3.2.1.3: glucan 1,4-alpha-glucosidase
This is an abbreviated version!
For detailed information about glucan 1,4-alpha-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.3
-
3.2.1.3
-
aspergillus
-
niger
-
glycogen
-
alpha-amylase
-
maltose
-
corn
-
awamori
-
amylolytic
-
pompe
-
sucrase
-
myopathy
-
saccharification
-
rhizopus
-
lactase
-
brush
-
sucrase-isomaltase
-
acarbose
-
dextrin
-
glycogenosis
-
maltotriose
-
amylopectin
-
flour
-
amylases
-
starch-binding
-
isomaltase
-
infantile
-
maltodextrins
-
occidentalis
-
bran
-
disaccharidase
-
food industry
-
pullulanase
-
liquefaction
-
beta-cyclodextrins
-
debranching
-
beta-amylase
-
carbohydrases
-
3.2.1.20
-
cassava
-
maltooligosaccharides
-
trehalase
-
saccharify
-
bioethanol
-
medicine
-
industry
-
energy production
-
paper production
-
glucanotransferase
-
nutrition
-
maltoheptaose
-
analysis
-
maltotetraose
-
biotechnology
-
cgtase
-
biofuel production
-
isoamylase
-
liquefied
-
1-deoxynojirimycin
-
starchy
-
synthesis
- 3.2.1.3
- aspergillus
- niger
- glycogen
- alpha-amylase
- maltose
- corn
- awamori
-
amylolytic
- pompe
- sucrase
- myopathy
-
saccharification
- rhizopus
- lactase
-
brush
- sucrase-isomaltase
- acarbose
- dextrin
- glycogenosis
- maltotriose
- amylopectin
- flour
- amylases
-
starch-binding
- isomaltase
-
infantile
- maltodextrins
- occidentalis
- bran
- disaccharidase
- food industry
- pullulanase
-
liquefaction
- beta-cyclodextrins
-
debranching
- beta-amylase
-
carbohydrases
-
3.2.1.20
- cassava
- maltooligosaccharides
- trehalase
-
saccharify
-
bioethanol
- medicine
- industry
- energy production
- paper production
-
glucanotransferase
- nutrition
- maltoheptaose
- analysis
- maltotetraose
- biotechnology
- cgtase
- biofuel production
- isoamylase
-
liquefied
- 1-deoxynojirimycin
-
starchy
- synthesis
Reaction
Synonyms
1,4-alpha-D-glucan glucohydrolase, 1,4-alpha-D-glucan-glucohydrolase, acid maltase, alpha-(1,4)-D-glucan glucohydrolase, alpha-1,4-D-glucan glucohydrolase, alpha-1,4-glucan glucohydrolase, AMG, AmyA, AmyC, AmyD, amyloglucosidase, AnGA, APGA1, AtriGA15A, exo-1,4-alpha-D-glucan glucanohydrolase, exo-1,4-alpha-D-glucanohydrolase, exo-1,4-alpha-glucosidase, exo-amylase, GA, GA A, GA1, GA2, GAI, GAII, GAM, GAM-1, GAM-2, gamma-amylase, GAMP, GHF15 glucoamylase, GLA, Gla1, GlaA, GLL1, Glu-1.1, Glu-A, Glu1, GlucaM, Glucan 1,4-alpha-glucosidase, glucoamylase, glucoamylase 1, glucoamylase 2, glucoamylase C, glucoamylase D, glucoamylase G1, glucoamylase GA15A, glucoamylase P, glucose amylase, GluR, glycoamylase, HjGA, HrGA, lysosomal alpha-glucosidase, maltase glucoamylase, maltase-glucoamylase, maltooligosaccharide-metabolizing enzyme, Meiotic expression upregulated protein 17, MGA, MGAM, More, PDE_05527, PoGA, PoGA15A, PoxGA15A, raw starch-degrading enzyme, raw starch-degrading glucoamylase, RSDE, RSDG, SBD, Sga1, SSG, Sta1, Sta1p, starch-digesting glucoamylase, TagA, tGA, TmGLA, TmGlu1, TtcGA
ECTree
3.2.1.3 glucan 1,4-alpha-glucosidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-D-glucopyranoside + H2O
D-glucose + 4-nitrophenol
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + 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
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-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
-
-
?
guaiacol-alpha-D-glucoside + H2O
guaiacol + beta-D-glucose
-
the enzyme also performs glucosylation of guaiacol-alpha-D-glucoside in the reverse reaction
-
-
r
isomaltose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltodextrin + H2O
beta-glucose + ?
-
-
-
?
maltodextrin + H2O
maltodextrin + beta-D-glucose
-
during incubation 5-(hydroxymethyl)-2-furfuraldehyde is released, resulting in a glycated enzyme
-
-
?
maltoheptaose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltohexaose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltooligomers + H2O
? + beta-D-glucose
substrate specificity
-
-
r
maltopentadecaose + H2O
maltotetradecaose + beta-D-glucose
-
low activity
-
-
?
maltopentaose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltotetraose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
maltotriose + H2O
D-glucose + ?
-
assay at pH 5.0, 75°C, reaction stopped by boiling at 100°C for 3 min
-
-
?
pullulan + H2O
beta-D-glucose + ?
-
182% of activity with soluble starch
-
-
?
pullulan + H2O
pullulan + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
short-chain amylose + H2O
beta-D-glucose + short-chain amylose
-
-
-
-
?
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
-
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
Aspergillus japonicus Saito
-
-
-
-
?
alpha-cyclodextrin + H2O
glucose + ?
-
6% of the activity with maltose
-
-
?
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 + ?
-
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
-
-
?
amylopectin + H2O
D-glucose + ?
-
84% of the activity with starch
-
-
?
amylopectin + H2O
D-glucose + ?
-
-
beta-glucose
?
amylose + H2O
amylose + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
amylose + H2O
amylose + beta-D-glucose
preferred substrate
-
-
?
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
-
the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules
-
-
?
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
-
-
?
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
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 + ?
-
amylose A, n = 25 and amylose B, n = 130
-
?
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 + ?
-
-
beta-glucose
?
glycogen + H2O
glycogen + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
glycogen + H2O
glycogen + beta-D-glucose
87% of activity with amylose
-
-
?
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
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 + H2O
maltotetraose + beta-D-glucose
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
preferred substrate
-
-
?
maltopentaose + H2O
maltotetraose + beta-D-glucose
-
preferred substrate
-
-
?
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
-
substrate of isozyme GA-II, no activity with isozyme GA-I
-
-
?
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
14% of activity with amylose
-
-
?
maltose + H2O
beta-D-glucose + D-glucose
-
24% of activity with soluble starch from potato
-
-
?
maltose + 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
-
exoglycosidic hydrolysis of terminal glucose
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
preferred substrate
-
-
?
maltotetraose + H2O
maltotriose + beta-D-glucose
-
preferred substrate
-
-
?
maltotriose + H2O
maltose + beta-D-glucose
-
exoglycosidic hydrolysis of terminal 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
40% of activity with amylose
-
-
?
maltotriose + H2O
maltose + glucose
-
47% of the activity with starch
-
-
?
maltotriose + H2O
maltose + glucose
-
46% of the activity with starch
-
-
?
maltotriose + H2O
maltose + glucose
-
68% of the activity with starch
-
-
?
maltotriose + H2O
maltose + glucose
-
hydrolysis by a multi-chain mechanism
-
-
?
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
-
-
?
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
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
-
-
-
-
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
-
-
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
-
-
-
?
phenyl alpha-maltoside + H2O
glucose + phenyl alpha-glucoside
-
-
-
-
?
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
?
Aspergillus flavus NSH9
best substrate, soluble starch and gelatinized raw sago starch
-
-
?
starch + H2O
?
-
corn starch, potato starch, hydrolyzed potato starch, and rice starch
-
-
?
starch + H2O
?
Aspergillus japonicus Saito
-
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
?
Aspergillus tritici CGMCC 3.15694.3.2
standard assay substrate is soluble corn starch. Highest specific activity toward soluble wheat starch and lowest specific activity toward soluble potato starch
-
-
?
starch + H2O
?
Aspergillus tritici WZ99
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
?
-
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
?
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
?
Penicillium oxalicum CGMCC 3.15650
raw starch, different raw starch flours, e.g. raw cassava starch or raw potato starch, the enzyme also hydrolyzes soluble starch
-
-
?
starch + H2O
?
Penicillium oxalicum GXU20
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, and low activity with raw corn 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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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
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 + ?
-
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
beta-glucose and maltooligosaccharides
?
starch + H2O
glucose + ?
-
wheat starch, potato starch, corn starch
-
-
?
starch + H2O
glucose + ?
-
wheat starch, potato starch, corn starch
-
-
?
starch + H2O
glucose + ?
-
waxy-maize starch, waxy-sorghum starch, floridean starch. Incomplete conversion to glucose in absence of alpha-amylase
-
-
?
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 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
-
the enzyme is required for degradation of raw 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
-
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
-
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 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
-
-
product analysis
-
?
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
-
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
-
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
-
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
-
soluble starch, very low activity
-
-
?
starch + H2O
starch + beta-D-glucose
-
soluble starch, very low activity
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
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
?
-
-
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
?
-
Aspergillus flavus NSH9
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
-
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additional information
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modelling of potato starch saccharification by Aspergillus niger, influences of assay conditions on activity, overview
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additional information
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regulation mechanisms of enzyme expression, overview
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additional information
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different regulation mechanisms, the regulation is influenced by carbohydrate degradation and consumption under different culture conditions, overview
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additional information
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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
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additional information
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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
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additional information
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Aspergillus tritici CGMCC 3.15694.3.2
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
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additional information
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Aspergillus tritici WZ99
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
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additional information
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pullulan is a poor substrate, substrate specificity, overview
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additional information
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the enzyme has debranching activity
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additional information
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poor activity with pullulan and laminarin
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additional information
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poor activity with pullulan and laminarin
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additional information
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substrate specificity, overview
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additional information
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Corallococcus coralloides CCTCC M2012528
substrate specificity, overview
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additional information
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substrate specificity, overview
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additional information
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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
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additional information
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endophytic fungus EF6
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soluble starch is the best substrate, various raw starches, i.e. soluble starch, corn, tapioca, wheat, rice, sticky rice starch, are used as substrates
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additional information
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enzyme shows broad substrate specificity and raw starch hydrolyzing activity
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additional information
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key intestinal enzymes involved in the breakdown of glucose
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additional information
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the key intestinal enzyme involved in the breakdown of glucose oligosaccharides in the small intestine
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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no activity with cyclodextrins and laminarin
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additional information
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key enzyme in ripening and production of good taste in fermented tofu production, overview
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additional information
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substrate specificities of isozymes GA-I and GA-II, cyclodextrins are poor substrates, overview
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additional information
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no activity with sucrose, 4-nitrophenyl-beta-D-maltoside, methyl-beta-D-glucopyranoside, pullulan, alpha-cyclodextrin, beta-cyclodextrin, and trehalose
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additional information
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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
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additional information
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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
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additional information
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the enzyme shows a broad substrate specificity
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additional information
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Penicillium oxalicum GXU20
the enzyme shows a broad substrate specificity
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additional information
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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
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additional information
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the enzyme is responsible for much of the isomaltase and maltase activities in the intestine of the frog
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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bifunctional enzyme performing hydrolysis or transglycosylation depending on the substrate
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additional information
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bifunctional enzyme performing hydrolysis or transglycosylation depending on the substrate
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additional information
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no hydrolysis of alpha-1,6 linkages
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additional information
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no hydrolysis of alpha-1,6 linkages
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additional information
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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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additional information
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the enzyme binds poorly to insoluble starch
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additional information
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no hydrolysis of alpha-1,6 linkages
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additional information
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no substrate: 4-nitrophenyl alpha-D-glucopyranoside
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additional information
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no substrate: 4-nitrophenyl alpha-D-glucopyranoside
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additional information
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no activity with pullulan, dextran, and isomaltose
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additional information
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no activity with pullulan, dextran, and isomaltose
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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no hydrolysis of alpha-1,6 linkages
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additional information
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no hydrolysis of alpha-1,6 linkages
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additional information
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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
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additional information
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no substrate: 4-nitrophenyl alpha-D-glucopyranoside
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additional information
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no substrate: 4-nitrophenyl alpha-D-glucopyranoside
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additional information
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Thermothelomyces thermophilus DSM 1799
no substrate: 4-nitrophenyl alpha-D-glucopyranoside
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additional information
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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
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additional information
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Trichoderma reesei ATCC 56765
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
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additional information
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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
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additional information
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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
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additional information
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Tricholoma matsutake NBRC 30605
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
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