch + H2O
D-glucose + ?
starch + H2O
starch + beta-D-glucose
sucrose + H2O
?
-
lower activity
-
-
?
sucrose + H2O
D-glucose + D-fructose
sweet potato starch + H2O
beta-D-glucose + ?
-
-
-
-
?
trehalose + H2O
D-glucose
-
-
-
-
?
turanose + H2O
D-fructose + D-glucose
-
-
-
-
?
wheat starch + H2O
beta-D-glucose + ?
-
-
-
-
?
xylan + H2O
xylan + beta-D-glucose
-
-
-
-
?
additional information
?
-
4 glucose
glucooligosaccharide + 3 H2O
-
reversion or condensation reactions are observed when glucoamylase is incubated with 10% glucose
-
-
r
4 glucose
glucooligosaccharide + 3 H2O
-
reversion or condensation reactions are observed when glucoamylase is incubated with 10% glucose
-
-
r
4 glucose
glucooligosaccharide + 3 H2O
-
reversion or condensation reactions are observed when glucoamylase is incubated with 10% glucose
-
-
r
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
12% of activity with starch
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
6% of the activity with maltose
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
alpha-cyclodextrin + H2O
?
-
-
-
?
alpha-cyclodextrin + H2O
?
-
-
-
-
?
alpha-cyclodextrin + H2O
alpha-cyclodextrin + beta-D-glucose
-
-
-
-
?
alpha-cyclodextrin + H2O
alpha-cyclodextrin + beta-D-glucose
-
-
-
-
?
alpha-cyclodextrin + H2O
glucose + ?
-
no activity
-
-
?
alpha-cyclodextrin + H2O
glucose + ?
-
-
-
-
?
alpha-cyclodextrin + H2O
glucose + ?
-
6% of the activity with maltose
-
-
?
amylopectin
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
from potato
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
best substrate, from potatoes or corn
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
amylopectin + beta-D-glucose
-
-
-
-
?
amylopectin + H2O
amylopectin + beta-D-glucose
-
preferred substrate
-
-
?
amylopectin + H2O
amylopectin + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose, best substrate
-
-
?
amylopectin + H2O
amylopectin + beta-D-glucose
94% of activity with amylose
-
-
?
amylopectin + H2O
beta-D-glucose + ?
-
933% of activity with soluble starch
-
-
?
amylopectin + H2O
beta-D-glucose + ?
-
-
-
-
?
amylopectin + H2O
beta-D-glucose + ?
-
100% of activity with soluble starch from potato
-
-
?
amylopectin + H2O
beta-D-glucose + ?
-
104% of activity with soluble starch from potato
-
-
?
amylopectin + H2O
beta-D-glucose + ?
-
-
-
-
?
amylopectin + H2O
beta-D-glucose + ?
-
104% of activity with soluble starch from potato
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
84% of the activity with starch
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
85% of activity with starch
-
-
?
amylopectin + H2O
D-glucose + ?
-
best substrate
-
-
?
amylopectin + H2O
D-glucose + ?
-
best substrate
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
high activity
-
-
?
amylopectin + H2O
D-glucose + ?
Cephalosporium eichhorniae
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
potato amylopectin
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
beta-glucose
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
-
-
?
amylose + H2O
?
-
-
-
-
?
amylose + H2O
?
-
-
-
-
?
amylose + H2O
?
-
-
-
-
?
amylose + H2O
?
from potato
-
-
?
amylose + H2O
?
from potato
-
-
?
amylose + H2O
?
from potato
-
-
?
amylose + H2O
?
-
-
-
-
?
amylose + H2O
?
-
low activity
-
-
?
amylose + H2O
?
-
-
-
-
?
amylose + H2O
amylose + beta-D-glucose
-
low activity
-
-
?
amylose + H2O
amylose + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
amylose + H2O
amylose + beta-D-glucose
preferred substrate
-
-
?
amylose + H2O
beta-D-glucose + ?
-
187% of activity with soluble starch
-
-
?
amylose + H2O
beta-D-glucose + ?
-
-
-
-
?
amylose + H2O
beta-D-glucose + ?
-
60% of activity with soluble starch from potato
-
-
?
amylose + H2O
beta-D-glucose + ?
-
74% of activity with soluble starch from potato
-
-
?
amylose + H2O
beta-D-glucose + ?
-
13% of activity with starch
-
-
?
amylose + H2O
beta-D-glucose + ?
-
-
-
-
?
amylose + H2O
beta-D-glucose + ?
-
63% of activity with soluble starch from potato
-
-
?
amylose + H2O
D-glucose + ?
-
best substrate
-
-
?
amylose + H2O
D-glucose + ?
-
-
-
-
?
amylose + H2O
D-glucose + ?
-
-
-
-
?
amylose + H2O
D-glucose + ?
-
-
-
-
?
amylose + H2O
D-glucose + ?
-
-
-
-
?
amylose + H2O
D-glucose + ?
potato amylose type III
-
-
?
amylose + H2O
D-glucose + ?
-
-
-
?
amylose + H2O
D-glucose + ?
-
-
-
?
amylose + H2O
D-glucose + ?
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
61% of the activity with starch
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
beta-glucose
?
amylose + H2O
glucose + ?
-
93% of the activity with starch
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
31% of the activity with starch
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
Cephalosporium eichhorniae
-
-
-
-
?
amylose + H2O
glucose + ?
-
short-chain
-
-
?
amylose + H2O
glucose + ?
-
short-chain
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
beta-glucose
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
beta-glucose
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
amylose + H2O
glucose + ?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
no activity
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
6% of the activity with maltose
-
-
?
dextran + H2O
?
-
-
-
-
?
dextran + H2O
?
-
no activity
-
-
?
dextran + H2O
?
-
-
-
-
?
dextrin + 6 H2O
7 beta-D-glucose
-
89% of activity with soluble starch from potato
-
-
?
dextrin + 6 H2O
7 beta-D-glucose
-
91% of activity with soluble starch from potato
-
-
?
dextrin + 6 H2O
7 beta-D-glucose
-
84% of activity with soluble starch from potato
-
-
?
dextrin + 6 H2O
7 D-glucose
-
-
-
-
?
dextrin + 6 H2O
7 D-glucose
-
the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
dextrin + 6 H2O
7 D-glucose
-
potato dextrin
-
-
?
dextrin + 6 H2O
7 D-glucose
-
potato dextrin, the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
dextrin + 6 H2O
7 D-glucose
a mixture of shorter linear and branched dextrin chains is hydrolyzed at the nonreducing ends into glucose
-
-
?
dextrin + 6 H2O
7 D-glucose
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
beta-limit dextrin
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
beta-limit dextrin
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
beta-limit dextrin
-
-
?
dextrin + H2O
?
-
beta-limit dextrin
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
beta-limit dextrin
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
-
-
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
-
90% of activity with soluble starch from potato
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
-
103% of activity with soluble starch from potato
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
-
150% of activity with starch
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
-
96% of activity with soluble starch from potato
-
-
?
glycogen + H2O
?
lower activity
-
-
?
glycogen + H2O
?
lower activity
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
82% of the activity with starch
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
shellfish glycogen, sweet-corn phytoglycogen, skate liver glycogen, human muscle glycogen, rabbit muscle glycogen, cat liver glycogen, cat liver glycogen. Incomplete conversion to glucose in absence of alpha-amylase
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
?
glycogen + H2O
glucose + ?
-
amylose A, n = 25 and amylose B, n = 130
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
Endomycopsis fibuligera
-
-
-
?
glycogen + H2O
glucose + ?
Endomycopsis fibuligera Y1
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
shellfish glycogen, sweet-corn phytoglycogen, skate liver glycogen, human muscle glycogen, rabbit muscle glycogen, cat liver glycogen, cat liver glycogen. Incomplete conversion to glucose in absence of alpha-amylase
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
beta-glucose
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glucose + ?
-
-
-
-
?
glycogen + H2O
glycogen + beta-D-glucose
-
-
-
-
?
glycogen + H2O
glycogen + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
glycogen + H2O
glycogen + beta-D-glucose
87% of activity with amylose
-
-
?
isomaltopentaose + H2O
?
-
-
-
-
?
isomaltopentaose + H2O
?
-
-
-
-
?
isomaltose
isomaltooligosaccharide
-
reversion or condensation reactions are observed when glucoamylase is incubated with 10% isomaltose
-
-
r
isomaltose
isomaltooligosaccharide
-
reversion or condensation reactions are observed when glucoamylase is incubated with 10% isomaltose
-
-
r
isomaltose
isomaltooligosaccharide
-
reversion or condensation reactions are observed when glucoamylase is incubated with 10% isomaltose
-
-
r
isomaltose + H2O
?
-
assay at pH 5.5, 40°C
-
-
?
isomaltose + H2O
?
low activity
-
-
?
isomaltose + H2O
beta-D-glucose
-
-
-
-
?
isomaltose + H2O
beta-D-glucose
-
-
-
r
isomaltose + H2O
glucose
-
-
-
-
?
isomaltose + H2O
glucose
-
10% of the activity with starch
-
-
?
isomaltose + H2O
glucose
-
-
-
-
?
isomaltose + H2O
glucose
-
-
-
-
?
isomaltose + H2O
glucose
-
-
-
-
?
isomaltose + H2O
glucose
-
-
-
-
?
isomaltose + H2O
glucose
-
-
-
-
?
isomaltose + H2O
glucose
-
-
-
-
?
isomaltose + H2O
glucose
-
-
-
-
?
isomaltotetraose + H2O
?
-
-
-
-
?
isomaltotetraose + H2O
?
-
-
-
-
?
isomaltotriose + H2O
?
-
-
-
-
?
isomaltotriose + H2O
?
-
-
-
-
?
maltoheptaose + 6 H2O
7 beta-D-glucose
-
-
-
?
maltoheptaose + 6 H2O
7 beta-D-glucose
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
maltohexaose + D-glucose
-
-
-
-
?
maltoheptaose + H2O
maltohexaose + D-glucose
-
-
-
?
maltoheptaose + H2O
maltohexaose + D-glucose
-
-
-
-
?
maltoheptaose + H2O
maltohexaose + D-glucose
-
-
-
-
?
maltoheptaose + H2O
maltohexaose + D-glucose
-
-
-
-
?
maltohexaose + 5 H2O
6 beta-D-glucose
-
-
-
?
maltohexaose + 5 H2O
6 beta-D-glucose
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
-
-
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
-
-
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
-
-
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
-
-
-
-
?
maltooligosaccharide + H2O
beta-D-glucose
-
55% of activity with soluble starch from potato
-
-
?
maltooligosaccharide + H2O
beta-D-glucose
-
49% of activity with soluble starch from potato
-
-
?
maltooligosaccharide + H2O
beta-D-glucose
-
54% of activity with soluble starch from potato
-
-
?
maltooligosaccharides + H2O
maltooligosaccharides + beta-D-glucose
-
high activity
-
-
?
maltooligosaccharides + H2O
maltooligosaccharides + beta-D-glucose
-
high activity
-
-
?
maltopentaose + 4 H2O
5 beta-D-glucose
-
-
-
?
maltopentaose + 4 H2O
5 beta-D-glucose
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
?
maltopentaose + H2O
?
-
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
-
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
low activity
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
-
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
-
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
preferred substrate
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
preferred substrate
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
-
-
-
?
maltose + H2O
2 beta-D-glucose
-
-
-
?
maltose + H2O
2 beta-D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
AAE85601
-
-
-
?
maltose + H2O
2 glucose
-
19% of the activity with starch
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
40% of the activity with starch
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
2 glucose
-
-
-
-
?
maltose + H2O
?
-
-
-
-
?
maltose + H2O
?
-
-
-
-
?
maltose + H2O
?
-
-
-
-
?
maltose + H2O
?
-
-
-
-
?
maltose + H2O
?
-
-
-
-
?
maltose + H2O
?
low activity
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
product analysis
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
product analysis
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
substrate of isozyme GA-II, no activity with isozyme GA-I
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
2% of activity with soluble starch from potato
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
17% of activity with soluble starch from potato
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
r
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
14% of activity with amylose
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
24% of activity with soluble starch from potato
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltose + H2O
D-glucose + ?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
60% of the activity with maltose
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
?
maltotetraose + H2O
?
-
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
-
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
low activity
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
-
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
-
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
-
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
preferred substrate
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
preferred substrate
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
-
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
-
-
-
?
maltotriose + 2 H2O
3 beta-D-glucose
-
-
-
-
?
maltotriose + 2 H2O
3 beta-D-glucose
-
-
-
-
?
maltotriose + 2 H2O
3 beta-D-glucose
-
-
-
?
maltotriose + 2 H2O
3 beta-D-glucose
-
-
-
?
maltotriose + 2 H2O
3 beta-D-glucose
-
-
-
-
?
maltotriose + 2 H2O
3 beta-D-glucose
-
-
-
-
?
maltotriose + 2 H2O
3 beta-D-glucose
-
-
-
-
?
maltotriose + 2 H2O
3 beta-D-glucose
-
-
-
-
?
maltotriose + H2O
?
-
-
-
-
?
maltotriose + H2O
?
-
-
-
?
maltotriose + H2O
?
-
-
-
?
maltotriose + H2O
maltose + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
maltotriose + H2O
maltose + beta-D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + beta-D-glucose
exoglycosidic hydrolysis of terminal glucose in forward reaction, preferred substrate, synthesis of isomaltose from beta-D-glucose in the reverse reaction with low activity
anomeric product configuration analysis at 80°C
-
r
maltotriose + H2O
maltose + beta-D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + beta-D-glucose
40% of activity with amylose
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
47% of the activity with starch
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
46% of the activity with starch
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
68% of the activity with starch
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
-
-
-
?
maltotriose + H2O
maltose + glucose
-
hydrolysis by a multi-chain mechanism
-
-
?
methyl-alpha-D-glucoside + H2O
methanol + alpha-D-glucose
-
-
-
-
?
methyl-alpha-D-glucoside + H2O
methanol + alpha-D-glucose
-
no activity
-
-
?
methyl-alpha-D-glucoside + H2O
methanol + alpha-D-glucose
-
5% of the activity with maltose
-
-
?
nigerose + H2O
2 alpha-D-glucose
-
-
-
-
?
nigerose + H2O
2 alpha-D-glucose
-
-
-
-
?
nigerose + H2O
2 alpha-D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
Cephalosporium eichhorniae
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
Endomycopsis fibuligera
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
Schwanniomyces castellii
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
Thermochaetoides thermophila
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
panose + H2O
?
-
-
-
-
?
panose + H2O
?
-
14% of the activity with starch
-
-
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
-
-
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
-
-
-
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
-
-
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
-
-
-
?
pullulan + H2O
?
-
assay at pH 5.5, 40°C
-
-
?
pullulan + H2O
?
-
52% of the activity with starch
-
-
?
pullulan + H2O
?
-
1.46% of the activity with starch
-
-
?
pullulan + H2O
?
-
no activity
-
-
?
pullulan + H2O
?
low activity
-
-
?
pullulan + H2O
?
low activity
-
-
?
pullulan + H2O
?
low activity
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
low activity
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
no activity
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
soluble potato starch + H2O
?
-
-
-
-
?
soluble potato starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
?
soluble starch + H2O
?
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + ?
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + ?
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + ?
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + ?
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + ?
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + ?
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + soluble starch
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + soluble starch
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + soluble starch
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + soluble starch
-
-
-
-
?
soluble starch + H2O
beta-D-glucose + soluble starch
-
-
-
-
?
starch + H2O
?
-
-
-
?
starch + H2O
?
-
raw starch
-
-
?
starch + H2O
?
best substrate, soluble starch and gelatinized raw sago starch
-
-
?
starch + H2O
?
-
soluble starch, which is the best substrate, and raw starch from cassava, potato, and corn
-
-
?
starch + H2O
?
best substrate, soluble starch and gelatinized raw sago starch
-
-
?
starch + H2O
?
-
corn starch, potato starch, hydrolyzed potato starch, and rice starch
-
-
?
starch + H2O
?
-
corn starch, potato starch, hydrolyzed potato starch, and rice starch
-
-
?
starch + H2O
?
standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch
-
-
?
starch + H2O
?
standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch
-
-
?
starch + H2O
?
standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch
-
-
?
starch + H2O
?
soluble starch and raw starch from sweet potato and corn
-
-
?
starch + H2O
?
-
soluble starch
-
-
?
starch + H2O
?
-
soluble starch
-
-
?
starch + H2O
?
-
recombinant N-terminal subunit of human small intestinal maltase-glucoamylase is used to explore digestion of native starches from different botanical sources, e.g. normal and waxy maize, wheat, potato, pea, banana, and tapioca starches, and high-amylose maize starch with 50-70% amylose, substrate specificity, overview
-
-
?
starch + H2O
?
-
soluble starch
-
-
?
starch + H2O
?
soluble starch
-
-
?
starch + H2O
?
raw starch
-
-
?
starch + H2O
?
raw starch, different raw starch flours, e.g. raw cassava starch or raw potato starch, the enzyme also hydrolyzes soluble starch
-
-
?
starch + H2O
?
starch-digesting glucoamylase PoGA15A shows high enzymatic activity with raw starch from raw corn and cassava flours and towards various raw starches. Enzymatic activities towards raw rice (211.3%), corn (206.7%), and cassava (100%) are much higher than for other tested raw starches, including potato (90.8%), buck wheat (59.9%), and sweet potato (25.3%). Direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol. Best substrate is soluble starch (706.8%). Effective hydrolysis of raw starch flour by the recombinant rPoGA15A enzyme preparation and alpha-amylase, kinetics at pH 4.5 and 40°C, detailed overview
-
-
?
starch + H2O
?
raw starch
-
-
?
starch + H2O
?
raw starch, different raw starch flours, e.g. raw cassava starch or raw potato starch, the enzyme also hydrolyzes soluble starch
-
-
?
starch + H2O
?
raw starch
-
-
?
starch + H2O
?
starch-digesting glucoamylase PoGA15A shows high enzymatic activity with raw starch from raw corn and cassava flours and towards various raw starches. Enzymatic activities towards raw rice (211.3%), corn (206.7%), and cassava (100%) are much higher than for other tested raw starches, including potato (90.8%), buck wheat (59.9%), and sweet potato (25.3%). Direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol. Best substrate is soluble starch (706.8%). Effective hydrolysis of raw starch flour by the recombinant rPoGA15A enzyme preparation and alpha-amylase, kinetics at pH 4.5 and 40°C, detailed overview
-
-
?
starch + H2O
?
-
starch granules from various botanical sources: rice, wheat, potato, sweet potato, cassava, and maize
-
-
?
starch + H2O
?
-
soluble starch
-
-
?
starch + H2O
?
-
Paselli starch or soluble starch
-
-
?
starch + H2O
?
soluble starch
-
-
?
starch + H2O
?
soluble starch, and low activity with raw corn starch
-
-
?
starch + H2O
beta-D-glucose + ?
-
raw sago starch
-
-
?
starch + H2O
beta-D-glucose + ?
-
activities with starch in descending order, wheat starch, rice starch, sago starch, potato starch, soluble starch, tapioca starch and corn starch
-
-
?
starch + H2O
beta-D-glucose + ?
Arachniotus sp.
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
Mucor rouxians
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
Mucor rouxians
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
maize starch, 105% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
native starch from potato, 105% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
rice starch, 110% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
maize starch, 83% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
native starch from potato, 92% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
rice starch, 95% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
glucoamylase is an exo-amylolytic enzyme that cleaves alpha-1,4-linked and alpha-1,6-linked glucose from starch
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
Thermochaetoides thermophila
soluble starch
-
-
?
starch + H2O
beta-D-glucose + ?
Thermochaetoides thermophila CT2
soluble starch
-
-
?
starch + H2O
beta-D-glucose + ?
-
strongest activity with soluble starch
-
-
?
starch + H2O
beta-D-glucose + ?
-
maize starch, 109% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
native starch from potato, 105% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
rice starch, 123% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
soluble and raw starch
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme hydrolyzes glucosidic bonds in amylase, amylopectin, and maltoligosaccharides
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
sole product
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
sole product
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
gelatinized and ungelatinized substrates: soluble, potato, sweet potato, and corn starch granules, determination of optimal substrate concentration, substrate specificity, overview
-
-
?
starch + H2O
D-glucose + ?
-
raw and cooked soluble starch from potato, no activity with corn starch and sweet potato starch
-
-
?
starch + H2O
D-glucose + ?
Endomycopsis fibuligera
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
soluble starch
-
-
?
starch + H2O
D-glucose + ?
-
important industrial enzyme that removes the glucose units from the non-reducing chain-ends of starch and glycogen by hydrolyzing alpha-1,4 linkages consecutively
-
-
?
starch + H2O
D-glucose + ?
-
-
sole end-product
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
?
starch + H2O
D-glucose + ?
-
one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine
-
-
?
starch + H2O
D-glucose + ?
one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme is responsible for the final step of mammalian starch digestion leading to the release of D-glucose
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
soluble starch
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
soluble corn and wheat starch granules
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme preferentially hydrolyzes all the starch substrates, soluble and raw. High substrate specificity is demonstrated towards soluble starch
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme preferentially hydrolyzes all the starch substrates, soluble and raw. High substrate specificity is demonstrated towards soluble starch
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
soluble starch
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme plays a role in the saccharification and fermentation of amylaceous substrates, notably in high cell density processes
-
-
?
starch + H2O
D-glucose + ?
-
soluble starch
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme plays a role in the saccharification and fermentation of amylaceous substrates, notably in high cell density processes
-
-
?
starch + H2O
D-glucose + ?
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
300fold preference for the alpha-1,4-glucosidic linkage over the alpha-1,6-glucosidic linkage
-
-
?
starch + H2O
glucose + ?
catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
-
-
-
?
starch + H2O
glucose + ?
-
with concentrated solutions of D-glucose, 10% w/v and 30% w/v, small amounts of isomaltose are produced as the sole reversion product
-
-
?
starch + H2O
glucose + ?
-
waxy-maize starch, waxy-sorghum starch, floridean starch. Incomplete conversion to glucose in absence of alpha-amylase
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
soluble
beta-glucose and maltooligosaccharides
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
raw starch and gelatinized starch
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
raw starch and gelatinized starch
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
wheat starch, potato starch, corn starch
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
wheat starch, potato starch, corn starch
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
soluble
-
?
starch + H2O
glucose + ?
-
soluble
-
?
starch + H2O
glucose + ?
-
-
-
-
?
starch + H2O
glucose + ?
-
-
-
-
?
starch + H2O
glucose + ?
-
soluble
beta-glucose
?
starch + H2O
glucose + ?
-
soluble
beta-glucose
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
soluble
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
waxy-maize starch, waxy-sorghum starch, floridean starch. Incomplete conversion to glucose in absence of alpha-amylase
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
-
-
-
?
starch + H2O
glucose + ?
-
soluble
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
soluble
-
-
?
starch + H2O
glucose + ?
-
soluble
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme contains 7 subsites for substrate binding, subsite affinities
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
soluble starch, raw rice starch, and raw wheat starch, the latter is the preferred substrate
-
-
?
starch + H2O
starch + beta-D-glucose
-
soluble starch, raw rice starch, and raw wheat starch, the latter is the preferred substrate
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
soluble starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of the starch chain, substrates corn cobs, maize starch, soluble starch, and wheat bran
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
hydrolysis of solid-state starch from raw chestnut homogenate, composition, 30% of the raw chestnut is starch, overview
-
-
?
starch + H2O
starch + beta-D-glucose
-
soluble potato starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme contains 7 subsites for substrate binding, subsite affinities
-
-
?
starch + H2O
starch + beta-D-glucose
-
soluble potato starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme contains 7 subsites for substrate binding, subsite affinities
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme contains 7 subsites for substrate binding, subsite affinities
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme contains 7 subsites for substrate binding, subsite affinities
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
product analysis
-
?
starch + H2O
starch + beta-D-glucose
-
-
product analysis
-
?
starch + H2O
starch + beta-D-glucose
-
soluble potato starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
16times and 29times higher activity with soluble starch compared to wheat or corn starch granules, respectively
-
-
?
starch + H2O
starch + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose, high activity
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
Mucor rouxians
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
Mucor rouxians
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
cooked corn starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
raw corn starch granules of different size, exoglycosidic hydrolysis of terminal glucose, determination of relation of granule surface area to adsorbed enzyme and activity including product liberation
-
-
?
starch + H2O
starch + beta-D-glucose
soluble starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the native enzyme shows low activity with raw starch due to a lack in starch binding domain
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
soluble starch, very low activity
-
-
?
starch + H2O
starch + beta-D-glucose
-
soluble starch, very low activity
-
-
?
starch + H2O
starch + beta-D-glucose
Thermochaetoides thermophila
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
3.3% of carbohydrate
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
additional information
?
-
-
the enzyme shows high affinity for the branched polysaccharides. It can digest raw starch
-
-
?
additional information
?
-
catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
-
-
?
additional information
?
-
-
catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
-
-
?
additional information
?
-
-
the hydrolysis reaction successively cleaves glucose residues from the nonreducing ends of starch, glycogen, and maltooligosaccharides
-
-
?
additional information
?
-
-
the hydrolysis reaction successively cleaves glucose residues from the nonreducing ends of starch, glycogen, and maltooligosaccharides
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme is active on the following substrates in descending order: glycogen, amylopectin, corn starch, rice starch, wheat starch, maltose, amylose, dextrin, maltotriose, raffinose, and sucrose
-
-
?
additional information
?
-
glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
-
-
?
additional information
?
-
-
glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
-
-
?
additional information
?
-
-
the enzyme is active on the following substrates in descending order: glycogen, amylopectin, corn starch, rice starch, wheat starch, maltose, amylose, dextrin, maltotriose, raffinose, and sucrose
-
-
?
additional information
?
-
glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
-
-
?
additional information
?
-
-
regulation mechanisms of enzyme expression, overview
-
-
?
additional information
?
-
-
immobilization of the enzyme on polyaniline polymer results in improved catalytic performance with decreased temperature optimum, and increased thermal stability and catalytic efficiency, overview
-
-
?
additional information
?
-
-
modelling of potato starch saccharification by Aspergillus niger, influences of assay conditions on activity, overview
-
-
?
additional information
?
-
-
glucoamylase functions via transient dimer formation during hydrolysis of insoluble substrates and address the question of the cooperative effect of starch binding and hydrolysis
-
-
?
additional information
?
-
-
modelling of potato starch saccharification by Aspergillus niger, influences of assay conditions on activity, overview
-
-
?
additional information
?
-
-
regulation mechanisms of enzyme expression, overview
-
-
?
additional information
?
-
-
different regulation mechanisms, the regulation is influenced by carbohydrate degradation and consumption under different culture conditions, overview
-
-
?
additional information
?
-
the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
-
-
?
additional information
?
-
-
the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
-
-
?
additional information
?
-
the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
-
-
?
additional information
?
-
the strain WZ99 glucoamylase shows a substrate bias of soluble starch > pullulan > cycledextrin. The enzyme degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
-
-
?
additional information
?
-
-
pullulan is a poor substrate, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme has debranching activity
-
-
?
additional information
?
-
poor activity with pullulan and laminarin
-
-
?
additional information
?
-
poor activity with pullulan and laminarin
-
-
?
additional information
?
-
-
substrate specificity overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the glucoamylase also shows steroidal saponin-rhamnosidase activity, EC 3.2.1.40, being able to hydrolyze the terminal rhamnosyl of steroidal saponins and the sugar chain at the C-3 position of spirostanosides, the enzyme also hydrolyzed the terminal rhamnosyl residues of the sugar chain at the C-3 position while retaining the glucosyl residues at the C-26 position of furostanosides, substrate specificity, overview
-
-
?
additional information
?
-
endophytic fungus EF6
-
soluble starch is the best substrate, various raw starches, i.e. soluble starch, corn, tapioca, wheat, rice, sticky rice starch, are used as substrates
-
-
?
additional information
?
-
-
enzyme shows broad substrate specificity and raw starch hydrolyzing activity
-
-
?
additional information
?
-
-
key intestinal enzymes involved in the breakdown of glucose
-
-
?
additional information
?
-
-
the key intestinal enzyme involved in the breakdown of glucose oligosaccharides in the small intestine
-
-
?
additional information
?
-
structure of the N-terminal catalytic subunit and the active site, and basis of inhibition and substrate specificity, overview, the catalytic subunit shows higher affinity for longer maltose oligosaccharides
-
-
?
additional information
?
-
-
structure of the N-terminal catalytic subunit and the active site, and basis of inhibition and substrate specificity, overview, the catalytic subunit shows higher affinity for longer maltose oligosaccharides
-
-
?
additional information
?
-
-
analysis of the basic catalytic properties of the N-terminal subunit of MGAM (ntMGAM) on the hydrolysis of glucan substrates and compared it with those of human native MGAM
-
-
?
additional information
?
-
-
no activity with cyclodextrins and laminarin
-
-
?
additional information
?
-
-
key enzyme in ripening and production of good taste in fermented tofu production, overview
-
-
?
additional information
?
-
-
substrate specificities of isozymes GA-I and GA-II, cyclodextrins are poor substrates, overview
-
-
?
additional information
?
-
-
no activity with sucrose, 4-nitrophenyl-beta-D-maltoside, methyl-beta-D-glucopyranoside, pullulan, alpha-cyclodextrin, beta-cyclodextrin, and trehalose
-
-
?
additional information
?
-
-
glucoamylase hydrolyzes alpha-1,4- and alpha-1,6-glycosidic linkages from the non-reducing ends of starch molecule, and specifically forms D-glucose units
-
-
?
additional information
?
-
-
glucoamylase hydrolyzes alpha-1,4- and alpha-1,6-glycosidic linkages from the non-reducing ends of starch molecule, and specifically forms D-glucose units
-
-
?
additional information
?
-
the enzyme shows a broad substrate specificity
-
-
?
additional information
?
-
the enzyme shows a broad substrate specificity
-
-
?
additional information
?
-
the intracellular enzyme shows a unique substrate specificity compared to already known glucoamylases, in addition to the hydrolysis of branched and linear alpha-glucans, the purified enzyme preferentially attacks maltotriose, overview, oligossaccharides Dp2, Dp4, Dp5, Dp6, and Dp7 as well as isomaltose, panose, and isopanose are poor substrates
-
-
?
additional information
?
-
-
the enzyme is responsible for much of the isomaltase and maltase activities in the intestine of the frog
-
-
?
additional information
?
-
the enzyme contains a carbohydrate-binding module, which functions independently to assist the carbohydrate-active enzyme, structure of a family 21 CBM from the starch-binding domain of Rhizopus oryzae glucoamylase, RoCBM21, determined by NMR spectroscopy
-
-
?
additional information
?
-
-
the enzyme consists of at least two domains, one for adsorption to the starch molecule in the N-terminal portion, and the other for catalyzing starch degradation in the C-terminal portion
-
-
?
additional information
?
-
-
reaction of the amyloglucosidase in concert with sweet almond beta-glucosidase, EC 3.2.1.21, to hydrolyze curcumin and eugenol in acetate buffer, method optimization, NMR product determinations, overview
-
-
?
additional information
?
-
bifunctional enzyme performing hydrolysis or transglycosylation depending on the substrate
-
-
?
additional information
?
-
-
bifunctional enzyme performing hydrolysis or transglycosylation depending on the substrate
-
-
?
additional information
?
-
-
no hydrolysis of alpha-1,6 linkages
-
-
?
additional information
?
-
-
no hydrolysis of alpha-1,6 linkages
-
-
?
additional information
?
-
-
glucoamylase is an exoglycosidase responsible for hydrolyzing the terminal alpha-1,4 glucosidic bonds of dextrins and related oligo- and polysaccharides, the reaction involves a proton transfer by acid catalysis, followed by formation of a transition state analogous to an oxocarbonium ion, and finally, a base-catalyzed nucleophilic attack of water, glutamic acid present in different regions of the enzyme-active site acts as the acid and base catalysts required for the reaction
-
-
?
additional information
?
-
the enzyme binds poorly to insoluble starch
-
-
?
additional information
?
-
-
no hydrolysis of alpha-1,6 linkages
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl alpha-D-glucopyranoside
-
-
?
additional information
?
-
-
no substrate: 4-nitrophenyl alpha-D-glucopyranoside
-
-
?
additional information
?
-
-
no activity with pullulan, dextran, and isomaltose
-
-
?
additional information
?
-
-
no activity with pullulan, dextran, and isomaltose
-
-
?
additional information
?
-
-
enzyme can attack alpha-1,4-glycosidic linkages and alpha-1,6-glycosidic linkages. The velocity of oligosaccharide hydrolysis decreases with a decrease in size of substrate
-
-
?
additional information
?
-
-
displays broad substrate specificity by cleaving alpha-1,4- and alpha-1,6-glycosidic linkages in starch, amylopectin, amylose and pullulan. No activity is observed on alpha-cyclodextrin
-
-
?
additional information
?
-
-
displays broad substrate specificity by cleaving alpha-1,4- and alpha-1,6-glycosidic linkages in starch, amylopectin, amylose and pullulan. No activity is observed on alpha-cyclodextrin
-
-
?
additional information
?
-
-
no hydrolysis of alpha-1,6 linkages
-
-
?
additional information
?
-
-
no hydrolysis of alpha-1,6 linkages
-
-
?
additional information
?
-
-
the enzyme is an exo-hydrolase that attacks the substrate from the non-reducing end, producing glucose with beta-anomeric configuration, substrate specificity with substrates from different sources in descending activity order: Paselli starch, soluble starch, corn-amylopectin, glycogen, and amylose, no activity with pullulan, alpha-cyclodextrin, beta-cyclodextrin, and gamma-cyclodextrin, TaGA is not able to catalyze the formation of oligosaccharides, e.g., by transglycosylation with glucose as substrate
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl alpha-D-glucopyranoside
-
-
?
additional information
?
-
-
no substrate: 4-nitrophenyl alpha-D-glucopyranoside
-
-
?
additional information
?
-
no substrate: 4-nitrophenyl alpha-D-glucopyranoside
-
-
?
additional information
?
-
branched glucooligosaccharides with a DP between five and twelve are produced from potato amylopectin digestion by alpha-amylase from Bacillus licheniformis and used as substrates for comparing their degradation by the glucoamylase GA2 from Hypocrea jecorina, analysis of the mode of action of the glucoamylase, substrate specificity, overview. The majority of branched gluco-oligosaccharides larger than DP7 have multiple branching points. The enzyme is active versus alpha-1,4- and alpha-1,6-linkages
-
-
?
additional information
?
-
branched glucooligosaccharides with a DP between five and twelve are produced from potato amylopectin digestion by alpha-amylase from Bacillus licheniformis and used as substrates for comparing their degradation by the glucoamylase GA2 from Hypocrea jecorina, analysis of the mode of action of the glucoamylase, substrate specificity, overview. The majority of branched gluco-oligosaccharides larger than DP7 have multiple branching points. The enzyme is active versus alpha-1,4- and alpha-1,6-linkages
-
-
?
additional information
?
-
the enzyme degrades alpha-1,4- and alpha-1,6-glycosidic linkages in various polysaccharides and also malto-oligosaccharides, substrate specificity, overview. No activity with beta-cyclodextrin, alpha-cyclodextrin, trehalose, kojibiose, and nigerose
-
-
?
additional information
?
-
-
the enzyme degrades alpha-1,4- and alpha-1,6-glycosidic linkages in various polysaccharides and also malto-oligosaccharides, substrate specificity, overview. No activity with beta-cyclodextrin, alpha-cyclodextrin, trehalose, kojibiose, and nigerose
-
-
?
additional information
?
-
the enzyme degrades alpha-1,4- and alpha-1,6-glycosidic linkages in various polysaccharides and also malto-oligosaccharides, substrate specificity, overview. No activity with beta-cyclodextrin, alpha-cyclodextrin, trehalose, kojibiose, and nigerose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4 glucose
glucooligosaccharide + 3 H2O
amylopectin + H2O
beta-D-glucose + ?
amylose + H2O
beta-D-glucose + ?
dextrin + 6 H2O
7 beta-D-glucose
dextrin + 6 H2O
7 D-glucose
glycogen + 3 H2O
4 beta-D-glucose
isomaltose
isomaltooligosaccharide
maltodextrin + H2O
beta-D-glucose + ?
-
-
-
-
?
maltooligosaccharide + H2O
beta-D-glucose
maltose + H2O
beta-D-glucose + D-glucose
maltotriose + 2 H2O
3 beta-D-glucose
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
starch + H2O
D-glucose + ?
starch + H2O
starch + beta-D-glucose
additional information
?
-
4 glucose
glucooligosaccharide + 3 H2O
-
reversion or condensation reactions are observed when glucoamylase is incubated with 10% glucose
-
-
r
4 glucose
glucooligosaccharide + 3 H2O
-
reversion or condensation reactions are observed when glucoamylase is incubated with 10% glucose
-
-
r
amylopectin + H2O
beta-D-glucose + ?
-
-
-
-
?
amylopectin + H2O
beta-D-glucose + ?
-
100% of activity with soluble starch from potato
-
-
?
amylopectin + H2O
beta-D-glucose + ?
-
104% of activity with soluble starch from potato
-
-
?
amylopectin + H2O
beta-D-glucose + ?
-
104% of activity with soluble starch from potato
-
-
?
amylose + H2O
beta-D-glucose + ?
-
-
-
-
?
amylose + H2O
beta-D-glucose + ?
-
60% of activity with soluble starch from potato
-
-
?
amylose + H2O
beta-D-glucose + ?
-
74% of activity with soluble starch from potato
-
-
?
amylose + H2O
beta-D-glucose + ?
-
13% of activity with starch
-
-
?
amylose + H2O
beta-D-glucose + ?
-
63% of activity with soluble starch from potato
-
-
?
dextrin + 6 H2O
7 beta-D-glucose
-
89% of activity with soluble starch from potato
-
-
?
dextrin + 6 H2O
7 beta-D-glucose
-
91% of activity with soluble starch from potato
-
-
?
dextrin + 6 H2O
7 beta-D-glucose
-
84% of activity with soluble starch from potato
-
-
?
dextrin + 6 H2O
7 D-glucose
-
-
-
-
?
dextrin + 6 H2O
7 D-glucose
-
the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
-
-
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
-
90% of activity with soluble starch from potato
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
-
103% of activity with soluble starch from potato
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
-
150% of activity with starch
-
-
?
glycogen + 3 H2O
4 beta-D-glucose
-
96% of activity with soluble starch from potato
-
-
?
isomaltose
isomaltooligosaccharide
-
reversion or condensation reactions are observed when glucoamylase is incubated with 10% isomaltose
-
-
r
isomaltose
isomaltooligosaccharide
-
reversion or condensation reactions are observed when glucoamylase is incubated with 10% isomaltose
-
-
r
maltooligosaccharide + H2O
beta-D-glucose
-
55% of activity with soluble starch from potato
-
-
?
maltooligosaccharide + H2O
beta-D-glucose
-
49% of activity with soluble starch from potato
-
-
?
maltooligosaccharide + H2O
beta-D-glucose
-
54% of activity with soluble starch from potato
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
2% of activity with soluble starch from potato
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
17% of activity with soluble starch from potato
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
24% of activity with soluble starch from potato
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
-
-
-
?
starch + H2O
?
-
-
-
?
starch + H2O
?
-
raw starch
-
-
?
starch + H2O
?
raw starch
-
-
?
starch + H2O
?
raw starch
-
-
?
starch + H2O
?
raw starch
-
-
?
starch + H2O
?
soluble starch
-
-
?
starch + H2O
beta-D-glucose + ?
-
raw sago starch
-
-
?
starch + H2O
beta-D-glucose + ?
Arachniotus sp.
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
Mucor rouxians
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
maize starch, 105% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
native starch from potato, 105% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
rice starch, 110% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
maize starch, 83% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
native starch from potato, 92% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
rice starch, 95% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
glucoamylase is an exo-amylolytic enzyme that cleaves alpha-1,4-linked and alpha-1,6-linked glucose from starch
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
-
-
?
starch + H2O
beta-D-glucose + ?
-
strongest activity with soluble starch
-
-
?
starch + H2O
beta-D-glucose + ?
-
maize starch, 109% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
native starch from potato, 105% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
rice starch, 123% of activity with soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
soluble starch from potato
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
important industrial enzyme that removes the glucose units from the non-reducing chain-ends of starch and glycogen by hydrolyzing alpha-1,4 linkages consecutively
-
-
?
starch + H2O
D-glucose + ?
-
one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine
-
-
?
starch + H2O
D-glucose + ?
one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme is responsible for the final step of mammalian starch digestion leading to the release of D-glucose
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
-
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme plays a role in the saccharification and fermentation of amylaceous substrates, notably in high cell density processes
-
-
?
starch + H2O
D-glucose + ?
-
the enzyme plays a role in the saccharification and fermentation of amylaceous substrates, notably in high cell density processes
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
soluble starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of the starch chain, substrates corn cobs, maize starch, soluble starch, and wheat bran
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
Mucor rouxians
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
soluble starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
additional information
?
-
catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
-
-
?
additional information
?
-
-
catalyses the hydrolysis of the alpha-1,4 glycosidic bonds of starch
-
-
?
additional information
?
-
glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
-
-
?
additional information
?
-
-
glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
-
-
?
additional information
?
-
glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme
-
-
?
additional information
?
-
-
regulation mechanisms of enzyme expression, overview
-
-
?
additional information
?
-
-
glucoamylase functions via transient dimer formation during hydrolysis of insoluble substrates and address the question of the cooperative effect of starch binding and hydrolysis
-
-
?
additional information
?
-
-
regulation mechanisms of enzyme expression, overview
-
-
?
additional information
?
-
-
different regulation mechanisms, the regulation is influenced by carbohydrate degradation and consumption under different culture conditions, overview
-
-
?
additional information
?
-
-
key intestinal enzymes involved in the breakdown of glucose
-
-
?
additional information
?
-
-
the key intestinal enzyme involved in the breakdown of glucose oligosaccharides in the small intestine
-
-
?
additional information
?
-
-
analysis of the basic catalytic properties of the N-terminal subunit of MGAM (ntMGAM) on the hydrolysis of glucan substrates and compared it with those of human native MGAM
-
-
?
additional information
?
-
-
key enzyme in ripening and production of good taste in fermented tofu production, overview
-
-
?
additional information
?
-
-
glucoamylase hydrolyzes alpha-1,4- and alpha-1,6-glycosidic linkages from the non-reducing ends of starch molecule, and specifically forms D-glucose units
-
-
?
additional information
?
-
-
glucoamylase hydrolyzes alpha-1,4- and alpha-1,6-glycosidic linkages from the non-reducing ends of starch molecule, and specifically forms D-glucose units
-
-
?
additional information
?
-
-
the enzyme is responsible for much of the isomaltase and maltase activities in the intestine of the frog
-
-
?
additional information
?
-
-
glucoamylase is an exoglycosidase responsible for hydrolyzing the terminal alpha-1,4 glucosidic bonds of dextrins and related oligo- and polysaccharides, the reaction involves a proton transfer by acid catalysis, followed by formation of a transition state analogous to an oxocarbonium ion, and finally, a base-catalyzed nucleophilic attack of water, glutamic acid present in different regions of the enzyme-active site acts as the acid and base catalysts required for the reaction
-
-
?
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(+)-catechin
noncompetitive inhibition
(2S,3S,4R,5R)-1-((1S,2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydro-1H-selenophenium-1-yl)-2,4,5,7-tetrahydroxyheptan-3-yl sulfate
-
a structure analogue of salacinol, synthesis, overview
(2S,3S,4R,5R)-1-((1S,2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydro-1H-thiophenium-1-yl)-2,4,5,7-tetrahydroxyheptan-3-yl sulfate
-
a structure analogue of salacinol, synthesis, overview
(2S,3S,4S)-1-[(2S,3S,4S)-4-carboxy-2,3,4-trihydroxybutyl]-3,4-dihydroxy-2-methoxytetrahydrothiophenium
-
a salacinol derivative, salacinol is a sulfonium ion with an internal sulfate counterion, synthesis of a compound with the D-arabinitol configuration in the heterocyclic ring displayed by salacinol, overview
1,2,7-trihydroxyindolizidine
1,4-dideoxy-1,4-[(1-butyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-hexyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-octadecyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-octyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-tetradecyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-tetradecyl)-(R)-episulfoniumylidene]-D-arabinitol triflate
-
-
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episelenoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episulfoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]iminonium]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(R)-epi-seleniumylidene]-D-arabinitol inner salt
-
-
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(R)-epi-sulfoniumylidene]-D-arabinitol inner salt
-
-
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(S)-epi-seleniumylidene]-D-arabinitol inner salt
-
-
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episelenoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episulfoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]iminonium]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[1-(3-methyl)-butyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[[1-(6-ethoxy)-hexyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[[1-(9-methoxy)-nonyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,7-dihydroxyindolizidine
2-Amino-2-ethyl-1,3-propanediol
2-deoxy-1-ene-salacinol
-
synthesis, overview
2-deoxy-2-fluorosalacinol
-
synthesis, overview
5-(1,4-dideoxy-1,4-episulfoniumylidene-D-arabinitol)-5-deoxy-D-ribonate inner salt
-
-
5-(1,4-dideoxy-1,4-episulfoniumylidene-L-arabinitol)-5-deoxy-D-ribonate inner salt
-
-
acarviosine
the inhibitor occupies the active-site pocket with the cyclohexitol moiety of acarviosine populating the -1 subsite
acarviostatin 103
-
component isolated from Streptomyces sp. strain PW638, also inhibitory to alpha-amylase, EC 3.2.1.1
amylase inhibitor from Streptomyces sp.
Endomycopsis fibuligera
-
-
-
BaCl2
-
5 mM, 17.4% inhibition
beta-D-glucose
-
slight inhibition up to 1 M concentration
beta-mercaptoethanol
-
5 mM, 89% inhibition
beta-O-methylacarviosinide
-
-
CaCl2
-
5 mM, 15.3% inhibition
caffeic acid
noncompetitive inhibition
cellobiose
-
5 mM, slight inhibition of starch hydrolysis
chlorogenic acid
noncompetitive inhibition
curcumin
-
is inhibitory at higher concentrations
D-galactose
-
22% inhibition, recombinant enzyme
D-glucono-1,5-lactone
-
non-competitive
D-glucosamine
-
68% inhibition, recombinant enzyme
D-xylose
-
64% inhibition, recombinant enzyme
diethyl dicarbonate
-
48% inhibition at 4 mM, 76% at 10 mM
dithiothreitol
-
5 mM, 79% inhibition
DTNB
-
42% inhibition at 10 mM, no inhibition at 1 mM
DTT
-
slight inhibition of isozyme GA-II at 1 mM, no inhibition of isozyme GA-I
epigallocatechin gallate
EGCG, noncompetitive inhibition
fructose
-
5 mM, slight inhibition of starch hydrolysis
gallic acid
noncompetitive inhibition
gentiobiose
-
20 mM, uncompetitive inhibition with starch as substrate
iodoacetamide
-
78% inhibition at 10 mM, 40% inhibition at 1 mM
KMnO4
-
1 mM, 40-43% inhibition
miglitol
-
a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain
myricetin
potent inhibitor with high binding affinity for both N- and C-terminals of the enzyme. Molecular dynamics reveal that myricetin interacts in its stretched conformation through water-mediated interactions with the C-terminus and by normal hydrogen bonding with the N-terminus. Residue W1369 of the extended 21 amino acid residue helical loop of C-terminal plays a major role in myricetin binding
N-(7-oxadecyl)-1-deoxynojirimycin
-
-
N-bromosuccimide
-
40% inhibition at 10 mM, 54% at 1 mM
N-butyl-deoxynojirimycin
-
-
N-decyl-deoxynojirimycin
-
-
N-methyl-deoxynojirimycin
-
-
NiCl2
-
5 mM, 17% inhibition
p-hydroxymercuribenzoate
-
-
Periodate
-
27% inhibition at 5 mM, 30% at 10 mM, 35% at 15 mM. 34% Glycosyl content of the enzyme is lost at 2.1 mM of periodate
phenyl alpha-D-glucoside
-
-
Phenylmethanesulfonylfluoride
-
-
phenylmethyl sulfonyl fluoride
-
53% inhibition at 5 mM
Propylene glycol
-
2%, 47% inhibition
pyridoxal 5'-phosphate
-
slight inhibition of isozyme GA-II at 1 mM, no inhibition of isozyme GA-I
Rose bengal
-
48% inhibition at 0.25 mg/ml
Schardinger dextrin
-
mixed inhibition with starch
sodiumdodecylsulfate
-
3 mM, complete inhibition
sorbitol
-
5 mM, slight inhibition of starch hydrolysis
sucrose
-
7.3 mM, 13.3% inhibition
tosylphenylalanylchloromethyl ketone
-
10% inhibition at 1 mM, 20% at 10 mM
Triton-X100
-
inhibits enzyme activity for 25% and 26% at concentrations of 1 mM and 2.5 mM, respectively, complete inhibition at 5 mM
Tween 20
-
2%, 27% inhibition
Tween 40
-
2%, 42% inhibition
Tween 80
-
2%, 25% inhibition
xylose
-
5 mM, slight inhibition of starch hydrolysis
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
Cephalosporium eichhorniae
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
Endomycopsis fibuligera
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
Schwanniomyces castellii
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
Thermochaetoides thermophila
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,2,7-trihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
Cephalosporium eichhorniae
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
Endomycopsis fibuligera
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
Schwanniomyces castellii
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
Thermochaetoides thermophila
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
-
-
1-deoxynojirimycin
-
-
1-deoxynojirimycin
Cephalosporium eichhorniae
-
-
1-deoxynojirimycin
Endomycopsis fibuligera
-
-
1-deoxynojirimycin
Schwanniomyces castellii
-
-
1-deoxynojirimycin
Thermochaetoides thermophila
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
Cephalosporium eichhorniae
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
Endomycopsis fibuligera
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
Schwanniomyces castellii
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
Thermochaetoides thermophila
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
-
2-epilentiginosine
-
-
2-epilentiginosine
Cephalosporium eichhorniae
-
-
2-epilentiginosine
Endomycopsis fibuligera
-
-
2-epilentiginosine
Schwanniomyces castellii
-
-
2-epilentiginosine
Thermochaetoides thermophila
-
-
2-mercaptoethanol
-
1 mM, complete loss of activity
2-mercaptoethanol
-
40% residual activity; no residual activity
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
4-chloromercuribenzoate
-
slight inhibition of isozyme GA-II at 1 mM, no inhibition of isozyme GA-I
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
complete inhibition at 10 mM, 72% inhibition at 1 mM
4-chloromercuribenzoate
Cephalosporium eichhorniae
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
Endomycopsis fibuligera
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
Schwanniomyces castellii
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
Thermochaetoides thermophila
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
4-chloromercuribenzoate
-
-
acarbose
binding structure, overview. Found in the active sites of both independent monomers. In both monomers an acarbose molecule is fitted and refined, assuming full occupancy
acarbose
-
84% inhibition at 0.004 mg/ml, 66% at 0.002 mg/ml
acarbose
-
0.1 mM, 93.2% loss of activity
acarbose
-
a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain
acarbose
bound to the active site primarily through side-chain interactions with its acarvosine unit, almost no interactions with its glycone rings, binding structure, overview
acarbose
-
inhibitory effect is 2 orders of magnitude higher for ntMGAM than for native MGAM
acarbose
-
25 ng/ml, 50% inhibition
acarbose
strong inhibition
Ag+
-
-
Ag+
-
21% inhibition of enzyme activity
Ag+
Cephalosporium eichhorniae
-
-
Ag+
Endomycopsis fibuligera
-
-
Ag+
-
38% inhibition of isozyme GA-I, 14% inhibition of isozyme GA-II at 1 mM
Ag+
-
1 mM AgNO3, 76-86% inhibition
Ag+
Schwanniomyces castellii
-
-
Ag+
Thermochaetoides thermophila
-
complete inhibition at 1 mM
Ag+
Thermochaetoides thermophila
-
-
Ag+
-
complete inhibition at 1 mM
Al3+
-
-
Al3+
-
33% inhibition at 1 mM, 67% at 10 mM
Al3+
-
5 mM, about 30% residual activity
Al3+
Cephalosporium eichhorniae
-
-
Al3+
Endomycopsis fibuligera
-
-
Al3+
-
20% inhibition of isozyme GA-II at 1 mM
Al3+
Schwanniomyces castellii
-
-
Al3+
Thermochaetoides thermophila
-
-
alpha-cyclodextrin
-
-
alpha-cyclodextrin
Cephalosporium eichhorniae
-
-
alpha-cyclodextrin
Endomycopsis fibuligera
-
-
alpha-cyclodextrin
Schwanniomyces castellii
-
-
alpha-cyclodextrin
Thermochaetoides thermophila
-
-
alpha-cyclodextrins
-
-
-
alpha-cyclodextrins
-
10 mM, 3% inhibition
-
amino alcohols
-
-
-
amino alcohols
Cephalosporium eichhorniae
-
-
-
amino alcohols
Endomycopsis fibuligera
-
-
-
amino alcohols
Schwanniomyces castellii
-
-
-
amino alcohols
Thermochaetoides thermophila
-
-
-
Ba2+
-
1 mM, 56% inhibition
Ba2+
-
5 mM, 90% residual activity
Ba2+
18% activation at 1 mM, 25% inhibition at 5 mM
beta-cyclodextrin
-
-
beta-cyclodextrin
Cephalosporium eichhorniae
-
-
beta-cyclodextrin
Endomycopsis fibuligera
-
-
beta-cyclodextrin
Schwanniomyces castellii
-
-
beta-cyclodextrin
Thermochaetoides thermophila
-
-
beta-cyclodextrins
-
-
-
beta-cyclodextrins
-
10 mM, 48% inhibition
-
beta-cyclodextrins
-
above 5 mM, slight inhibition
-
blintol
-
-
blintol
-
a selenium analogue of salacinol, is very effective in controlling blood glucose levels in rats after a carbohydrate meal, thus providing a lead candidate for the treatment of type 2 diabetes, synthesis, overview
Ca2+
-
-
Ca2+
Cephalosporium eichhorniae
-
-
Ca2+
Endomycopsis fibuligera
-
-
Ca2+
-
1 mM, 15-16% inhibition
Ca2+
-
5 mM, 78% residual activity
Ca2+
Schwanniomyces castellii
-
-
Ca2+
Thermochaetoides thermophila
-
-
castanospermine
-
-
castanospermine
Cephalosporium eichhorniae
-
-
castanospermine
Endomycopsis fibuligera
-
-
castanospermine
Schwanniomyces castellii
-
-
castanospermine
Thermochaetoides thermophila
-
-
Cd2+
-
-
Cd2+
Cephalosporium eichhorniae
-
-
Cd2+
Endomycopsis fibuligera
-
-
Cd2+
-
complete inhibition
Cd2+
-
1 mM, 17-18% inhibition
Cd2+
Schwanniomyces castellii
-
-
Cd2+
Thermochaetoides thermophila
-
-
Co2+
-
26% inhibition at 1 mM
Co2+
complete inhibition at 1-5 mM
Cr3+
62% inhibition at 1 mM, complete inhibition at 5 mM
Cr3+
-
complete inhibition at 1 mM
Cu2+
-
-
Cu2+
-
6% inhibition at 1 mM, 44% at 10 mM
Cu2+
activates at above 1 mM, inhibits at above 5 mM
Cu2+
-
complete inhibition
Cu2+
-
85% inhibition at 1 mM
Cu2+
Cephalosporium eichhorniae
-
-
Cu2+
22% inhibition at 1 mM, complete inhibition at 5 mM
Cu2+
Endomycopsis fibuligera
-
-
Cu2+
-
53% inhibition at 10 mM
Cu2+
-
10 mM, 71% residual activity with substrate starch, 31% with substrate maltose
Cu2+
-
5 mM, 48% residual activity
Cu2+
-
inhibits maltase activity
Cu2+
Schwanniomyces castellii
-
-
Cu2+
Thermochaetoides thermophila
-
12% inhibition at 1 mM
Cu2+
Thermochaetoides thermophila
-
-
Cu2+
-
complete inhibition at 1 mM
Cu2+
14% inhibition at 5 mM
D-glucose
-
44% inhibition, recombinant enzyme
D-glucose
-
strong product inhibition
EDTA
-
1 mM, 98% inhibition
EDTA
-
51% inhibition at 2 mM
EDTA
-
slight inhibition of isozyme GA-II at 1 mM, no inhibition of isozyme GA-I
EDTA
-
10% inhibition at 1 mM, 30% at 10 mM
EDTA
Cephalosporium eichhorniae
-
-
EDTA
22% inhibition at 10 mM
EDTA
Endomycopsis fibuligera
-
-
EDTA
-
10 mM, 16% inhibition
EDTA
Schwanniomyces castellii
-
-
EDTA
Thermochaetoides thermophila
-
-
EDTA
-
5 mM, 78% inhibition
Fe2+
-
5% inhibition of enzyme activity
Fe2+
activates at 1-5 mM, inhibits at 10 mM
Fe2+
27% inhibition at 1 mM, complete inhibition at 5 mM
Fe2+
-
29% inhibition at 10 mM
Fe2+
-
16% inhibition of isozyme GA-II at 1 mM
Fe2+
Thermochaetoides thermophila
-
80% inhibition at 1 mM
Fe2+
48% inhibition at 5 mM
Fe3+
-
1 mM, 34% inhibition
Fe3+
-
5 mM, about 40% residual activity
Fe3+
-
5 mM, 83% residual activity
Fe3+
activates at 1-5 mM, inhibits at 10 mM
Fe3+
Cephalosporium eichhorniae
-
-
Fe3+
62% inhibition at 1 mM, complete inhibition at 5 mM
Fe3+
Endomycopsis fibuligera
-
-
Fe3+
-
complete inhibition
Fe3+
Schwanniomyces castellii
-
-
Fe3+
Thermochaetoides thermophila
-
-
gamma-cyclodextrin
-
-
gamma-cyclodextrin
Cephalosporium eichhorniae
-
-
gamma-cyclodextrin
Endomycopsis fibuligera
-
-
gamma-cyclodextrin
Schwanniomyces castellii
-
-
gamma-cyclodextrin
Thermochaetoides thermophila
-
-
Guanidine-HCl
-
-
Guanidine-HCl
Cephalosporium eichhorniae
-
-
Guanidine-HCl
Endomycopsis fibuligera
-
-
Guanidine-HCl
Schwanniomyces castellii
-
-
Guanidine-HCl
Thermochaetoides thermophila
-
-
Hg2+
-
1 mM, 70% inhibition
Hg2+
-
46% inhibition at 0.002 mM
Hg2+
-
32% inhibition at 1 mM, 69% at 10 mM
Hg2+
-
10 mM, strong inhibition
Hg2+
-
5 mM, about 30% residual activity
Hg2+
-
1 mM, 48% inhibition, glucoamylase M2
Hg2+
-
1 mM, 49% inhibition, glucoamylase M1
Hg2+
-
complete inhibition
Hg2+
-
89% inhibition at 1 mM
Hg2+
Cephalosporium eichhorniae
-
-
Hg2+
Endomycopsis fibuligera
-
-
Hg2+
endophytic fungus EF6
-
-
Hg2+
-
complete inhibition
Hg2+
-
34% inhibition of isozyme GA-II, 49% inhibition of isozyme GA-I at 1 mM
Hg2+
-
10 mM, 10% residual activity
Hg2+
-
5 mM, 7% residual activity; 5 mM, no residual activity
Hg2+
-
potent inhibitor for glucoamylase I and II
Hg2+
-
5 mM, 70% inhibition
Hg2+
-
1 mM, 64-70% inhibition
Hg2+
Schwanniomyces castellii
-
-
Hg2+
Thermochaetoides thermophila
-
complete inhibition at 1 mM
Hg2+
Thermochaetoides thermophila
-
-
Hg2+
-
5 mM, 53% inhibition
Hg2+
52% inhibition at 5 mM
iodoacetate
-
-
iodoacetate
Cephalosporium eichhorniae
-
-
iodoacetate
Endomycopsis fibuligera
-
-
iodoacetate
Schwanniomyces castellii
-
-
iodoacetate
Thermochaetoides thermophila
-
-
K+
-
9% inhibition at 10 mM
K+
-
15% inhibition of isozyme GA-II at 1 mM
kotalanol
-
-
kotalanol
-
a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain
kotalanol
-
natural inhibitor isolated from the roots and stems of the plant Salacia reticulata
kotalanol
-
isolated from the roots and stems of the plant Salacia reticulata, contains an intriguing inner-salt sulfonium-sulfate structure, inhibition of glucosidases by salacinol and kotalanol is due to their ability to mimic both the shape and charge of the oxacarbenium-ion-like transition state involved in the enzymatic reactions
lentiginosine
-
-
lentiginosine
Cephalosporium eichhorniae
-
-
lentiginosine
Endomycopsis fibuligera
-
-
lentiginosine
Schwanniomyces castellii
-
-
lentiginosine
Thermochaetoides thermophila
-
-
maltitol
-
-
maltitol
-
20 mM, noncompetitive inhibition with starch as substrate
maltitol
Cephalosporium eichhorniae
-
-
maltitol
Endomycopsis fibuligera
-
-
maltitol
Schwanniomyces castellii
-
-
maltitol
Thermochaetoides thermophila
-
-
maltose
-
maltotetraose
-
maltotriose
pronounced inhibition above 2 mM
maltotriose
-
substrate inhibition of AmyC
methyl alpha-D-glucoside
-
competitive with maltose and non-competitive with starch
methyl alpha-D-glucoside
-
-
methyl alpha-D-glucoside
-
10 mM, 30% inhibition
Mg2+
-
-
Mg2+
-
5 mM, 85% residual activity
Mn2+
-
-
Mn2+
-
activates 51% and 65% at 5 mM and 10 mM, respectively, inhibitory at above 15 mM
Mn2+
-
1 mM, 12% inhibition, glucoamylase M2
Mn2+
Cephalosporium eichhorniae
-
-
Mn2+
34.5% inhibition at 1-5 mM
Mn2+
Endomycopsis fibuligera
-
-
Mn2+
-
22% inhibition of isozyme GA-II at 1 mM
Mn2+
-
5 mM, 59% residual activity
Mn2+
-
1 mM, 20-29% inhibition
Mn2+
Schwanniomyces castellii
-
-
Mn2+
Thermochaetoides thermophila
-
11% inhibition at 1 mM
Mn2+
Thermochaetoides thermophila
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
78% inhibition at 0.01 mM
N-bromosuccinimide
-
complete inhibition at 1 mM of isozyme GA-I and isozyme GA-II
N-bromosuccinimide
Cephalosporium eichhorniae
-
-
N-bromosuccinimide
Endomycopsis fibuligera
-
-
N-bromosuccinimide
Schwanniomyces castellii
-
-
N-bromosuccinimide
Thermochaetoides thermophila
-
-
N-bromosuccinimide
-
5 mM, 83% inhibition
N-bromosuccinimide
-
almost complete inhibition at 1 mM
N-ethylmaleimide
-
-
N-ethylmaleimide
-
5 mM, complete inhibition
Na+
at above 5 mM
Ni2+
-
1 mM, 63% inhibition
Ni2+
Cephalosporium eichhorniae
-
-
Ni2+
44% inhibition at 1 mM, 70% at 5 mM
Ni2+
Endomycopsis fibuligera
-
-
Ni2+
Schwanniomyces castellii
-
-
Ni2+
Thermochaetoides thermophila
-
-
Ni2+
-
5 mM, 74% inhibition
Pb2+
-
-
Pb2+
activates at above 1 mM, inhibits at above 5 mM
Pb2+
-
5 mM, 77% residual activity
Pb2+
Cephalosporium eichhorniae
-
-
Pb2+
Endomycopsis fibuligera
-
-
Pb2+
-
5 mM Pb(CH3COO)2, 25% inhibition
Pb2+
-
1 mM, 20-29% loss of activity
Pb2+
Schwanniomyces castellii
-
-
Pb2+
Thermochaetoides thermophila
-
-
Pb2+
30% inhibition at 5 mM
PMSF
-
slight inhibition
PMSF
-
53% inhibition at 10 mM
salacinol
-
-
salacinol
-
a naturally occurring glycosidase inhibitor isolated from roots and stems of a Sri Lankan plant, Salacia reticulata, the OH group on C-2 of salacinol is critical as a hydrogen-bond donor with functional groups in the active site of the enzyme
salacinol
-
isolated from Salacia reticulata, a plant native to Sri Lanka and India that has been used in the Ayurvedic system of medicine for the treatment of diabetes, inhibition of the isolated recombinant N-terminal catalytic domain
salacinol
-
natural inhibitor isolated from the roots and stems of the plant Salacia reticulata
salacinol
-
isolated from the roots and stems of the plant Salacia reticulata, contains an intriguing inner-salt sulfonium-sulfate structure, inhibition of glucosidases by salacinol is due to their ability to mimic both the shape and charge of the oxacarbenium-ion-like transition state involved in the enzymatic reactions, the compound is capable of attenuating the spike in blood glucose levels
SDS
-
41% inhibition at 1 mM, 86% at 10 mM
SDS
30% inhibition at 5 mg/ml
SDS
-
60% inhibition at 1 mM, 80% at 10 mM
SDS
-
complete inhibition at 1 mM
sodium dodecylsulfate
-
3 mM, complete inhibition
sodium dodecylsulfate
-
2%, 76% inhibition
sodium dodecylsulfate
-
3 mM, complete inhibition
Sr2+
-
1 mM, 68% inhibition
trestatin
-
-
trestatin
Cephalosporium eichhorniae
-
-
trestatin
Endomycopsis fibuligera
-
-
trestatin
Schwanniomyces castellii
-
-
trestatin
Thermochaetoides thermophila
-
-
Tris
-
-
Tris
Cephalosporium eichhorniae
-
-
Tris
Endomycopsis fibuligera
-
-
Tris
Schwanniomyces castellii
-
-
Tris
Thermochaetoides thermophila
-
-
Triton X-100
20% inhibition at 20 mg/ml
Triton X-100
-
2%, 60% inhibition
Urea
-
-
Urea
-
17% inhibition at 1 mM, 20% at 10 mM
Urea
Cephalosporium eichhorniae
-
-
Urea
Endomycopsis fibuligera
-
-
Urea
-
5 M, complete inhibition
Urea
-
5 M, complete inhibition
Urea
Schwanniomyces castellii
-
-
Urea
Thermochaetoides thermophila
-
-
Urea
-
5 M, complete inhibition
Zn2+
-
-
Zn2+
activates at above 1 mM, inhibits at above 5 mM
Zn2+
-
78% inhibition at 1 mM
Zn2+
Cephalosporium eichhorniae
-
-
Zn2+
28% inhibition at 1 mM, 43% at 5 mM
Zn2+
Endomycopsis fibuligera
-
-
Zn2+
Schwanniomyces castellii
-
-
Zn2+
Thermochaetoides thermophila
-
25% inhibition at 1 mM
Zn2+
Thermochaetoides thermophila
-
-
Zn2+
-
5 mM, complete inhibition
Zn2+
27% inhibition at 5 mM
additional information
-
remarkable insensitivity of the enzyme to end product inhibition
-
additional information
-
the deglycosylated enzyme is more sensitive to proteolytic degradation by subtilisin than the native enzyme
-
additional information
-
glucose, cycloheximide, and actinomycin D nearly completely suppresses enzyme expression, repression mechanism, overview
-
additional information
-
product inhibition, kinetics
-
additional information
-
binding of a short heterobidentate inhibitor simultaneously directed toward the catalytic and starch binding domains causes dimerization of glucoamylase and not, an intramolecular conformational rearrangement mediated by linker flexibility
-
additional information
-
not inhibitory at 5 mM: Ag2+, Ca2+, Zn2+, Mg2+ and Cd2+ and EDTA
-
additional information
-
tannins isolated from extracts of pomegranate, cranberry, grape, and cocoa inhibit the activity of glucoamylase and alpha-amylase in vitro. In general, larger and more complex tannins, such as those in pomegranate and cranberry, more effectively inhibit the enzymes than less polymerized cocoa tannins
-
additional information
EDTA and Na2EDTA do not affect the enzyme activity
-
additional information
-
EDTA and Na2EDTA do not affect the enzyme activity
-
additional information
-
no inhibition by iodoacetic acid and PMSF
-
additional information
-
no inhibition by PMSF
-
additional information
enzyme activity is significantly inhibited when the substrate concentration exceeds approximately 10fold the Km value
-
additional information
-
the purified enzyme is sensitive to proteolytic degradation by alpha-chymotrypsin
-
additional information
structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity
-
additional information
-
structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity
-
additional information
-
structure-activity relationship and stereochemistry of inhibitors, synthesis of chain-extended sulfonium and selenonium salts of 1,4-anhydro-4-thio- or 4-seleno-D-arabinitol, analogues of the naturally occurring glycosidase inhibitor salacinol, by nucleophilic attack at the least hindered carbon atom of 4,6-O-benzylidene-2,5-di-O-p-methoxybenzyl-D-mannitol-1,3-cyclic sulfate by 2,3,5-tri-O-p-methoxybenzyl-1,4-anhydro-4-thio-or 4-seleno-D-arabinitol, giving the sulfonium and selenonium sulfates, respectively, and subsequent deprotection with trifluoroacetic acid, the extended polyhydroxylated aliphatic side chain is incorporated while maintaining the stereochemistry of C-2' and C-3' of salacinol or blintol, overview
-
additional information
-
ghavamiol, a nitrogen analogue of salacinol, is inactive as inhibitor
-
additional information
-
iodoacetamide and urea are poor inhibitors
-
additional information
kinetics and mechanism of inhibition of the recombinant glucoamylase subunit Ct-MGAM and sucrase subunit Ct-SI, overview
-
additional information
-
kinetics and mechanism of inhibition of the recombinant glucoamylase subunit Ct-MGAM and sucrase subunit Ct-SI, overview
-
additional information
-
no inhibition by neuraminidase inhibitor and EDTA at 1-10 mM
-
additional information
-
AmyC, but not AmyD, exhibits substrate inhibition, the Ki for substrate inhibition decreases with increasing length of the oligosaccharides. AmyC accumulates an enzyme maltose-maltotriose dead-end complex in the steady state, kinetics and modelling, overview
-
additional information
Thermochaetoides thermophila
-
poor inhibition by Ba2+ at 1 mM
-
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0.125
4-methylumbelliferyl-alpha-D-glucoside
-
-
3.4
4-nitrophenyl alpha-D-glucoside
-
wild-type enzyme
70
alpha-D-glucopyranosyl fluoride
-
wild-type enzyme
0.063 - 0.065
amylose DP 18
-
0.38
amylotriose
-
pH 6.5, 40°C, recombinant enzyme
17
isomaltoheptaose
-
recombinant glucoamylase
18
isomaltohexaose
-
recombinant glucoamylase
16
isomaltopentaose
-
recombinant glucoamylase
15
isomaltotetraose
-
recombinant glucoamylase
18
isomaltotriose
-
recombinant glucoamylase
150
kojibiose
-
wild-type enzyme
0.025 - 7.59
maltoheptaose
0.045 - 7.43
maltohexaose
0.03 - 6.66
maltopentaose
0.032 - 9.9
maltotetraose
2.75
p-nitrophenyl alpha-D-glucoside
-
-
5.6
p-nitrophenyl-alpha-D-glucoside
-
glucoamylase M2
0.31
Phenyl alpha-maltoside
-
-
10
Phenyl-alpha-maltoside
-
glucoamylase M2
18
pullulan
-
enzyme form GIII
0.4
short-chain amylose
-
-
-
0.0011 - 5.75
soluble starch
-
additional information
maltose
0.0002
amylopectin
-
glucoamylase G2 or G3
0.0003
amylopectin
-
glucoamylase G1
0.16
amylopectin
-
glucoamylase G5
0.17
amylopectin
-
glucoamylase G4
0.3
amylopectin
-
enzyme form GIII
1.65
amylopectin
-
glucoamylase M2
2
amylopectin
-
pH 5.0, 55°C
4.2
amylopectin
-
pH 5.0, 37°C, isozyme GA-II
6.1
amylopectin
-
enzyme form GI
7.4
amylopectin
-
enzyme form GII
17.1
amylopectin
-
pH 5.0, 37°C, isozyme GA-I
0.0021
amylose
-
DP = 18, glucoamylase G1, G2 or G3
0.146
amylose
-
glucoamylase M2
2.3
amylose
-
pH 5.0, 37°C, isozyme GA-I
2.4
amylose
-
pH 5.0, 37°C, isozyme GA-II
2.5
amylose
-
pH 5.0, 55°C
0.063
amylose DP 18
-
glucoamylase G4
-
0.065
amylose DP 18
-
glucoamylase G5
-
0.17
Dextrin
-
free enzyme
0.73
Dextrin
-
glucoamylase M2
0.83
Dextrin
-
immobilized enzyme
0.0005
glycogen
-
glucoamylase G2
0.0006
glycogen
-
glucoamylase G3
0.0007
glycogen
-
glucoamylase G1
0.62
glycogen
-
glucoamylase G5
0.63
glycogen
-
glucoamylase G4
0.8
glycogen
-
glycogen from rabbit liver, enzyme form GIII
1.25
glycogen
-
glucoamylase M2
1.7
glycogen
-
pH 5.0, 55°C
1.8
glycogen
-
glycogen from oyster, enzyme form GIII
6.2
glycogen
-
pH 5.0, 37°C, isozyme GA-II
210
glycogen
-
glycogen from oyster, enzyme form GI
240
glycogen
-
glycogen from rabbit liver, enzyme form GI
250
glycogen
-
glycogen from oyster, enzyme form GII
300
glycogen
-
glycogen from rabbit liver, enzyme form GII
820
glycogen
-
glycogen from rabbit liver
1100
glycogen
-
glycogen from oyster
2.41
isomaltose
-
pH 5.0, 75°C
12.3
isomaltose
-
mutant enzyme S411C
17.4
isomaltose
-
mutant enzyme S184H
20
isomaltose
-
glucoamylase G1
20.1
isomaltose
-
glucoamylase G2
20.4
isomaltose
-
glucoamylase G3
21.7
isomaltose
-
glucoamylase G4
23
isomaltose
-
glucoamylase G5
23.5
isomaltose
-
wild-type enzyme
24.6
isomaltose
-
wild-type enzyme
26.2
isomaltose
-
wild-type enzyme
27.9
isomaltose
-
mutant enzyme S411A
36.4
isomaltose
-
glucoamylase M2
38
isomaltose
-
wild-type enzyme
38
isomaltose
-
recombinant glucoamylase
39
isomaltose
-
mutant enzyme Gly183Lys
40
isomaltose
-
enzyme form GIII
42
isomaltose
-
mutant enzyme S119Y
47
isomaltose
-
enzyme form GI or GII
53.6
isomaltose
45°C, pH 4.5
2.74
maltodextrin
-
pH 4.5, 60°C, native enzyme
3.64
maltodextrin
-
pH 4.5, 60°C, glycated enzyme
0.025
maltoheptaose
-
glucoamylase G2
0.026
maltoheptaose
-
glucoamylase G1
0.027
maltoheptaose
-
glucoamylase G3
0.04
maltoheptaose
pH 5.0, 40°C
0.058
maltoheptaose
-
glucoamylase G5
0.059
maltoheptaose
-
glucoamylase G4
0.07
maltoheptaose
-
mutant enzyme S411C
0.083
maltoheptaose
-
wild-type enzyme
0.1
maltoheptaose
-
enzyme form GII
0.104
maltoheptaose
-
mutant enzyme S411A
0.11
maltoheptaose
-
enzyme form GI
0.12
maltoheptaose
-
wild-type enzyme
0.12
maltoheptaose
-
recombinant glucoamylase
0.132
maltoheptaose
-
mutant enzyme S411G
0.14
maltoheptaose
-
wild-type enzyme or mutant enzymes Gly183Lys or S184H
0.148
maltoheptaose
-
mutant enzyme S411D
0.15
maltoheptaose
-
immobilized enzyme
0.15
maltoheptaose
-
enzyme form GIII
0.158
maltoheptaose
-
mutant enzyme S119Y
0.61
maltoheptaose
45°C, pH 4.5
2.21
maltoheptaose
-
pH 5.0, 75°C
7.59
maltoheptaose
-
pH 6.5, 40°C, recombinant enzyme
0.045
maltohexaose
-
glucoamylase G2
0.048
maltohexaose
-
glucoamylase G1
0.05
maltohexaose
-
glucoamylase G3
0.05
maltohexaose
pH 5.0, 40°C
0.059
maltohexaose
-
glucoamylase G4
0.06
maltohexaose
-
glucoamylase G5
0.11
maltohexaose
-
wild-type enzyme
0.11
maltohexaose
-
enzyme form GII
0.11
maltohexaose
-
recombinant glucoamylase
0.12
maltohexaose
-
enzyme form GI
0.16
maltohexaose
-
enzyme form GIII
0.206
maltohexaose
-
mutant enzyme S119Y
0.287
maltohexaose
-
recombinant AmyC, pH 5.5, 40°C
0.62
maltohexaose
-
recombinant AmyD, pH 5.5, 40°C
1.88
maltohexaose
-
pH 5.0, 75°C
7.43
maltohexaose
-
pH 6.5, 40°C, recombinant enzyme
0.03
maltopentaose
pH 5.0, 40°C
0.05
maltopentaose
-
IP-MGAM, immunoprecipitated maltase-glucoamylase
0.066
maltopentaose
-
glucoamylase G3
0.067
maltopentaose
-
glucoamylase G4 or G5
0.07
maltopentaose
-
glucoamylase G1
0.071
maltopentaose
-
glucoamylase G2
0.1
maltopentaose
-
wild-type enzyme
0.1
maltopentaose
-
recombinant glucoamylase
0.13
maltopentaose
-
free enzyme
0.14
maltopentaose
-
enzyme form GII
0.16
maltopentaose
-
enzyme form GI
0.17
maltopentaose
-
enzyme form GIII
0.17
maltopentaose
-
mutant enzyme S119Y
0.224
maltopentaose
-
recombinant AmyC, pH 5.5, 40°C
0.93
maltopentaose
-
recombinant AmyD, pH 5.5, 40°C
1.63
maltopentaose
-
pH 5.0, 75°C
3.94
maltopentaose
-
pH 6.5, 40°C, recombinant enzyme
6.66
maltopentaose
-
ntMGAM, N-terminal subunit of MGAM, Vmax: 6.97 U/mg
0.101
maltose
-
pH 6.5, 40°C, recombinant enzyme
0.18
maltose
-
8°C, pH 4.5, wild-type G1
0.28
maltose
-
8°C, pH 4.5, wild-type G2
0.53
maltose
-
mutant enzyme S411C
0.53
maltose
-
recombinant AmyC, pH 5.5, 40°C
0.58
maltose
-
IP-MGAM, immunoprecipitated maltase-glucoamylase
0.67
maltose
-
glucoamylase G4 and G5
0.68
maltose
-
glucoamylase G1 and G2
0.69
maltose
-
glucoamylase G3
0.72
maltose
-
45°C, pH 4.4
0.76
maltose
-
pH 4.5, 35°C, recombinant mutant T62A
0.78
maltose
50°C, pH 4.5
0.78
maltose
-
pH 4.5, 35°C, recombinant mutant T290A
0.82
maltose
-
pH 4.5, 35°C, recombinant mutant H391Y
0.83
maltose
-
pH 4.5, 35°C, recombinant wild-type enzyme
0.87
maltose
pH 5.0, 40°C
0.88
maltose
-
pH 4.5, 35°C, recombinant mutant S30P/T62A/H391Y
0.89
maltose
-
pH 4.5, 35°C, recombinant mutant S119P
0.9
maltose
-
mutant enzyme S184H
1
maltose
-
pH 4.5, 35°C, recombinant mutant D20C/A27C/S30P/G137A
1.01
maltose
-
wild-type enzyme
1.08
maltose
-
mutant enzyme G183K
1.1
maltose
-
mutant enzyme S119Y
1.16
maltose
-
pH 4.5, 35°C, recombinant mutant S30P/T290A/H391Y
1.19
maltose
-
pH 4.5, 35°C, recombinant mutant S30P/H391Y
1.21
maltose
-
recombinant enzyme expressed in Aspergillus niger
1.26
maltose
-
mutant enzyme S411A
1.35
maltose
-
pH 4.5, 35°C, recombinant mutant S30P/T290A
1.4
maltose
-
wild-type enzyme
1.59
maltose
-
mutant enzyme S411G
1.8
maltose
-
30°C, pH 4.2, glucoamylase immobilized on macroporous silica
1.82
maltose
-
recombinant enzyme expressed in Saccharomyces cerevisiae
1.9
maltose
-
enzyme form GI or GII
2
maltose
-
enzyme form GIII
2.97
maltose
-
recombinant enzyme expressed in Pichia pastoris
3
maltose
-
wild-type enzyme
3
maltose
-
glucoamylase M2
3
maltose
-
recombinant glucoamylase
3.5
maltose
-
pH 5.0, 70°C
3.5
maltose
-
values about 0.8 mg/ml for starch
3.58
maltose
-
mutant enzyme S411D
3.78
maltose
-
recombinant AmyD, pH 5.5, 40°C
4.9
maltose
pH 5.0, 50°C, recombinant enzyme
5.4
maltose
-
pH 4.5, 65°C, recombinant enzyme
6.2
maltose
-
free enzyme
7.71
maltose
-
ntMGAM, N-terminal subunit of MGAM, Vmax: 8.26 U/mg
9.19
maltose
-
pH 4.5, 60°C, glycated enzyme
12.49
maltose
-
pH 4.5, 60°C, native enzyme
13.4
maltose
-
pH 5.0, 75°C
27.4
maltose
-
immobilized enzyme
0.032
maltotetraose
-
8°C, pH 4.5, wild-type G1
0.05
maltotetraose
-
IP-MGAM, immunoprecipitated maltase-glucoamylase
0.058
maltotetraose
-
8°C, pH 4.5, wild-type G2
0.082
maltotetraose
-
glucoamylase G4
0.083
maltotetraose
-
glucoamylase G5
0.088
maltotetraose
-
glucoamylase G3
0.095
maltotetraose
-
glucoamylase G1 or G2
0.14
maltotetraose
pH 5.0, 40°C
0.18
maltotetraose
-
wild-type enzyme
0.18
maltotetraose
-
recombinant glucoamylase
0.21
maltotetraose
-
enzyme form GII
0.23
maltotetraose
-
enzyme form GI
0.25
maltotetraose
-
mutant enzyme S119Y
0.26
maltotetraose
-
enzyme form GIII
0.276
maltotetraose
-
recombinant AmyC, pH 5.5, 40°C
1.03
maltotetraose
-
pH 6.5, 40°C, recombinant enzyme
1.35
maltotetraose
-
pH 5.0, 75°C
1.51
maltotetraose
-
recombinant AmyD, pH 5.5, 40°C
3
maltotetraose
-
ntMGAM, N-terminal subunit of MGAM, Vmax: 7.65 U/mg
9.9
maltotetraose
pH 5.0, 50°C, recombinant enzyme
0.16
maltotriose
pH 5.0, 40°C
0.2
maltotriose
-
15°C, pH 4.2, glucoamylase immobilized on macroporous silica
0.21
maltotriose
-
glucoamylase G1, G2 or G3
0.22
maltotriose
-
IP-MGAM, immunoprecipitated maltase-glucoamylase
0.23
maltotriose
-
glucoamylase G4
0.24
maltotriose
-
glucoamylase G5
0.25
maltotriose
-
recombinant enzyme expressed in Saccharomyces cerevisiae
0.28
maltotriose
-
recombinant enzyme expressed in Aspergillus niger
0.29
maltotriose
-
wild-type enzyme
0.29
maltotriose
-
recombinant enzyme expressed in Pichia pastoris
0.29
maltotriose
-
recombinant glucoamylase
0.33
maltotriose
-
20°C, pH 4.0
0.33
maltotriose
AAE85601
pH 4.0, 20°C
0.39
maltotriose
-
mutant enzyme S119Y
0.487
maltotriose
-
recombinant AmyC, pH 5.5, 40°C
0.57
maltotriose
-
enzyme form GII
0.59
maltotriose
-
enzyme form GI
0.64
maltotriose
-
enzyme form GIII
0.89
maltotriose
-
30°C, pH 4.2, glucoamylase immobilized on macroporous silica
1.4
maltotriose
-
glucoamylase M2
1.88
maltotriose
-
recombinant AmyD, pH 5.5, 40°C
1.9
maltotriose
pH 5.0, 50°C, recombinant enzyme
1.93
maltotriose
-
pH 5.0, 75°C
4.6
maltotriose
-
ntMGAM, N-terminal subunit of MGAM, Vmax: 9.58 U/mg
22
nigerose
-
-
32
nigerose
-
wild-type enzyme
12
panose
-
-
13
panose
-
enzyme form GII
14
panose
-
enzyme form GI or GIII
15.4
panose
-
glucoamylase G1
15.8
panose
-
glucoamylase G2
16.7
panose
-
glucoamylase G4
16.9
panose
-
glucoamylase G5
17
panose
-
wild-type enzyme
17.2
panose
-
glucoamylase G3
0.0011
soluble starch
-
soluble
-
0.2
soluble starch
-
pH 5.0, 37°C, isozyme GA-II
-
0.26
soluble starch
-
pH 4.7, 55°C
-
1.9
soluble starch
-
pH 4.5, 40°C, purified native enzyme
-
3
soluble starch
-
pH 5.3, 40°C, recombinant enzyme
-
4
soluble starch
-
pH 5.0, 37°C, isozyme GA-I
-
5.75
soluble starch
-
pH 4.5, 60°C
-
0.0002
starch
-
soluble, glucoamylase G1 or G3
0.0003
starch
-
soluble, glucoamylase G2
0.017
starch
-
30°C, pH 4.2, glucoamylase immobilized on macroporous silica
0.031
starch
-
immobilized enzyme, pH 5.5, 90°C
0.045
starch
-
soluble, glucoamylase G4
0.048
starch
-
soluble, glucoamylase G5
0.05
starch
-
pH 3.5-5.5, 50°C
0.1
starch
-
free enzyme, pH 5.5, 90°C
0.12
starch
-
immobilized enzyme, pH 5.5, 70°C
0.16
starch
-
mutant enzyme, pH 5.0, 40°C
0.18
starch
-
free enzyme, pH 5.5, 70°C
0.238
starch
-
immobilized enzyme, pH 5.5, 50°C
0.25
starch
-
wild-type enzyme, pH 5.0, 40°C
0.333
starch
-
free enzyme, pH 5.5, 50°C
0.43
starch
-
pH 4.2, 60°C, immobilized enzyme
1.1
starch
-
pH 4.8, 37°C, deglycosylated enzyme
1.15
starch
-
pH 4.5, 55°C, multilamellar liposome-entrapped enzyme
1.2
starch
-
pH 4.8, 37°C, native enzyme
1.4
starch
-
pH 4.5, 40°C, ACG-7
1.55
starch
-
pH 4.5, 55°C, free soluble enzyme
1.6
starch
-
pH 4.5, 40°C, native enzyme
1.6
starch
-
pH 5.5, 40°C, native enzyme
1.64
starch
-
pH 4.5, 55°C, large unilamellar liposome-entrapped enzyme
1.7
starch
-
pH 4.5, 40°C, ACG-13
2
starch
-
pH 4.5, 40°C, ACG-1
2.3 - 2.9
starch
-
pH 5.5, 40°C, EDTA-coupled enzyme
3.57
starch
-
pH 4.0, 60°C, isozyme GA-I
3.8 - 4.1
starch
-
pH 5.0, 55°C
4.76
starch
-
pH 4.2, 60°C, free enzyme
6.25
starch
-
pH 4.0, 65°C, isozyme GA-II
additional information
maltose
-
3.9 mg/ml
additional information
maltose
-
Km value 0.029 mg/ml, pH 5.5, temperature not specified in the publication
additional information
maltose
-
Km value 1.5 mg/ml, pH 5.5, 60°C
additional information
maltose
-
Km value 3.9 mg/ml, pH 5.5, 65°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
0.56 g/l for amylopectin from potato
-
additional information
additional information
-
6.8 mg/ml for maltose, 1.9 mg/ml for soluble starch
-
additional information
additional information
-
0.76 g/l for glycogen from oyster
-
additional information
additional information
-
0.97 g/l for soluble starch of Zulkowsky type
-
additional information
additional information
-
0.92% for soluble starch, glucoamylase M2
-
additional information
additional information
-
101 g/l for dextran
-
additional information
additional information
-
Km-values for the wild type enzyme and the mutant enzymes V181T/N182Y/G183A, P307A/T310V/Y312M/N313G and V181T/N182Y/G183A/P307A/T310V/Y312M/N313G
-
additional information
additional information
-
0.48 mg/ml for starch with glucoamylase II and III. 0.5 mg/ml for starch with glucoamylase I
-
additional information
additional information
-
0.741 mg/ml, hydrolysis of amylopectin with glucoamylase I. 0.667 mg/ml, hydrolysis of amylopectin with glucoamylase II. 0.455 mg/ml. Hydrolysis of amylose with glucoamylase I. 0.286 mg/ml, hydrolysis of amylose with glucoamylase II. 1.11 mg/ml, hydrolysis of glycogen with glucoamylase I. 1.54 mg/ml, hydrolysis of glycogen with glucoamylase II
-
additional information
additional information
-
4 g/l for maltose
-
additional information
additional information
-
3.8 g/l for pullulan
-
additional information
additional information
-
6.57 mg/ml for glucoamylase I with starch as substrate, 4.52 mg/ml for glucoamylase II with starch as substrate. 0.15 mg/ml for glucoamylase II with alpha-cyclodextrin as substrate, 2.0 mg/ml for glucoamylase II with beta-cyclodextrin as substrate
-
additional information
additional information
-
0.37 g/l for glycogen from rat liver
-
additional information
additional information
-
1.2 g/l for soluble starch
-
additional information
additional information
-
0.025% for starch
-
additional information
additional information
-
0.333 mg/ml for maltose
-
additional information
additional information
-
Km-values for C320A/E400C and the cysteinesulfinic acid derivative of C320A/E400C
-
additional information
additional information
-
7.8 mg/ml for soluble starch
-
additional information
additional information
-
kinetics and thermodynamics
-
additional information
additional information
-
kinetics, recombinant enzyme
-
additional information
additional information
-
kinetics and thermodynamics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
detailed reaction kinetics
-
additional information
additional information
-
kinetics and thermodynamics, substrate specificity for fermentation
-
additional information
additional information
-
ligand binding kinetics, wild-type enzyme and mutants
-
additional information
additional information
-
modelling of potato starch saccharification by commercial Aspergillus niger enzyme, kinetics
-
additional information
additional information
-
biphasic kinetics for maltodextrin degradation
-
additional information
additional information
-
kinetic analysis of glucoamylase-catalyzed hydrolysis of starch granules from various botanical sources, overview, Ko increases as the starch granule crystaline structure becomes dense
-
additional information
additional information
-
kinetics and thermodynamics of native and EDTA-coupled enzyme, overview
-
additional information
additional information
-
kinetics and thermodynamics of polyacrylamide gel-immobilized purified enzyme
-
additional information
additional information
-
kinetics of native enzyme, and aniline-coupled glucoamylase-1/ACG-1, aniline-coupled glucoamylase-7/ACG-7, and 13 min aniline-coupled glucoamylase-13/ACG-13, overview
-
additional information
additional information
-
kinetics of starch hydrolysis by AMG modeled for two different systems, free enzyme in aqueous solution and entrapped enzyme within vesicles in aqueous suspension, overview, Michaelis-Menten kinetic model with product inhibition for intrinsic kinetics
-
additional information
additional information
-
Km-value: 4.34 g/l with corn maltodextrin as a substrate for the N-terminal subunit of MGAM, Vmax: 7.51 U/mg with corn maltodextrin as a substrate for the N-terminal subunit of MGAM. Km-value: 7.01 g/l with alpha-limit dextrin as a substrate for the N-terminal subunit of MGAM, Vmax: 11.0 U/mg with alpha-limit dextrin as a substrate for the N-terminal subunit of MGAM. Km-value: 0.06 g/l with corn maltodextrin as a substrate for the immunoprecipitated maltase-glucoamylase. Km-value: 0.49 g/l with alpha-limit dextrin as a substrate for immunoprecipitated maltase-glucoamylase, Vmax: 11.0 U/mg with alpha-limit dextrin as a substrate for the immunoprecipitated maltase-glucoamylase
-
additional information
additional information
-
steady-state and pre-steady-state kinetic measurements using maltooligosacchrides as substrates, analysis and modelling, overview
-
additional information
additional information
-
thermodynamics and kinetics of starch hydrolysis, overview
-
additional information
additional information
-
Michaelis-Menten and Lineweaver-Burk kinetics
-
additional information
additional information
-
4.5 g/l with soluble starch
-
additional information
additional information
-
kinetic values Km and Vmax with soluble starch are 2.84 mg/ml and 239.2 U/ml, respectively, Lineweaver-Burk kinetics
-
additional information
additional information
-
KM values for amylopectin, glycogen and starch are 0.056, 0.062 and 0.065 mg/ml, respectively
-
additional information
additional information
Michaelis-Menten kinetics, Km and Vmax of the glucoamylase are calculated as 15.02 g/l and 81.13 U/mg, pH 5.0, 45°C
-
additional information
additional information
-
Michaelis-Menten kinetics, Km and Vmax of the glucoamylase are calculated as 15.02 g/l and 81.13 U/mg, pH 5.0, 45°C
-
additional information
additional information
-
using raw cassava starch as substrate, the enzyme has a Km value of 0.72 mg/mL with Vmax of 0.01248 mmol/min/mg
-
additional information
starch
-
0.21 mg/ml
additional information
starch
-
1 mg/ml, 50°C, pH 4.0
additional information
starch
-
10 mg/ml, 55°C, pH 5.0
additional information
starch
-
2.4 mg/ml, 60°C
additional information
starch
-
5.1 mg/ml, 60°C, pH4.5
additional information
starch
-
0.32 mg/ml
additional information
starch
-
3.8-4.1 mg/ml
additional information
starch
-
value between 0.14 and 0.26 mg/ml
additional information
starch
-
value is 0.1 mg/ml
additional information
starch
-
value is 0.11 mg/ml
additional information
starch
-
value is 0.4 mg/ml
additional information
starch
-
value is 0.44 g/l
additional information
starch
-
value is 0.44 g/l
additional information
starch
-
value is 1.06 mg/ml
additional information
starch
-
value is 1.9 mg/ml
additional information
starch
Endomycopsis fibuligera
-
value is 20 mg/ml
additional information
starch
-
value is 5.75 mg/ml
additional information
starch
-
value is about 18 mg/ml
additional information
starch
-
value is between 0.21 and 0.28 mg/ml
additional information
starch
-
value is between 2.5 and 4.35 mg/ml
additional information
starch
-
Km value is 0.33 mg/ml, pH 5.0, 40°C
additional information
starch
Km value of wild-type is 34.5 mg/ml, pH 4.6, 70°C, of mutant T47A 61.1 mg/ml, mutant W48A 52.9 mg/ml
additional information
starch
-
Km value of wild-type is 34.5 mg/ml, pH 4.6, 70°C, of mutant T47A 61.1 mg/ml, mutant W48A 52.9 mg/ml
additional information
starch
-
Km value 0.094 mg/ml, pH 5.5, temperature not specified in the publication
additional information
starch
-
Km value 0.2 mg/ml, pH 5.5, 60°C
additional information
starch
-
Km value 0.21 mg/ml, pH 5.5, 65°C
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105360
-
x * 105360, recombinant N-terminal catalytic domain, MALDI-TOF mass spectrometry
116000
-
1 * 116000 + 1 * 212000, SDS-PAGE
128000
-
1 * 128000, glucoamylase II, SDS-PAGE
130000
-
about, recombinant enzyme, native PAGE
133000
-
x * 133000 + x * 90000, SDS-PAGE
141000
-
x * 141000 + x * 95000, SDS-PAGE
150000
-
2 * 150000, glucoamylase I, SDS-PAGE
16000 - 46000
-
gel filtration
186000
-
2 * 186000, SDS-PAGE
212000
-
1 * 116000 + 1 * 212000, SDS-PAGE
230000
-
glucoamylase I, gel filtration
250000
-
SDS-PAGE, assumed
292000
recombinant intracellular enzyme, native PAGE
33000
-
1 * 65000 + 1 * 33000, SDS-PAGE
440000
-
papain solubilized enzyme, gel filtration
47000
-
SDS-PAGE, assumed
48500
-
SDS-PAGE, assumed
51000
-
enzyme form GA-II, gel filtration
52000
-
enzyme form GA-I, gel filtration
53000
-
1 * 53000, enzyme form GA-I, SDS-PAGE
550000
-
detergent solubilized enzyme, gel filtration
56583
-
x * 56000, SDS-PAGE, x * 56583, mass spectrometry
57151
-
x * 62000, SDS-PAGE, x * 57151, mass spectrometry
58600
-
glucoamylase 2, ultracentrifugal equilibrium sedimentation
61400
-
glucoamylase 3, ultracentrifugal equilibrium sedimentation
62031
endophytic fungus EF6
-
1 * 62200, SDS-PAGE, 1 * 62031, mass spectrometry
62200
endophytic fungus EF6
-
1 * 62200, SDS-PAGE, 1 * 62031, mass spectrometry
62800
x * 62800, deduced from nucleotide sequence
65400
Thermochaetoides thermophila
-
gel filtration and native PAGE
67000
-
glucoamylase II, gel filtration
67500
-
1 * 67500, SDS-PAGE
68000
-
experimental molecular weight for glucoamylase 2, excellent agreement with the theoretical value
72000 - 74000
-
gel filtration
72063
-
1 * 93000, wild-type and mutant enzyme, SDS-PAGE, 1 * 72876, wild-type enzyme, mass spectrometry, 1 * 72063, mutant enzyme, mass spectrometry
72876
-
1 * 93000, wild-type and mutant enzyme, SDS-PAGE, 1 * 72876, wild-type enzyme, mass spectrometry, 1 * 72063, mutant enzyme, mass spectrometry
77600
-
x * 77600, SDS-PAGE
79000
-
1 * 79000, glucoamylase G3, SDS-PAGE
79500
-
equilibrium sedimentation
79920
-
x * 77000, recombinant enzyme, SDS-PAGE, x * 79920, amino acid sequence calculation
80000
x * 80000, SDS-PAGE
82327
-
x * 82327, mass spectroscopy, recombinant GA expressed in Pichia pastoris
82330
-
recombinant enzyme expressed in Pichia pastoris, matrix-assisted laser desorption ionization mass spectrometry
82839
-
x * 82839, mass spectroscopy, recombinant GA expressed in Aspergillus niger
82840
-
recombinant enzyme expressed in Aspergillus niger, MALDI-MS
83700
-
calculation from diffusion and sedimentation data
83869
-
x * 83869, mass spectroscopy, recombinant GA expressed in Saccharomyces cerevisiae
83870
-
recombinant enzyme expressed in Saccharomyces cerevisiae, matrix-assisted laser desorption ionization mass spectrometry
84000
-
glucoamylase I, calculation from diffusion and sedimentation data
86000
-
glucoamylase II, calculation from diffusion and sedimentation data
86500
-
x * 86500, SDS-PAGE
89000
-
x * 60000, isozyme GA-I, SDS-PAGE, x * 89000, isozyme GA-II, SDS-PAGE
92000
x * 92000, extracellular enzyme
93000
-
1 * 93000, wild-type and mutant enzyme, SDS-PAGE, 1 * 72876, wild-type enzyme, mass spectrometry, 1 * 72063, mutant enzyme, mass spectrometry
94000
-
experimental molecular weight for GA1:L0
95000
-
x * 141000 + x * 95000, SDS-PAGE
96000
-
x * 96000, glucoamylase II, SDS-PAGE
98000
-
native extracellular enzyme, native PAGE
100000
-
glycoamylase I, density gradient ultracentrifugation
100000
-
mutant S54P/T314A/H415Y
100000
-
x * 100000, SDS-PAGE
140000
-
glucoamylase II, gel filtration
140000
-
x * 140000 + x * 85000, SDS-PAGE
26850
Cephalosporium eichhorniae
-
sucrose density gradient centrifugation
26850
Cephalosporium eichhorniae
-
SDS-PAGE, assumed
40000
Endomycopsis fibuligera
-
SDS-PAGE, assumed
40000
-
value about, SDS-PAGE, assumed
40000
-
1 * 40000, SDS-PAGE
42000
-
gel filtration
42000
-
SDS-PAGE, assumed
42000
-
SDS-PAGE, assumed
42000
-
x * 42000, SDS-PAGE
48000
-
glucoamylase I, gel filtration
48000
-
glucoamylase I, approach to equilibrium method, gel filtration
48000
-
x * 48000, SDS-PAGE
49000
-
glucoamylase II, approach to equilibrium method
49000
-
x * 49000, glucoamylase II, SDS-PAGE
54000
-
-
54000
-
glucoamylase III, gel filtration
54000
-
glucoamylase II, approach to equilibrium method, gel filtration
54000
-
1 * 54000, enzyme form GA-II, SDS-PAGE
55000
-
glucoamylase I, gel filtration
55000
-
1 * 55000, SDS-PAGE
56000
-
gel filtration
56000
-
x * 56000, SDS-PAGE
56000
-
x * 56000, SDS-PAGE, x * 56583, mass spectrometry
57000
-
gel filtration
57000
-
SDS-PAGE, assumed
57000
-
x * 57000, glucoamylase G5, SDS-PAGE
58000
-
gel filtration
58000
Endomycopsis fibuligera
-
gel filtration
58000
-
x * 58000, glucoamylase G4, SDS-PAGE
59000
-
glucoamylase I, approach to equilibrium method
59000
-
x * 59000, glucoamylase I, SDS-PAGE
60000
-
gel filtration
60000
x * 60000, SDS-PAGE
60000
-
x * 60000, glucoamylase II, SDS-PAGE
60000
-
1 * 60000, glucoamylase II, SDS-PAGE
60000
-
x * 60000, isozyme GA-I, SDS-PAGE, x * 89000, isozyme GA-II, SDS-PAGE
61000
-
SDS-PAGE, assumed
61000
-
1 * 61000, SDS-PAGE
61000
-
x * 61000, enzyme form GI, SDS-PAGE
62000
endophytic fungus EF6
-
gel filtration
62000
-
glucoamylase I, gel filtration
62000
-
isozyme GA-I, gel filtration
62000
-
experimental molecular weight for low-glycosylated linker variant dgGA
62000
-
x * 62000, deduced from nucleotide sequence
62000
-
x * 62000, SDS-PAGE, x * 57151, mass spectrometry
63000
-
gel filtration
63000
-
native enzyme, gel filtration
64000
Thermochaetoides thermophila
-
SDS-PAGE, assumed
64000
Thermochaetoides thermophila
-
1 * 64000, SDS-PAGE
64000
-
1 * 64000, isozyme GA-I, SDS-PAGE, 1 * 91000, isozyme GA-II, SDS-PAGE
65000
-
SDS-PAGE, assumed
65000
-
1 * 65000 + 1 * 33000, SDS-PAGE
66000
-
SDS-PAGE, assumed
66000
-
SDS-PAGE, assumed
66000
-
x * 66000, SDS-PAGE
66000
x * 66000, SDS-PAGE
66000
x * 66000, SDS-PAGE
66000
x * 66000, SDS-PAGE
66000
Thermochaetoides thermophila
x * 66000, recombinant enzyme, SDS-PAGE
66000
-
2 * 66000, enzyme active state, SDS-PAGE
66000
-
native extracellular enzyme, gel filtration
68400
-
SDS-PAGE assumed
68400
-
1 * 68400, SDS-PAGE
69000
-
-
69000
-
glucoamylase I, calculation from sedimentation and diffusion data
69000
-
1 * 69000, glucoamylase G5, SDS-PAGE
70000
-
calculated molecular weight for low-glycosylated linker variant dgGA
70000
-
x * 70000, enzyme form GII, SDS-PAGE
70000
-
x * 70000, glucoamylase M2, SDS-PAGE
70000
-
1 * 70000, glucoamylase G4, SDS-PAGE
70000
x * 70000, SDS-PAGE, recombinant glucoamylase
72000
-
native enzyme, native PAGE
72000
-
x * 72000, SDS-PAGE
72000
-
4 * 72000, SDS-PAGE
72000
-
x * 72000, glucoamylase I, SDS-PAGE
72000
-
x * 72000, glucoamylase 2, SDS-PAGE
73000
-
calculated molecular weight for dgGA:L0
73000
-
experimental molecular weight for glucoamylase1
73000
-
x * 73000, glucoamylase 1, SDS-PAGE
73000
4 * 73000, intracellular enzyme, SDS-PAGE
74000
-
glucoamylase G3, SDS-PAGE
74000
-
glucoamylase 1, ultracentrifugal equilibrium sedimentation
75000
gel filtration
75000
-
sucrose density gradient centrifugation
75000
-
glucoamylase I, approach to equilibrium method, gel filtration
75000
-
SDS-PAGE, assumed
75000
-
x * 75000, SDS-PAGE
75000
-
x * 75000, SDS-PAGE
75000
-
x * 75000, glucoamylase I, SDS-PAGE
76000
-
Bio-Sil-Sec-400 gel filtration
76000
-
SDS-PAGE, assumed
77000
-
-
77000
-
SDS-PAGE, assumed
77000
-
SDS-PAGE, assumed, value about
77000
-
x * 77000, recombinant enzyme, SDS-PAGE, x * 79920, amino acid sequence calculation
78000
-
x * 78000, enzyme form GIII, SDS-PAGE
78000
-
1 * 78000, glucoamylase 1 and 2, SDS-PAGE
78000
-
1 * 78000, glucoamylase I, SDS-PAGE
82000
-
gel filtration
82000
-
calculated molecular weight for glucoamylase1
83000
-
SDS-PAGE
83000
-
x * 83000, SDS-PAGE
85000
-
calculated molecular weight for GA1:L0
85000
-
x * 140000 + x * 85000, SDS-PAGE
87000
-
gel filtration
87000
-
native enzyme, gel filtration
88000
-
1 * 88000, SDS-PAGE
88000
-
1 * 88000, SDS-PAGE
90000
-
sucrose density gradient sedimentation
90000
-
isozyme GA-II, gel filtration
90000
-
experimental molecular weight for dgGA:L0
90000
-
x * 90000, glucoamylase I, SDS-PAGE
90000
-
x * 133000 + x * 90000, SDS-PAGE
90000
-
x * 90000, wild-type and mutant enzymes
91000
-
x * 91000, SDS-PAGE
91000
-
1 * 64000, isozyme GA-I, SDS-PAGE, 1 * 91000, isozyme GA-II, SDS-PAGE
additional information
-
value about 33000 or 65000
additional information
-
value about 75000 to 86000
additional information
-
value between 85000 and 14000
additional information
-
value between 95000 and 141000
additional information
-
values about 44700, 71000, 74500
additional information
-
values about 53000 and 54000
additional information
-
values about 66000, 70000, 75000
additional information
-
values about 69000 and 86500
additional information
-
values about 70000 and 90000
additional information
-
values of 150000, 68000, 84000, 79000
additional information
-
values of 74000, 58600, 61400
additional information
-
values of 74000, 63000 and 72800
additional information
-
values of 91000, 73000, 59000 and 70000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
oligomer
x * 80000, SDS-PAGE
?
-
x * 82327, mass spectroscopy, recombinant GA expressed in Pichia pastoris
?
-
x * 82839, mass spectroscopy, recombinant GA expressed in Aspergillus niger
?
-
x * 83869, mass spectroscopy, recombinant GA expressed in Saccharomyces cerevisiae
?
-
x * 75000, glucoamylase I, SDS-PAGE
?
-
x * 60000, glucoamylase II, SDS-PAGE
?
x * 78000, recombinant enzyme, SDS-PAGE, x * 55100, about, recombinant enzyme, sequence calculation
?
-
x * 78000, recombinant enzyme, SDS-PAGE, x * 55100, about, recombinant enzyme, sequence calculation
-
?
-
x * 90000, wild-type and mutant enzymes
?
-
x * 62000, SDS-PAGE, x * 57151, mass spectrometry
?
-
x * 90000, glucoamylase I, SDS-PAGE
?
-
x * 70000, glucoamylase M2, SDS-PAGE
?
x * 51000, extracellular enzyme, SDS-PAGE
?
-
x * 51000, extracellular enzyme, SDS-PAGE
-
?
-
x * 51000, extracellular enzyme, SDS-PAGE
-
?
-
x * 72000, glucoamylase 2, SDS-PAGE
?
-
x * 74000, glucoamylase G3, SDS-PAGE
?
-
x * 73000, glucoamylase 1, SDS-PAGE
?
-
x * 58000, glucoamylase G4, SDS-PAGE
?
-
x * 57000, glucoamylase G5, SDS-PAGE
?
-
x * 72000, glucoamylase 2, SDS-PAGE
-
?
-
x * 66000, SDS-PAGE
-
?
-
x * 77000, recombinant enzyme, SDS-PAGE, x * 79920, amino acid sequence calculation
?
x * 72920, about, sequence calculation
?
-
x * 72920, about, sequence calculation
-
?
-
x * 72920, about, sequence calculation
-
?
-
x * 105360, recombinant N-terminal catalytic domain, MALDI-TOF mass spectrometry
?
-
x * 48000, SDS-PAGE
-
?
-
x * 60000, isozyme GA-I, SDS-PAGE, x * 89000, isozyme GA-II, SDS-PAGE
?
-
x * 49000, glucoamylase II, SDS-PAGE
?
-
x * 59000, glucoamylase I, SDS-PAGE
?
-
x * 72000, glucoamylase I, SDS-PAGE
?
-
x * 96000, glucoamylase II, SDS-PAGE
?
-
x * 72000, glucoamylase I, SDS-PAGE
-
?
-
x * 96000, glucoamylase II, SDS-PAGE
-
?
x * 75400, SDS-PAGE, x* 65400, polypeptide without the signal peptide (616 amino acid residues), sequence calculation
?
-
x * 75400, SDS-PAGE, x* 65400, polypeptide without the signal peptide (616 amino acid residues), sequence calculation
-
?
-
x * 140000 + x * 85000, SDS-PAGE
?
-
x * 133000 + x * 90000, SDS-PAGE
?
x * 92000, extracellular enzyme
?
-
x * 56000, SDS-PAGE
-
?
x * 62800, deduced from nucleotide sequence
?
x * 70000, SDS-PAGE, recombinant glucoamylase
?
-
x * 70000, enzyme form GII, SDS-PAGE
?
-
x * 78000, enzyme form GIII, SDS-PAGE
?
-
x * 61000, enzyme form GI, SDS-PAGE
?
-
x * 56000, SDS-PAGE, x * 56583, mass spectrometry
?
-
x * 56000, SDS-PAGE, x * 56583, mass spectrometry
-
?
x * 88000, SDS-PAGE, x * 65989, calculated
?
Thermochaetoides thermophila
x * 66000, recombinant enzyme, SDS-PAGE
?
Thermochaetoides thermophila CT2
-
x * 66000, recombinant enzyme, SDS-PAGE
-
?
x * 66000, SDS-PAGE, x * 66400, calculated
?
-
x * 141000 + x * 95000, SDS-PAGE
?
x * 88000, SDS-PAGE, x * 65989, calculated
?
-
x * 88000, SDS-PAGE, x * 65989, calculated
-
?
-
x * 62000, deduced from nucleotide sequence
?
AAE85601
x * 75000, SDS-PAGE, recombinant protein, x * 62000, calculated
dimer
-
complex formation with a heterobidentate ligand induces dimerization
dimer
-
1 * 65000 + 1 * 33000, SDS-PAGE
dimer
-
2 * 150000, glucoamylase I, SDS-PAGE
dimer
-
1 * 116000 + 1 * 212000, SDS-PAGE
dimer
-
2 * 186000, SDS-PAGE
dimer
-
2 * 66000, enzyme active state, SDS-PAGE
monomer
-
1 * 83500, native enzyme, SDS-PAGE
monomer
-
1 * 88000, SDS-PAGE
monomer
-
1 * 67500, SDS-PAGE
monomer
-
1 * 72000-74000, SDS-PAGE
monomer
-
1 * 64000, isozyme GA-I, SDS-PAGE, 1 * 91000, isozyme GA-II, SDS-PAGE
monomer
-
1 * 64000, isozyme GA-I, SDS-PAGE, 1 * 91000, isozyme GA-II, SDS-PAGE
-
monomer
-
1 * 63000, SDS-PAGE
monomer
-
1 * 78000, glucoamylase I, SDS-PAGE
monomer
-
1 * 60000, glucoamylase II, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
monomer
-
1 * 72000, SDS-PAGE
monomer
-
1 * 72000, SDS-PAGE
-
monomer
-
a starch binding and a catalytic domain interspersed by a highly glycosylated polypeptide linker
monomer
-
1 * 93000, wild-type and mutant enzyme, SDS-PAGE, 1 * 72876, wild-type enzyme, mass spectrometry, 1 * 72063, mutant enzyme, mass spectrometry
monomer
-
1 * 68400, SDS-PAGE
monomer
-
1 * 79000, glucoamylase G3, SDS-PAGE
monomer
-
1 * 78000, glucoamylase 1 and 2, SDS-PAGE
monomer
-
1 * 69000, glucoamylase G5, SDS-PAGE
monomer
-
1 * 70000, glucoamylase G4, SDS-PAGE
monomer
-
1 * 79000, glucoamylase G3, SDS-PAGE
-
monomer
-
1 * 78000, glucoamylase 1 and 2, SDS-PAGE
-
monomer
-
1 * 69000, glucoamylase G5, SDS-PAGE
-
monomer
-
1 * 70000, glucoamylase G4, SDS-PAGE
-
monomer
-
1 * 58000, SDS-PAGE
monomer
Cephalosporium eichhorniae
-
1 * 26850, SDS-PAGE
monomer
endophytic fungus EF6
-
1 * 62200, SDS-PAGE, 1 * 62031, mass spectrometry
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 88000, SDS-PAGE
monomer
-
1 * 72800, SDS-PAGE
monomer
-
1 * 128000, glucoamylase II, SDS-PAGE
monomer
-
1 * 54000, enzyme form GA-II, SDS-PAGE
monomer
-
1 * 53000, enzyme form GA-I, SDS-PAGE
monomer
-
1 * 54000, enzyme form GA-II, SDS-PAGE
-
monomer
-
1 * 53000, enzyme form GA-I, SDS-PAGE
-
monomer
-
1 *75000, SDS-PAGE
monomer
-
1 * 82000, SDS-PAGE
monomer
-
1 * 69000, SDS-PAGE
monomer
-
1 * 69000, SDS-PAGE
-
monomer
-
1 * 66000, native extracellular enzyme, SDS-PAGE
monomer
-
1 * 66000, native extracellular enzyme, SDS-PAGE
-
monomer
-
1 * 105000, SDS-PAGE
monomer
-
1 * 61000, SDS-PAGE
monomer
-
1 * 75000, SDS-PAGE
monomer
Thermochaetoides thermophila
-
1 * 64000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
-
monomer
1 * 61500, SDS-PAGE
monomer
-
1 * 61500, SDS-PAGE
-
tetramer
4 * 73000, intracellular enzyme, SDS-PAGE
tetramer
-
4 * 72000, SDS-PAGE
tetramer
-
4 * 72000, SDS-PAGE
-
additional information
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The model of enzyme HrGA with two molecules in the asymmetric unit includes residues 29-616 and up to seven N-glycosylation sites and has acarbose bound in the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
-
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
-
additional information
the enzyme from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
additional information
-
the enzyme from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
additional information
-
the enzyme from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
structure-function relationship analysis
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
the G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region
additional information
-
the G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region
additional information
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
the starch-binding domain (SBD) of glucoamylase from Aspergillus niger is a small globular protein containing a disulfide bond. The structure of the SBD has been determined by NMR. Cys509 and Cys604 are at the N- and C-termini, respectively, and they are linked by a disulfide bond, analysis of the conformation surrounding the disulfide bond, overview
additional information
-
the starch-binding domain (SBD) of glucoamylase from Aspergillus niger is a small globular protein containing a disulfide bond. The structure of the SBD has been determined by NMR. Cys509 and Cys604 are at the N- and C-termini, respectively, and they are linked by a disulfide bond, analysis of the conformation surrounding the disulfide bond, overview
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
-
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
-
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
-
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
-
additional information
-
enzyme amino acid sequence analysis by MALDI-TOF mass spectrometry
additional information
the enzyme contains an N-terminal subunit, NtMGAM, that is proximal to the membrane-bound end and a C-terminal luminal subunit, CtMGAM, determination of the structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity, overview, NtMGAM has five major structural domains: a trefoil type-Pdomain, residues 1-51, an N-terminal beta-sandwich domain, residues 52269, a catalytic (beta/alpha)8 barrel domain, residues 270-651, with two inserted loops (i.e. insert 1, residues 367-416, and insert 2, residues 447-492, protruding out between beta3 and alpha3 and between beta4 and alpha4, respectively) a proximal C-terminal domain, residues 652-730, and a distal C-terminal domain, residues 731-868, both with beta-sandwich topologies, structure comparison with other glycosyl hydrolase family 31 enzymes, overview
additional information
-
the enzyme contains an N-terminal subunit, NtMGAM, that is proximal to the membrane-bound end and a C-terminal luminal subunit, CtMGAM, determination of the structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity, overview, NtMGAM has five major structural domains: a trefoil type-Pdomain, residues 1-51, an N-terminal beta-sandwich domain, residues 52269, a catalytic (beta/alpha)8 barrel domain, residues 270-651, with two inserted loops (i.e. insert 1, residues 367-416, and insert 2, residues 447-492, protruding out between beta3 and alpha3 and between beta4 and alpha4, respectively) a proximal C-terminal domain, residues 652-730, and a distal C-terminal domain, residues 731-868, both with beta-sandwich topologies, structure comparison with other glycosyl hydrolase family 31 enzymes, overview
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate bindingwith highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
-
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate bindingwith highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
Mucor rouxians
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
Mucor rouxians
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
peptide sequencing by mass spectrometry
additional information
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
the sequences from 1-19, 39-454, and 533-629 belong to the signal peptide, the catalytic domain of the glycosyl hydrolase family 15, and the starch-binding domain, respectively. Construction of a three-dimensional structure of PoGA15A by modelling using the known crystal structure of the glucoamylase from Hypocrea jecorina (PDB 2vn7). The three-dimensional structure shows that the catalytic domain is predicted to mainly contain an alpha-helix and a beta-propeller, which form the barrel structure. The starch-binding domain is predicted to have a beta-sandwich fold with eight beta-strands distributed in the two beta-sheets
additional information
-
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
-
additional information
-
glucoamylases consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. The relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
-
additional information
-
the sequences from 1-19, 39-454, and 533-629 belong to the signal peptide, the catalytic domain of the glycosyl hydrolase family 15, and the starch-binding domain, respectively. Construction of a three-dimensional structure of PoGA15A by modelling using the known crystal structure of the glucoamylase from Hypocrea jecorina (PDB 2vn7). The three-dimensional structure shows that the catalytic domain is predicted to mainly contain an alpha-helix and a beta-propeller, which form the barrel structure. The starch-binding domain is predicted to have a beta-sandwich fold with eight beta-strands distributed in the two beta-sheets
-
additional information
-
secondary structure analysis, the enzyme contains a family 21 carbohydrate-binding module involving residues W47, Y83, and Y93, the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, molecular modelling, structure-function relatioship
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate bindingwith highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
the enzyme contains a carbohydrate-binding module, which functions independently to assist the carbohydrate-active enzyme, structure of a family 21 CBM from the starch-binding domain of Rhizopus oryzae glucoamylase, RoCBM21, determined by NMR spectroscopy, CBM has a beta-sandwich fold with an immunoglobulin-like structure, ligand-binding properties, comparisons of CBM structures and topologies, docking simulations, overview
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
additional information
-
glucoamylase is a two-domain protein composed by a N-terminal serinethreonine-rich domain and a C-terminal domain with the typical structure of the catalytic domain of fungal glucoamylases
additional information
structure analysis of Sta1p, modelling
additional information
-
glucoamylase is a two-domain protein composed by a N-terminal serinethreonine-rich domain and a C-terminal domain with the typical structure of the catalytic domain of fungal glucoamylases
-
additional information
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
-
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
-
additional information
-
enzyme structure modelling and comparison of the structural model of Tetracladium sp. glucoamylase with the solved structure of the Hypocrea jecorina glucoamylase
additional information
-
two protein bands with MW of 70000 Da and 76000 Da are deteced by SDS-PAGE
additional information
the enzyme contains a signal peptide for secretion joined to the catalytic domain by a linker
additional information
-
the enzyme contains a signal peptide for secretion joined to the catalytic domain by a linker
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
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A276C/S347C
101% of wild-type kcat
A276C/S347C/S298C
107% of wild-type kcat
C320A
-
barely improved thermostability or altered activity
D71N
-
increase in thermosability at 65 and 75°C
DELTA439-441
-
increase in thermosability at 65 and 75°C
E389M
104% of wild-type kcat
G127A/P128A
-
site-directed mutagenesis, the mutation decreases the enzyme thermostability compared to the wild-type protein
G137A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
G139A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
G183K
-
slight increase in activity as compared with the wild-type enzyme towards maltose. The mutation broadens the optimal pH range for activity towards acidic as well as alkaline conditions. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
G396A
90% of wild-type kcat
G396A/G407A
92% of wild-type kcat
G407A
96% of wild-type kcat
G447S
-
increase in thermosability at 65 and 75°C
H391M
89% of wild-type kcat
I136L
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
P128A
-
site-directed mutagenesis, the mutant destabilizes the enzyme
P128A/G139A/I136L
-
site-directed mutagenesis, mutations G139A and I136L, located in the center of alpha-helix, completely compensate for the destabilization caused by substitution P128A
P307A/T310V/Y312M/N313G
-
up to 15fold decreased turnover-number for alpha-1,4-linked substrates. Up to 9fold increase in Km-value for alpha-1,6-linked substrates
Q409P
-
increase in thermosability at 65 and 75°C
S119Y
-
slight increase in activity as compared with the wild-type enzyme towards maltose. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
S184H
-
slight increase in activity as compared with the wild-type enzyme towards maltose. The mutation broadens the optimal pH range for activity towards acidic as well as alkaline conditions. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
S298C/L354C
104% of wild-type kcat
S386L
103% of wild-type kcat
S411A
-
54-74% of the catalytic efficiency of the wild type enzyme. Increased pH-optimum by 0.8 units for both maltose and maltoheptaose hydrolysis while maintaining a high level of activity and catalytic efficiency. In hydrolysis of 28% DE 10 maltodextrin, the mutant enzyme has a pH optimum of 7 compared with 5.6 for wild-type enzyme, and has higher initial rates of glucose production than wild-type enzyme at all pH values tested above pH 6.6
S411C
-
54-74% of the catalytic efficiency of the wild type enzyme
S411D
-
6-12% of the catalytic efficiency of the wild type enzyme
S411G
-
catalytic efficiency like that of wild type enzyme for isomaltose, maltose and maltoheptaose hydrolysis at pH 4.4
S411H
-
6-12% of the catalytic efficiency of the wild type enzyme
S418L
103% of wild-type kcat
S54P/T314A/H415Y
-
the mutant enzyme is more thermostable compared to the wild-type enzyme at 70°C. The mutation does not affect the protein secretion nor the production of the enzyme
T390L
101% of wild-type kcat
T416L
101% of wild-type kcat
V181T/N182Y/G183A
-
2fold increased Km-value for alpha-1,4-linked substrates: For alpha-1,6-linked substrates a 2fold increase in Km and a 3fold decrease in turnover-number
V181T/N182Y/G183A/P307A/T310V/Y312M/A313G
-
remarkably low Km-value for isomaltotriose through isomaltoheptaose and elevated turnover-number on isomaltose, resulting in an approximately 2fold improved catalytic effeciency
S54P/T314A/H415Y
-
the mutant enzyme is more thermostable compared to the wild-type enzyme at 70°C. The mutation does not affect the protein secretion nor the production of the enzyme
-
A246C
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
-
G137A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
-
G139A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
-
P128A
-
site-directed mutagenesis, the mutant destabilizes the enzyme
-
D20C/A27C/S30P/G137A
-
site-directed mutagenesis, the mutant, designated THS8, is highly thermotolerant with increased stability at 80°C compared to the wild-type enzyme
H391Y
-
random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
R54L
-
active site mutant. For inhibitor acarbose, a rapid binding event is apparently intersected by a slower secondary binding event. Mutant shows a dramatically higher Kd value for acarbose
T290A
-
random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
T62A
-
random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
W120F
-
mutant of G1, 3% of wild-type kcat for maltose, 2% of kcat for maltotriose
W317F
-
mutant of G1, 90% of wild-type kcat for maltose, 97% of kcat for maltotriose
W52F
-
mutant of G2, almost no activity with maltose and maltotriose
Y175F
-
mutation in subsite +3. Mutant displays only minor differences to wild-type in affinities to inhibitors acarbose and an acarbose conjugate
I339G
about 10% of wild-type specific activity
T47A
about 50% of wild-type specific activity
T47A/W48A
about 25% of wild-type specific activity
W48A
about 55% of wild-type specific activity
I339G
-
about 10% of wild-type specific activity
-
T47A
-
about 50% of wild-type specific activity
-
T47A/W48A
-
about 25% of wild-type specific activity
-
W48A
-
about 55% of wild-type specific activity
-
W47A
-
site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
Y32A
-
site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
Y32A/Y47A
-
site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
H447A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A/D450A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
R15A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
T462A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
H447A/D450A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
R15A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
T462A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
H447A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
H447A/D450A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
R15A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
T462A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
W622C
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 87% reduced activity compared to the wild-type enzyme
W622D
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95% reduced activity compared to the wild-type enzyme
W622G
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95.7% reduced activity compared to the wild-type enzyme
W622H
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 48% reduced activity compared to the wild-type enzyme
W622S
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 83% reduced activity compared to the wild-type enzyme
W622C
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 87% reduced activity compared to the wild-type enzyme
-
W622D
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95% reduced activity compared to the wild-type enzyme
-
W622G
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95.7% reduced activity compared to the wild-type enzyme
-
W622H
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 48% reduced activity compared to the wild-type enzyme
-
W622S
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 83% reduced activity compared to the wild-type enzyme
-
A246C
-
the T50-value is enhanced by 4°C to 73°C. Compared to wild-type enzyme, the mutant is twice as active at 66°C but half as active at 45°C
A246C
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
E400C
-
cysteinesulfinic acid derivative of C320A/E400C-SO2H has a 700times higher turnover number towards maltose relative to C320A/E400C, while the Km-value is unchanged. Compared to wild-type enzyme, the C400-SO2H derivative has a turnover number of 150-190% and 85-320% on maltooliogosaccharides and isomaltooligosaccharides respectively, while Km-values are similar to that of wild-type for disaccharides and 3.5-5.5fold and 1.8-2.5fold higher for the longer maltooligosaccharides and isomaltooligosaccharides. The inhibition constant of cysteinesulfinic acid derivative of C320A/E400C-SO2H for acarbose increases more than 10000-fold
E400C
-
further oxidation of Cys thiol group to sulfinic acid, up to 300% higher kcat and decreased Km compared to wild-type, depending on substrate
E180Q
-
mutant of G1, 48% of wild-type kcat for maltose, 88% of kcat for maltotriose
E180Q
-
active site mutant. For inhibitor acarbose, a rapid binding event is apparently intersected by a slower secondary binding event. Mutant shows a dramatically higher Kd value for acarbose
additional information
-
the enzyme from commercial preparation is immobilized by sorption on a carbon support Sibunit, starch and dextrin hydrolysis kinetic parameters of glucoamylase, including the rate constant of thermal inactivation, show that immobilization of the enzyme results in a 1000fold increase in enzyme stability in comparison to the dissolved enzyme, presence of the dextrin substrate has a stabilizing effect, increase in dextrin concentration to 53% increases the thermostability of the immobilized enzyme, the immobilized-enzyme biocatalyst for starch saccharification has a high operational stability, half-inactivation time at 60°C exceeds 30 days, method optimization, overview
additional information
-
the enzyme immobilized on foamed glass covered with the catalytic filament carbon layer is highly active and stable, the effect of the carbon layer synthesized on the surface of aluminum oxide on the properties of biocatalysts shows that the glucoamylase adsorbed on the carbon-containing mesoporous ny-aluminum oxide exhibits a greater activity than the glucoamylase adsorbed on the macroporous alpha-aluminum oxide, kinetics, overview
additional information
-
molecular construction, molecular modeling and molecular dynamics of engineered enzyme with higher thermostability through optimized intrinsic interactions within alpha-helix D, overview
additional information
-
molecular construction, molecular modeling and molecular dynamics of engineered enzyme with higher thermostability through optimized intrinsic interactions within alpha-helix D, overview
-
additional information
-
immobilization of the enzyme on polyaniline polymer results in improved catalytic performance with decreased temperature optimum, and increased thermal stability and catalytic efficiency with increased Vmax and reduced Km, overview
additional information
-
improvement of enzyme for inductrial applications
additional information
-
entrapment of amyloglucosidase into dipalmitoylphosphatidylcholine multilamellar vesicles and large unilamellar vesicles, vesicle formation, method optimization, enzyme activity is very stable during the first three batch runs, overview
additional information
-
random mutagenesis and mutant screening by plate thermostability assay for increased thermotolerance at 65-80°C, overview
additional information
-
engineered low-glycosylated variant of glucoamylase 1 with a short linker, low-glycosylated GA1 (dgGA). Low-glycosylated linker variant of GA1; GA1:L0 and dgGA:L0
additional information
-
disulfide-deficient mutant of the starch-binding domain of glucoamylase
additional information
-
improvement of enzyme for inductrial applications
-
additional information
presence of the beta domain is essential for catalytic activity of the enzyme. The catalytic domain alone is not able to hydrolyze soluble starch while starch hydrolysis activity is restored in the catalytic domain in the presence of the beta domain. The catalytic domain displays lower thermostability compared with the intact wild-type and exhibits enhanced thermostability in the presence of the beta domain in vitro. Truncation of the wild-type enzyme or mutagenesis of the residues that participate in the interdomain interaction at its beta domain also lead to the reduced thermostability of the enzyme
additional information
-
presence of the beta domain is essential for catalytic activity of the enzyme. The catalytic domain alone is not able to hydrolyze soluble starch while starch hydrolysis activity is restored in the catalytic domain in the presence of the beta domain. The catalytic domain displays lower thermostability compared with the intact wild-type and exhibits enhanced thermostability in the presence of the beta domain in vitro. Truncation of the wild-type enzyme or mutagenesis of the residues that participate in the interdomain interaction at its beta domain also lead to the reduced thermostability of the enzyme
additional information
-
presence of the beta domain is essential for catalytic activity of the enzyme. The catalytic domain alone is not able to hydrolyze soluble starch while starch hydrolysis activity is restored in the catalytic domain in the presence of the beta domain. The catalytic domain displays lower thermostability compared with the intact wild-type and exhibits enhanced thermostability in the presence of the beta domain in vitro. Truncation of the wild-type enzyme or mutagenesis of the residues that participate in the interdomain interaction at its beta domain also lead to the reduced thermostability of the enzyme
-
additional information
CauloGA gene product that is expressed in Escherichia coli is prone to forming inclusion bodies. Most of the gene product is expressed in a soluble and active form when it was expressed as a fusion protein with Staphylococcus Protein A
additional information
-
CauloGA gene product that is expressed in Escherichia coli is prone to forming inclusion bodies. Most of the gene product is expressed in a soluble and active form when it was expressed as a fusion protein with Staphylococcus Protein A
-
additional information
-
purified glucoamylase is chemically modified by cross-linking with aniline hydrochloride in the presence of 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide for 1, 7, or 13 min, resulting in aniline-coupled glucoamylase-1/ACG-1, aniline-coupled glucoamylase-7/ACG-7, and 13 min aniline-coupled glucoamylase-13/ACG-13, the aniline coupling of GA has profound enhancing effects on temperature, pH optima, and pKas of active site residues, overview
additional information
-
enzyme immobilization on polyacrylamide gel highly decreases the entropy and enthalpy of thermal enzyme deactivation
additional information
-
co-expressed recombinant barley alpha-amylase 1 mutant and recombinant GLA synergistically enhanced the rate of hydrolysis by about 3fold for corn and wheat starch granules, compared to the sum of the individual activities, exo-endo synergism, reaction ratios, overview
additional information
effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase. Deletion of the starch-binding domain for raw starch-digesting glucoamylase rPoGA15A leads to reduced activity of the truncated enzyme with raw starches
additional information
-
effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase. Deletion of the starch-binding domain for raw starch-digesting glucoamylase rPoGA15A leads to reduced activity of the truncated enzyme with raw starches
-
additional information
-
preparation of Ca-alginate gel beads, activation by p-benzoquinoone, and immobilization of purified enzyme, method, development, comparison of catalytic activities of free and immobilized enzyme, overview. Km values of free and entrapped glucoamylase are almost identical, while the covalently immobilized enzyme shows the lowest affinity for substrate. The covalently immobilized enzyme retains its activity over 36 days of shelf storage and after 30 repeated use runs
additional information
-
sga1delta, significant reduction in conidiation
additional information
-
improvement of enzyme for inductrial applications
additional information
-
use of cell surface engineering to display Rhizopus oryzae glucoamylase on the cell surface of yeast Saccharomyces cerevisiae, improvement in enzymatic desizing of starched cotton cloth using yeast codisplaying glucoamylase and cellulose-binding domain, overview
additional information
-
improvement of enzyme for industrial applications
additional information
-
immobilization of the enzyme onto chemically synthesized poly(o-toluidine) salt and base powders using adsorption and covalent crosslinking with glutaraldehyde, overview, The immobilized enzyme has a better thermal stability than the free enzyme
additional information
-
construction of a series of hybrid enzymes by interchanging domains of glucoamylase Sta1 from Saccharomyces cerevisiae and beta-glucosidase Bgl1 from Saccharomycopsis fibuligera strain ATCC 9947 based on the homology-based structural models of the two proteins. The replacement of native Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
additional information
-
construction of a mutant enzymes with improved catalytic activity with substrate starch by introduction of the starch binding domain from the glucoamylase of Aspergillus niger, overview
additional information
-
construction of a series of hybrid enzymes by interchanging domains of glucoamylase Sta1 from Saccharomyces cerevisiae and beta-glucosidase Bgl1 from Saccharomycopsis fibuligera strain ATCC 9947 based on the homology-based structural models of the two proteins. The replacement of native Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
-
additional information
-
enzyme is mutagenised using nitrous acid and gamma (60Co) irradiation in a sequential manner to isolate deregulated mutants for enhanced production of glucoamylase
additional information
-
enzyme is mutagenised using nitrous acid and gamma (60Co) irradiation in a sequential manner to isolate deregulated mutants for enhanced production of glucoamylase
-
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20
-
purified enzyme, 30-40% remaining activity
22 - 30
-
purified enzyme, pH 6.0, 6-8 h, stable
27
-
purified isozymes, 72 h, no loss in activity
30 - 60
-
6 h, pH 7.0, completely stable at 30°C, loss of 10% activity at 40°C, loss of 20% at 50°C, and of 30% at 60°C
30 - 65
-
completely stable for 1 h
30 - 80
recombinant enzyme GlucaM retains full activity after 1 h of incubation at below 60°C and retains about 60% of the original activity after 1 h at 70°C, but it loses 60% of the original activity after 1 h of incubation at 80°C
37
-
freshly isolated purified commercial preparation, 10 h, loss of 50% activity, purified commercial preparation after 6 months of storage, 10 h, loss of 75% activity
4
-
no loss of activity after 8 d
4 - 50
purified enzyme, stable at
40 - 70
-
30 min, glucoamylase I and II, stable
46
-
40 min, about 20% loss of activity
52
-
40 min, about 40% loss of activity
56
-
40 min, about 85% loss of activity
60 - 80
-
the thermal stability at 70°C and other temperatures of the deglycosylated enzyme is reduced compared to the native enzyme
68
-
4.5% remaining activity
70 - 80
-
irreversible thermoinactivation kinetic analysis of recombinant wild-type and mutant enzymes, overview
99
purified enzyme, pH 4.5, 10 min, inactivation
100
purified recombinant enzyme, pH 5.0, loss of 43% activity after 15 min, loss of 80% activity after 30 min, and of 88% after 45 min, inactivation after 60 min
100
-
36% remaining activity after 10 min at pH 7.0, loss of 89% activity at pH 5.0
30
-
enzyme in solid-state fermentation process of chestnut, pH 6.0, about 90% remaining activity after 24 h
30
-
purified enzyme, stable
30
-
10 min, enzyme form GA-II is stable up to
30 - 40
-
purified enzyme, completely stable for 2 h
30 - 40
-
purified enzyme, 80% of maximal activity within this range
40
-
approx. 15% loss of activity after 30 min
40
-
purified native enzyme, 30 min, stable
40
-
purified isozymes, 72 h, no loss in activity
40
purified extracellular enzyme, pH 5.0, 1 h, stable up to
40
-
isozyme GA-I, stable up to
40
-
10 min, enzyme form GA-I is stable up to
40
-
15 min, stable up to
40
-
30 min, purified recombinant AmyC and AmyD, completely stable, rapid inactivation above
40
-
purified enzyme, pH 6.0, loss of 30% activity after 2 h, loss of 60% activity after 8 h
45
-
purified native enzyme, 60 min, 59% activity remaining
45
-
purified native enzyme, after 90 min about 95% of activity is remaining, after 300 min 20% activity remains
45
-
pH 4.5, 10 min, quite stable up to
50
-
stable up to
50
-
purified isozymes, 72 h, 46% activity remaining
50
-
purified native enzyme, 1 h, stable, 50% activity remaining after 2 h
50
-
half-life of free enzyme is 33.8 h, half-life of immobilized enzyme is 190 h
50
-
pH 4.5, 30 min, stable
50
-
pH 5.0, soluble enzyme half-life: 160 h, liposome-entrapped enzyme shows full activity after 180 h
50
-
glucoamylase M1, stable
50
-
pH 6.0, 5 min, stable up to
50
purified extracellular enzyme, pH 5.0, 1 h, loss of 50% activity
50
-
15 min, stable in presence of 1.25% soluble starch, about 80% loss of activity without starch
50
-
purified enzyme, 70% remaining activity
50
Endomycopsis fibuligera
-
pH 5.5, 30 min, stable
50
endophytic fungus EF6
-
purified enzyme, 1 h, stable up to, rapid decrease in activity above
50
-
half-life of native enzyme is 128 min
50
-
native enzyme shows a half-life of 128.37 min
50
-
purified native enzyme, 79% remaining activity after 60 min
50
-
stable up to, recombinant enzyme
50
-
recombinant enzyme, stable up to, stability is enhanced by Ca2+
50
-
2 h, about 50% loss of activity of enzyme form E4', about 15% loss of activity of enzyme form E4
50
-
pH 4.6, 15 min, stable up to
50
-
pH 6.4, 15 min, stable up to
50
-
purified enzyme in absence of substrate, 1 h, stable
50
purified native enzyme, pH 4.5, 1 h, completely stable up to
50
purified recombinant intracellular enzyme, 48 h, stable
50
-
30 min, 85% loss of activity
50
-
30 min, inactivation of both purified recombinant AmyC and AmyD
50
-
pH 6.0, 5 min, stable
50
-
60 min, 45% of activity of the free enzyme is remaining, and 70-95% of the immobilized enzyme
50
-
60 min, 50% loss of activity
50
-
purified enzyme, pH 6.0, 1 h, loss of 90% activity
50
-
30 min, mutants W622C and W622S, stable
50
-
6 h, completly stable
50
-
purified recombinant enzyme, 48 h, 25% increased activity
50 - 60
-
stable
50 - 60
Thermochaetoides thermophila
-
stable at, purified enzyme
55
-
no loss of activity after 30 min
55
Arachniotus sp.
-
no loss of activity after 5 min at pH 5.5
55
-
freshly isolated purified commercial preparation, 10 h, loss of over 80% activity, purified commercial preparation after 6 months of storage, 10 h, loss of over 90% activity
55
-
10 min, pH 4.0, enzyme form G1, G2, G3, G4 and G5, stable up to
55
endophytic fungus EF6
-
purified enzyme, 1 h, 45% activity remaining
55
-
half-life of purified enzyme is 7 min, irreversible inactivation
55
-
no loss of activity after 1 h
55
-
purified enzyme in absence of substrate, 1 h, stable
55
-
15 min, stable up to
55
purified native enzyme, pH 4.5, 1 h, 90% activity remaining
55
purified recombinant intracellular enzyme, half-life is 8 h
55
-
60 min, 60% loss of activity
60
-
approx. 20% loss of activity after 30 min
60
Arachniotus sp.
-
approx. 5% loss of activity after 5 min at pH 5.5
60
-
purified recombinant enzyme mutant S54P/T314A/H415Y, stable up to, irreversible thermo-inactivation of the mutant enzyme follows first-order kinetics
60
-
purified enzyme, about 62% of initial activity remains after 1 h of incubation
60
purified recombinant enzyme, pH 5.0, stable for 15 min, loss of 20% activity after 30 min, and of 50% after 45 min, 12% activity remains after 90 min, inactivation after 120 min
60
-
pH 4.5, 5 min, stable up to
60
-
pH 4.5, 30 min, 10% loss of activity
60
-
half-life of wild-type enzyme is 3.6 h, of mutant enzyme 7.3 h
60
-
100% enzyme activity after 240 min at 60°C
60
-
complete loss of activity above
60
-
40 min, complete loss of activity
60
purified extracellular enzyme, pH 5.0, 1 h, inactivation
60
-
pH 7.0, half-life is 13 h
60
-
half-life of native enzyme is 25 min
60
-
native enzyme shows a half-life of 25.67 min, ACG-13 shows a half-life of 67.3 min
60
-
purified native enzyme, half-life is 26 min
60
-
immobilized enzyme, stable up to, melting temperature of the free enzyme
60
-
isozyme GA-II, stable up to
60
-
half-life more than 60 min
60
-
purified enzyme in absence of substrate, half-life is 45 min
60
purified native enzyme, pH 4.5, 1 h, 30% activity remaining
60
purified recombinant intracellular enzyme, half-life is 1 h
60
-
5 min, more than 95% loss of activity
60
-
pH 6.0, 5 min, complete inactivation
60
-
60 min, 90% loss of activity
60
Thermochaetoides thermophila
purified recombinant enzyme, stable
60
-
50% loss of activity after 12 h
60
-
pH 6.0, 6 h, about 40% loss of activity, half-life: 7.3 h
60
-
no loss of activity after 30 min
60
AAE85601
stable for 30 min
65
-
approx. 80% loss of activity after 30 min
65
Arachniotus sp.
-
50% loss of activity after 5 min at pH 5.5
65
-
purified recombinant enzyme mutant S54P/T314A/H415Y, half-life is 76 min
65
-
purified isozymes, 95% activity remaining
65
-
60 min, 2.5% loss of activity
65
-
pH 7.0, half-life is 8 h
65
-
37°C, 10 min, stable up to
65
-
80% remaining activity
65
-
10 min, 50% loss of activity
65
purified native enzyme, pH 4.5, 1 h, 20% activity remaining
65
purified recombinant intracellular enzyme, inctivation within 5 min
65
approx. 20% and 50% losss of activity after 20 h and 48 h, respectively, in the presence of 30% glucose
65
Thermochaetoides thermophila
-
60 min, 50% activity remaining of purified enzyme
70
Arachniotus sp.
-
approx. 90% loss of activity after 5 min at pH 5.5
70
-
purified enzyme, about 45% of initial activity remains after 1 h of incubation
70
-
half-life in absence of starch: 15 min. Half-life in presene of 3% w/v starch or sorbitol: 50 min. Half-life in presence of 10% sorbitol: 40 min. Half-life in presence of 30% sorbitol: 65 min
70
-
250 min, immobilized enzyme loses 60% of its activity, half-life: 220 min. Free enzyme loses 75% of its activity, half-life 140 min
70
-
crosslinked glucoamylase crystals, 1.5% loss of activity after 1 h in the presence of 4% starch, soluble glucoamylase, 17% loss of activity in the presence of 4% starch, complete loss of activity in the absence of starch
70
-
isoform GAM-1, half-life 45 min, isoform GAM-2, half-life 216 min
70
-
pH 6.0, 5 min, complete loss of activity
70
-
1 h, about 50% loss of activity
70
-
pH 7.0, half-life is 40 min
70
-
fairly stable at approximately 4% of soluble starch
70
Cephalosporium eichhorniae
-
15 min, 50% inactivation
70
-
purified enzyme, 30-40% remaining activity
70
-
melting temperature of the immobilized enzyme
70
-
rapid inactivation above
70
purified native enzyme, pH 4.5, 1 h, inactivation
70
-
no loss of activity after 24 h, 90% loss of activity after 60 h
70
-
no loss of activity after 24 h, 90% loss of activity after 60 h
70
-
60 min, loss of activity of the free enzyme, and 60-90% activity remaining of the immobilized enzyme
70
-
no loss of activity after 30 min
70
Thermochaetoides thermophila
-
30 min, 40% activity remaining of purified enzyme
70
Thermochaetoides thermophila
purified recombinant enzyme, 60 min, 80% remaining activity
70
-
pH 6.0, half-life: 30 min
70
-
no loss of activity after 24 h, 90% loss of activity after 60 h
70
-
30-40% loss of activity after 10 min, approx. 90% loss of activity after 40 min, complete loss of activity after 60 min
70
AAE85601
30 min, 60-70% residual activity
70
purified enzyme, inactivation
75
Arachniotus sp.
-
almost complete loss of activity after 5 min at pH 5.5
75
-
no activity loss after incubation at 75°C for 6 h, half life at 80°C 2.6 h
80
-
purified enzyme, about 28% of initial activity remains after 1 h of incubation
80
purified recombinant enzyme, pH 5.0, loss of 8% activity after 15 min, loss of 20% activity after 30 min, and of 75% after 45 min, 3% activity remains after 75 min, inactivation after 90 min
80
-
crosslinked glucoamylase crystals, 23% loss of activity after 1 h in the presence of 4% starch, soluble glucoamylase, 38% loss of activity in the presence of 4% starch, complete loss of activity in the absence of starch
80
-
half-life less than 3 min
80
-
stable up to for 30 min at pH 7.0, loss of 40% activity at pH 5.0
80
Endomycopsis fibuligera
-
complete loss of activity
80
-
25% loss of activity after 24 h
80
-
no loss of activity after 24 h, 90% loss of activity after 60 h
80
Thermochaetoides thermophila
purified recombinant enzyme, half-life is 40 min
80
-
50% loss of activity after 7 h
80
-
pH 6.0, half-life: 10 min
80
-
no loss of activity after 24 h, 90% loss of activity after 60 h
80
-
purified recombinant enzyme, half-life in absence of Ca2+ is 15 min, in presence of 5 mM Ca2+ is 2 h
90
purified recombinant enzyme, pH 5.0, loss of 12% activity after 15 min, loss of 75% activity after 30 min, and of 85% after 45 min, inactivation after 75 min
90
-
crosslinked glucoamylase crystals, 48% loss of activity after 1 h in the presence of 4% starch, soluble glucoamylase, 55% loss of activity in the presence of 4% starch, complete loss of activity in the absence of starch
90
-
no loss of activity after 12 h, 50% loss of activity after 24 h
90
-
no loss of activity after 12 h, 50% loss of activity after 24 h
90
-
50% loss of activity after 30 min
90
Thermochaetoides thermophila
purified recombinant enzyme, half-life is 10 min
90
-
no loss of activity after 12 h, 50% loss of activity after 24 h
90
-
purified recombinant enzyme, 4 min, 2% of maximal activity remaining in absence of Ca2+, 68% in presence of 5 mM Ca2+
additional information
-
-
additional information
-
starch or glycerol improve the thermal stability
additional information
-
thermostability of immobilized glucoamylase increases considerably as a result of covalent immobilization onto poly(2-hydroxyethyl methacrylate)/ethylene glycol dimetharylate microspheres
additional information
-
inactivation kinetics
additional information
-
the deglycosylated enzyme shows a higher aggregation rate compared to the native enzyme dependent on pH and presence of divalent cations, e.g. Mg2+ or Ca2+
additional information
-
the enzyme immobilized on polyaniline polymer shows an increased temperature stability compared to the free enzyme
additional information
-
during the thermal inactivation progress, combined with the loss of the helical structure and a majority of the tertiary structure, tryptophan residues are partially exposed and further lead to glucoamylases aggregating. The thermal stability of isoforms GAM-1 and GAM-2 is largely improved in the presence of sorbitol and trehalose by maintaining the native state of glucoamylases and preventing their thermal aggregation
additional information
-
stability profile
additional information
-
removal of N-linked sugar led to a significant decrease in thermostability
additional information
-
Ca2+ and Na+ highly increase the thermal stability of the enzyme
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2.53fold by DEAE-Fractogel and Concanacalin A-Sepharose chromatography
-
3 enzyme forms: GI, GII and GIII
-
5 forms of glucoamylase: G1-G5
-
affinity chromatography
-
affinity chromatography on acarbose-Sepharose, Q-Sepharose
-
affinity chromatography, ultrafiltration and ion exchange
-
ammonium sulfate fractionation, gel filtration
-
ammonium sulfate precipitation and gel filtration
-
ammonium sulfate precipitation, anion exchange, gel filtration, hydrophobic interaction chromatography
-
ammonium sulfate precipitation, anion exchange, hydrophobic interaction chromatography
Thermochaetoides thermophila
-
ammonium sulfate precipitation, gel filtration and ion exchange
ammonium sulfate precipitation, gel filtration, affinity chromatography
-
ammonium sulfate precipitation, ion exchange
-
ammonium sulfate, G-25 Sephadex, Mono Q, Econo-Pac S, TSK 2000 Gel
-
ammonium sulfate, Q-Sepharose, Mono Q, gel filtration
Arachniotus sp.
-
ammonium sulfate, Sephadex G-25
-
anion exchange and gel filtration chromatographie
-
anion exchange, gel filtration
-
crude glucoamylase preparation is partially purified by acetone precipitation (80% saturation) and is used in enzyme assays
-
DEAE-cellulose, ultrafiltration, CM-cellulose
-
ethanol precipitation and affinity chromatography using acarbose
-
ethanol precipitation, ion exchange and gel filtration
-
extracellular enzyme 1.32fold from crude cell extract by anion exchange chromatography and dialysis
-
further purification of the commercial preparation by anion exchange chromatography
-
glucoamylase starch binding domain, affinity purification on granular corn starch
glucoamylases from a wild-type and a deoxy-D-glucose-resistant mutant Aspergillus niger to apparent homogeneity by ammonium sulfate fractionation, anion exchange chromatography, and hydrophobic interaction chromatography, the wild-tyype enzyme is purified 25.4fold, the mutant 30.6fold
-
ion exchange and gel filtration
ion exchange, gel filtration
lyophilization, acetone precipitation, SP-Sepharose, Sephadex G-50
-
membrane filtration and gel filtration
Cephalosporium eichhorniae
-
native enzyme 14.49fold from culture medium by ammonium sulfate fractionation, anion exchange chromatography and gel filtration
endophytic fungus EF6
-
native enzyme 18fold from viscus, by ammonium sulfate fractionation, alternating gel filtration and ion exchange chromatography steps, to homogeneity
-
native enzyme 24fold by ammonium sulfate fractionation, dialysis, cation exchange chromatography, ultrafiltration, and gel filtration, to homogeneity
-
native enzyme 47.9fold by anion exchange chromatography and gel filtration
-
native enzyme 5.0fold by ammonium sulfate fractionation, gel filtration, and cation and anion exchange chromatography to homogeneity
-
native enzyme 60.61fold by ethanol precipitation, hydrophobic interaction chromatography, and cation exchange chromatography, recombinant secreted His-tagged truncated enzyme from Pichia pastoris strain GS115 culture supernatant by nickel affinity chromatography
native enzyme 63.3fold by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, followed by another step of anion exchange chromatography to homogeneity
-
native enzyme 63fold to homogeneity by ammonium sulfate precipitation, anion exchange and hydrophobic interaction chromatography, and again anion exchange chromatography
-
native enzyme 68.2% by dialysis, gel filtration and anion exchange chromatography, more than 90% of native GA A binds to raw starch
-
native enzyme 93fold from pancreas to homogeneity by glycogen precipitation, ion exchange chromatography, and gel filtration
-
native enzyme by ion exchange and hydrophobic interaction chromatography
-
native enzyme partially 10.2fold by ammonium sulfate fractionation, gel filtration, and ion exchange chromatography
-
native enzyme to homogeneity by anion exchange and hydrophobic interaction chromatography, and gel filtration
-
native extracellular enzyme 2.73fold from submerged culture by starch adsorption chromatography and gel filtration
-
native extracellular enzyme 26.2fold to homogeneity by ammonium sulfate precipitation, anion exchange chromatography, and hydrophobic interaction chromatography, followed by gel filtration
-
native extracellular enzyme 33.2fold by ammonium sulfate fractionation, anion exchange chromatography, hydrophobic interaction chromatography, ultrafiltration, and gel filtration
native extracellular enzyme 39fold to homogeneity by ammonium sulfate precipitation, anion exchange chromatography, and hydrophobic interaction chromatography
-
native extracellular enzyme 53.64fold by ammonium sulfate fractionation, hydrophobic interaction chromatography, ion exchange chromatography, and native PAGE
native extracellular enzyme from culture supernatant 7.3fold to homogeneity by ammonium sulfate fractionation and gel filtration
-
native isozymes 120fold by starch affinity chromatography, isozyme separation by PAGE zymography
-
native isozymes GA-I and GA-II
-
native soluble enzyme from culture medium 16.3 fold to homogeneity by ammonium sulfate fractionation, ion exchange and hydrophobic interaction chromatography, and gel filtration
Thermochaetoides thermophila
-
partially purification to 30fold homogeneity by heat treatment and gel filtration chromatography
-
precipitation with PEG, affinity chromatography, chromatofocusing
-
recombinant AmyC and AmyD from Pichia pastoris strain X33 culture supernatant by affinity chromatography, the recombinant enzymes are deglycosylated with endoglycosidase H and PNGase F
-
recombinant enzyme 22fold from Escherichia coli to homogeneity using heat treatment, anion exchange chromatography, and gel filtration
-
recombinant enzyme 80.9fold from Escherichia coli by heat treatment at 70°C, hydrophobic interaction chromatography, and gel filtration
recombinant enzyme from Aspergillus niger strain MBin118 by alpha-cyclodextrin affinity chromatography, elution with beta-cyclodextrin, followed by dialysis and ultrafiltration, to homogeneity
recombinant enzyme from Aspergillus niger strain MBin118 by alpha-cyclodextrin affinity chromatography, elution with beta-cyclodextrin, followed by dialysis, to homogeneity
recombinant enzyme from Escherichia coli strain MV1184 by heat treatment at 50°C for 30 min, two steps of ion exchange chromatography, and gel filtration
-
recombinant enzyme from Escherichia coli strain MV1184 by heat treatment at 56°C for 30 min, two steps of ion exchange chromatography, and gel filtration
-
recombinant enzyme from Pichia pastoris by ultrafiltration, gel filtration, and anion exchange chromatography to homogeneity
recombinant enzyme from Pichia pastoris strain GS115 culture supernatant
Thermochaetoides thermophila
recombinant enzyme mutant S54P/T314A/H415Y from Saccharomyces cerevisiae by acarbose affinity chromatography
-
recombinant enzyme to homogeneity from Saccharomyces cerevisiae cell culture medium, by ammonium sulfate fractionation, and anion exchange and affinity chromatography
-
recombinant glucoamylase
-
recombinant glucoamylase subunit Ct-MGAM splice form N20 and subunit Ct-SI from Spodoptera frugiperda Sf9 cells
recombinant glucoamylase, acarbose affinity chromatography
recombinant glucoamylase, ultrafiltration, SP-Sepharose, Q-Sepharose
recombinant His-tagged enzyme 10fold from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged enzyme 50.2fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant intracellular enzyme 37fold from Escherichia coli by heat treatment at 70°C for 30 min, anion exchange chromatography, and gel filtration to homogeneity
recombinant secreted His-tagged N-terminal subunit of human small intestinal enzyme from S2 cell culture medium by nickel affinity and anion exchange chromatography, followed by dialysis
-
recombinant wild-type and mutant enzymes from Saccharomyces cerevisiae strain AH22 medium by gel filtration and ion exchange chromatography to homogeneity
secreted, recombinant N-terminal catalytic domain from Drosophila S2 cell culture supernatant by chelating resin and anion exchange chromatography
-
starch affinity chromatography, partially purified
-
Superdex 200, Superose 12
three enzyme forms: glucoamylase 1, 2 and 3
-
three enzyme forms: I, II, and III
-
two enzyme forms: GA-I and GA-II
-
two native isozymes GA-I and GA-II, 5.8 and 9.6fold, respectively, to homogeneity
-
ultracentrifugation, anion exchange, gel permeation
-
ultrafiltrate, DEAE-Toyopearl 650 S, Sephadex G-150
-
ultrafiltration and gel filtration, anion exchange hydrophobic interaction chromatography
-
ultrafiltration, anion exchange, gel filtration
Endomycopsis fibuligera
-
ultrafiltration, gel filtration
-
ultrafiltration, gel filtration, affinity chromatography
-
ultrafiltration, ion exchange and gel filtration
-
-
-
-
Endomycopsis fibuligera
-
-
Cephalosporium eichhorniae
-
ammonium sulfate precipitation, gel filtration and ion exchange
-
ammonium sulfate precipitation, gel filtration and ion exchange
-
ammonium sulfate precipitation, gel filtration and ion exchange
-
ammonium sulfate precipitation, gel filtration and ion exchange
-
gel filtration
-
glucoamylase I and II
-
ion exchange and gel filtration
-
ion exchange and gel filtration
-
ion exchange, gel filtration
-
ion exchange, gel filtration
-
recombinant enzyme from Aspergillus niger strain MBin118 by alpha-cyclodextrin affinity chromatography, elution with beta-cyclodextrin, followed by dialysis, to homogeneity
recombinant enzyme from Aspergillus niger strain MBin118 by alpha-cyclodextrin affinity chromatography, elution with beta-cyclodextrin, followed by dialysis, to homogeneity
Superdex 200, Superose 12
-
Superdex 200, Superose 12
-
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analysis
-
method for anchoring native acarbose to gold chip surfaces for surface plasmon resonance studies employing glucoamylase as analyte. The key method is the chemoselective and protecting group-free oxime functionalization of the pseudo-tetrasaccharide-based inhibitor acarbose. At pH 7.0 the association and dissociation rate constants for the acarbose-glucoamylase interaction are 10000 per M and s and 103 per s, respectively, and the conformational change to a tight enzyme-inhibitor complex affects the dissociation rate constant by a factor of 100 per s. The acarbose-presenting surface plason resonance surfaces can be used as a glucoamylase sensor that allows rapid, label-free affinity screening of small carbohydrate-based inhibitors in solution
medicine
-
enzyme inhibitors are very effective in controlling blood glucose levels, and thus are lead candidates for the treatment of type 2 diabetes
biofuel production
the sake yeast strains constructed in this study are expected to produce bioethanol from starchy materials such as corn. Furthermore, to improve the efficiency of hydrolysis, a combination of sake yeast and various enzymes that cleave alpha-glucoside bonds shall be used
biofuel production
the sake yeast strains constructed in this study are expected to produce bioethanol from starchy materials such as corn. Furthermore, to improve the efficiency of hydrolysis, a combination of sake yeast and various enzymes that cleave alpha-glucoside bonds shall be used
biofuel production
-
the secreted glucoamylase from Paenibacillus amylolyticus strain NEO03 possesses properties suitable for saccharification processes such as biofuel production
biofuel production
-
the secreted glucoamylase from Paenibacillus amylolyticus strain NEO03 possesses properties suitable for saccharification processes such as biofuel production
-
biotechnology
-
immobilization of the enzyme on alginate beads for large-scale hydrolysis of starch in a fluidized bed of enzyme-alginate particles, method development, comparison to packed and batch mode, overview
biotechnology
-
improvement of the yeast enzyme for starch degradation in biotechnological applications by introduction of the starch binding domain from the glucoamylase of Aspergillus niger, chimeric enzyme in Saccharomyces cerevisiae strain Y428, overview
biotechnology
the enzyme is potentially useful in improvement of industrial starch processing by eliminating the need to adjust both pH and temperature
biotechnology
Thermochaetoides thermophila
-
the enzyme might be useful in biotechnological processes
biotechnology
-
enzyme immobilization on polyacrylamide gel results in an enzyme with increases thermostability for use in biocatalysis
biotechnology
-
the enzyme from commercial preparation is immobilized by sorption on a carbon support Sibunit, starch and dextrin hydrolysis kinetic parameters of glucoamylase, including the rate constant of thermal inactivation, show that immobilization of the enzyme results in a 1000fold increase in enzyme stability in comparison to the dissolved enzyme, presence of the dextrin substrate has a stabilizing effect, increase in dextrin concentration to 53% increases the thermostability of the immobilized enzyme, the immobilized-enzyme biocatalyst for starch saccharification has a high operational stability, half-inactivation time at 60°C exceeds 30 days
biotechnology
-
the enzyme immobilized on foamed glass covered with the catalytic filament carbon layer is highly active and stable, the effect of the carbon layer synthesized on the surface of aluminum oxide on the properties of biocatalysts shows that the glucoamylase adsorbed on the carbon-containing mesoporous ny-aluminum oxide exhibits a greater activity than the glucoamylase adsorbed on the macroporous alpha-aluminum oxide, kinetics, overview
energy production
-
the enzyme is useful in fuel ethanol production, enzyme properties and performance, overview
energy production
-
design of a bioanode that directly utilizes starch as a fuel in an enzymatic biofuel cell. The enzymatic fuel cell is based on three enzymes (alpha-amylase, glucoamylase and glucose oxidase). The carbon paste electrode containing these three enzymes and tetrathiafulvalene can both saccharize and oxidize starchy biomass. In cyclic voltammetry, catalytic currents are successfully observed with both glucose and starchy white rice used as a substrate. A membraneless white rice/O2 biofuel cell is assembled and the electrochemical performance is evaluated. The three-enzyme-based electrode is used as a bioanode and an immobilized bilirubin oxidase (derived from Myrothecium verrucaria) electrode is used as a biocathode. The biofuel cell deliveres an open circuit voltage of 0.522 V and power density of up to 0.099 mW/cm
food industry
-
key enzyme in ripening and production of good taste in fermented tofu production, overview
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
Schwanniomyces castellii
-
ethanol production, production of sugars
food industry
Thermochaetoides thermophila
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
Endomycopsis fibuligera
-
ethanol production, production of sugars
food industry
Cephalosporium eichhorniae
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
-
ethanol production, production of sugars
food industry
ethanol production, production of sugars
food industry
glucoamylase is an important group of enzymes in starch processing in the food industries, as it is used for the production of glucose and fructose syrup from liquefied starch
food industry
the enzyme performs highly efficient hydrolysis of raw starches and direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol suggesting that the enzyme has a number of potential applications in industrial starch processing and starch-based ethanol production. Effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase
food industry
-
glucoamylase is an important group of enzymes in starch processing in the food industries, as it is used for the production of glucose and fructose syrup from liquefied starch
-
food industry
-
the enzyme performs highly efficient hydrolysis of raw starches and direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol suggesting that the enzyme has a number of potential applications in industrial starch processing and starch-based ethanol production. Effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase
-
industry
-
immobilization of the enzyme on polyaniline polymer allows an improved catalytic performance and application of the enzyme in industrial processes
industry
-
Rhizopus enzymes are useful in industrial applications
industry
-
the enzyme can be useful in industrial processing and hydrolysis of starch
industry
Thermochaetoides thermophila
-
the enzyme is used in industrial starch degradation
industry
-
the enzyme is useful in industrial applications
industry
-
the enzyme is useful in industrial applications
industry
-
the enzyme is useful in industrial applications
industry
-
the enzyme is useful in industrial applications
industry
-
the enzyme is useful in industrial applications
industry
-
the enzyme is useful in industrial applications as glycoside hydrolase
industry
-
glucoamylase is used industrially to catalyze the hydrolysis of alpha-1,4-glycosidic bonds to release beta-D-glucose from the nonreducing ends of starch or oligosaccharides
industry
-
glucoamylases have been used with alpha-amylases for the industrial conversion of starch into glucose, intact cells of thermotolerant yeasts can be used as colloidal biocatalysts in starch degradation processes
industry
-
glucoamylases have been used with alpha-amylases for the industrial conversion of starch into glucose, intact cells of thermotolerant yeasts can be used as colloidal biocatalysts in starch degradation processes
industry
-
improvement in enzymatic desizing of starched cotton cloth using yeast codisplaying glucoamylase and cellulose-binding domain, overview
industry
an important industrial enzyme used in starch enzymatic saccharification
industry
glucoamylase from Aspergillus niger is an industrially important biocatalyst that is utilized in the mass production of glucose from raw starch or soluble oligosaccharides
industry
this glucoamylase may find important applications in the starch saccharification industry and in bioethanol production
industry
-
biotechnological applications of this glucoamylase from Aspergillus japonicus in the recycling and deinking process by the paper industries. Glucoamylases are used in food, pharmaceutical and textile industries
industry
-
biotechnological applications of this glucoamylase from Aspergillus japonicus in the recycling and deinking process by the paper industries. Glucoamylases are used in food, pharmaceutical and textile industries
-
industry
-
the enzyme is useful in industrial applications
-
industry
-
this glucoamylase may find important applications in the starch saccharification industry and in bioethanol production
-
nutrition
-
optimization of solid-state enzymatic hydrolysis of chestnut in food production using the Aspergillus niger glucoamylase in concert with an alpha-amylase, overview
nutrition
-
the enzyme of the M115 mutant strain is useful for enhanced ethanol production by Saccharomyces cerevisiae, strain ATTC26602, using raw starch as substrate in solid state fermentation
nutrition
-
feeding of maltase-glucoamylase null and wild-type mice with starch diets ad libitum and ad limitum. After ad libitum meals, null and wild-type mice have similar increases of blood glucose concentration. At low intakes, null mice have less fractional glucogenesis than wild-type mice. Null mice do not reduce fractional glucogenesis responses to ad libitum intakes demonstrating the dominant role of sucrose-isomaltase activity during full feeding
nutrition
-
tannins isolated from extracts of pomegranate, cranberry, grape, and cocoa inhibit the activity of glucoamylase and alpha-amylase in vitro. In general, larger and more complex tannins, such as those in pomegranate and cranberry, more effectively inhibit the enzymes than less polymerized cocoa tannins
paper production
-
biotechnological applications of this glucoamylase from Aspergillus japonicus in the recycling and deinking process by the paper industries
paper production
-
biotechnological applications of this glucoamylase from Aspergillus japonicus in the recycling and deinking process by the paper industries
-
synthesis
-
the immobilized enzyme with high operational stability can be used for continuous production of glucose from soluble dextrin
synthesis
-
production of glucose, which is a feed stock for high fructose syrup
synthesis
-
the enzyme of the M115 mutant strain is useful for enhanced ethanol production by Saccharomyces cerevisiae, strain ATTC26602, using raw starch as substrate in solid state fermentation
synthesis
-
entrapment of amyloglucosidase into dipalmitoylphosphatidylcholine multilamellar vesicles and large unilamellar vesicles for biocatalysis inside liposomes and bioanalytical applications, overview
synthesis
-
enzyme immobilization on polyacrylamide gel results in an enzyme with increases thermostability for use in biocatalysis
synthesis
-
glycosylation of the phenolic hydroxyl group of the phenyl propanoid systems, eugenol and curcumin, using an amyloglucosidase from Rhizopus sp. and a beta-glucosidase from sweet almonds together with carbohydrates D-glucose, D-mannose, maltose, sucrose,and D-mannitol in di-isopropyl ether produce glycosides at 7-52% yields in 72 h, method optimization, overview, two compounds are glycosylated in order to enhance their water solubility and pharmacological activities
synthesis
-
preparations of glucoamylase are widely used in many branches of industry for hydrolyzing starch-containing raw materials
synthesis
-
the enzyme is industrially an important biocatalyst that decomposes starch into glucose by tearing-off alpha-1,4-linked glucose residue from the non-reduced end of the polysaccharide chain
synthesis
-
enzyme may be used for raw corn starch hydrolysis and subsequent bioethanol production using Saccharomyces cerevisiae. The yield in terms of grams of ethanol produced per gram of sugar consumed is 0.365 g/g, with 71.6% of theoretical yield from raw corn starch