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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mechanism
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
multichain type mechanism
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
catalytic mechanism
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
catalytic mechanism
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion, the term beta relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
catalytic mechanism, reaction mechanism
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
active site structure, carbohydrate binding subsites, role of a conformational change of the inner loop in the catalytic mechanism, T342 is involved, overview
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
general acid-base catalytic reaction mechanism
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
Glu367 is important in catalysis, the plant enzyme shows a reaction mechanism different from the bacterial enzyme, overview
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
roles of Glu186 and Glu380 as general acid and general base catalyst in the catalytic reaction, reaction mechanism involving residue T342
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
roles of Glu186 and Glu380 as general acid and general base catalyst in the catalytic reaction, substrate binding and reaction mechanism
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion, the term beta relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
mode of action of the exo-amylase
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose
-
-
-
-
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4-nitrophenyl alpha-D-galactoside + H2O
4-nitrophenol + D-galactose
-
-
-
?
4-nitrophenyl alpha-maltopyranoside + H2O
4-nitrophenol + alpha-maltopyranose
-
-
-
?
4-nitrophenyl maltopentaose + H2O
4-nitrophenol + maltopentaose
-
-
-
?
4-nitrophenyl-maltoheptaoside + H2O
?
-
-
-
-
?
4-nitrophenyl-maltopentaoside + H2O
?
-
-
-
-
?
alpha-glucan + H2O
?
-
-
-
?
amylodextrin + H2O
?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
amylopectin + H2O
maltose + ?
amylopektin + H2O
?
-
-
-
?
amylose + H2O
beta-maltose
amylose + H2O
maltose
Sorghum sp.
-
from starch
-
-
?
amylose + H2O
maltose + ?
glycogen + H2O
beta-maltose
glycogen + H2O
maltose + ?
maltal + H2O
2-deoxymaltose
-
-
-
?
maltodextrin + H2O
maltose
-
maltodextrins with chain length from 9 to 198 glucose residues
and very small amounts of glucose and maltotriose
?
maltoheptaose + H2O
maltose + D-glucose + ?
the exo-type enzyme can catalyze the successive liberation of beta-maltose from the nonreducing ends of alpha-1,4-linked glucopyranosyl polymers. A phenomenon called multiple or repetitive attack is observed where the enzyme releases several maltose molecules in a single enzyme-substrate complex. The multiple attack action needs the force of enzyme sliding on the substrate. In addition, it is important for the multiple attack that the enzyme and substrate have the characteristics of a stable productive substrate-enzyme complex through a hydrogen bond between the nonreducing end of the substrate and the carboxyl residue of the enzyme
-
-
?
maltooligosaccharide + H2O
?
-
beta-amylase hydrolyzes maltooligosaccharides more readily as their degree of polymerization increases, this being strongest for maltooligosaccharides larger than 13 glucose residues and very weakly for maltotriose, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
maltopentaose + H2O
2 maltose + D-glucose
maltose + H2O
?
the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan
-
-
?
maltotetraose + H2O
2 maltose
maltotriose + H2O
?
-
very poor substrate
-
-
?
maltotriose + H2O
maltose + D-glucose
p-nitrophenyl alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
p-nitrophenylmaltopentaoside + H2O
p-nitrophenol + maltopentaose
catalyzes the release of p-nitrophenol, specific substrate
-
-
?
pullulan + H2O
?
-
-
-
-
?
soluble starch + H2O
maltose + ?
starch + H2O
beta-maltose
starch + H2O
beta-maltose + ?
-
-
-
-
?
additional information
?
-
amylopectin + H2O
?
from potato, active site structure, Glu-186 and Glu-380 play important roles as general acid and base catalyst
-
-
?
amylopectin + H2O
?
-
114.6% of the activity with amylose, soluble starch, amylose and amylopectin are the most suitable substrates, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
amylopectin + H2O
?
-
88% of the activity with starch
-
-
?
amylopectin + H2O
?
-
88% of the activity with starch
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
and limit dextrin
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin + H2O
maltose + ?
from potato
-
-
?
amylopectin + H2O
maltose + ?
catalyzes the release of maltose residues, amylopectin and starch are better substrates than amylose
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin + H2O
maltose + ?
from potato
-
-
?
amylopectin + H2O
maltose + ?
-
from potato
-
-
?
amylopectin + H2O
maltose + ?
Sorghum sp.
-
from starch, preferred substrate
-
-
?
amylopectin + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
amylopectin + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
amylose + H2O
?
DPn is 16
-
-
?
amylose + H2O
?
-
EX-I, soluble starch, amylose and amylopectin are the most suitable substrates, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
amylose + H2O
?
-
79% of the activity with starch
-
-
?
amylose + H2O
?
-
79% of the activity with starch
-
-
?
amylose + H2O
beta-maltose
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
DP = 17
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
partly oxidized amylose
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
maltose + ?
catalyzes the release of maltose residues, less good substrate than starch and amylopectin
-
-
?
amylose + H2O
maltose + ?
-
-
-
-
?
dextrin + H2O
?
-
-
-
-
?
dextrin + H2O
?
-
13% of the activity with starch
-
-
?
dextrin + H2O
?
-
13% of the activity with starch
-
-
?
glycogen + H2O
?
-
49.4% of the activity with amylose
-
-
?
glycogen + H2O
?
the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan
-
-
?
glycogen + H2O
beta-maltose
-
-
-
?
glycogen + H2O
beta-maltose
-
-
-
-
?
glycogen + H2O
beta-maltose
-
-
and limit dextrin
?
glycogen + H2O
beta-maltose
-
from oyster
-
-
?
glycogen + H2O
beta-maltose
-
-
-
-
?
glycogen + H2O
beta-maltose
-
type III and type VIII
-
-
?
glycogen + H2O
beta-maltose
-
-
-
-
?
glycogen + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
glycogen + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
34.6% of the activity with amylose
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
23.3% of the activity with amylose
-
-
?
maltopentaose + H2O
2 maltose + D-glucose
substrate/product binding structure, sugar subsite conformations, overview
-
-
?
maltopentaose + H2O
2 maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltopentaose + H2O
2 maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
beta-amylase is an exo-enzyme that catalyzes the hydrolysis of the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, Glu-172 and Glu-367 are catalytic residues, binding mode of substrate, substrate recognition mechanism, enzyme structure
-
-
?
maltopentaose + H2O
?
-
beta-amylase is an inverting enzyme that hydrolyzes the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, catalytic mechanism, Glu-172 acts as general acid, Glu-367 acts as general base
-
-
?
maltopentaose + H2O
?
binding mode of substrate in the active site
-
-
?
maltopentaose + H2O
?
hydrolyzes the alpha-1,4-glucosidic linkage liberating beta-maltose from the non-reducing end of substrate, good substrate, mode of binding in the active site, catalytic mechanism, enzyme/domain structure
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
13.8% of the activity with amylose
-
-
?
maltopentose + H2O
?
-
40% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
maltopentose + H2O
?
-
40% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
maltotetraose + H2O
2 maltose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltotetraose + H2O
2 maltose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
7.6% of the activity with amylose
-
-
?
maltotetraose + H2O
?
-
37% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
maltotetraose + H2O
?
-
37% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
maltotriose + H2O
maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltotriose + H2O
maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
-
-
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
-
catalyzes the release of maltose
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
catalyzes the release of maltose
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
starch granules from various sources
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
soluble starch + H2O
maltose + ?
maximum activity with 1.2 % soluble starch. Less activity is observed with starch from corn, rice, glycogen
-
-
?
starch + H2O
?
in vitro breakdown of semicrystalline starch particles by beta-amylases increases significantly if they act together with glucan, water dikinase
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran, the enzyme from strain MNU82 utilizes raw and cooked starch
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
beta-amylase hydrolyzes alpha-1,4-linkage, raw starch granules from potato, wheat, rice and corn, with the granules from rice being the best substrate, beta-amylase attacks very slowly on the starch granules, hydrolyzes corn granules efficiently at 45°C
-
-
?
starch + H2O
?
beta-amylase is an exo-enzyme that catalyzes the hydrolysis of the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, Glu-172 and Glu-367 are catalytic residues, substrate recognition mechanism, enzyme structure
-
-
?
starch + H2O
?
-
beta-amylase is an inverting enzyme that hydrolyzes the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, catalytic mechanism, Glu-172 acts as general acid, Glu-367 acts as general base
-
-
?
starch + H2O
?
catalyzes the hydrolysis of alpha-1,4-glucosidic linkages of soluble starch, and liberates beta-anomeric maltose from the nonreducing ends, exo-acting enzyme, composed of two functional domains, a catalytic domain: domains A and B, and starch-binding domain: domain C, beta-amylase has three carbohydrate-binding sites aside from the active site: two in domain B named Site2 and Site3, one in domain C named Site1, roles of these sites in the catalytic reaction and raw starch-binding, beta-amylase hardly hydrolyzes raw starch from wheat, corn, potato or sweet potato, but binds to it strongly
-
-
?
starch + H2O
?
hydrolyzes the alpha-1,4-glucosidic linkage liberating beta-maltose from the non-reducing end of substrate, enzyme/domain structure, starch binding site in domain C, catalytic mechanism
-
-
?
starch + H2O
?
potato starch or Hylon VII
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
beta-amylase is an exo-amylase acting on starch with the successive removal of maltose molecules from the non-reducing ends of the glucose polymers with inversion of the anomeric configuration
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
active site structure, Glu-186 and Glu-380 play important roles as general acid and base catalyst, catalyzes the liberation of beta-anomeric maltose from the non-reducing ends
-
-
?
starch + H2O
?
-
beta-amylase hydrolyzes alpha-1,4-linkage, raw starch granules from potato, wheat, rice and corn, with the granules from rice being the best substrate, no efficient hydrolysis of raw starch granules, very slow enzymic attack
-
-
?
starch + H2O
?
-
catalyzes the release of maltose from soluble starch, three-dimensional structures of Sd2L and V233A mutant of Sd1
-
-
?
starch + H2O
?
from potato, catalyzes the release of maltose from the non-reducing ends of starch, three-dimensional structure of Sd2L
-
-
?
starch + H2O
?
soluble starch
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
beta-amylase should be a key enzyme in starch degradation during the germination of millet seeds, enzyme activity increases during days 1-4 of germination
-
-
?
starch + H2O
?
-
106.9% of the activity with amylose, soluble starch, amylose and amylopectin are the most suitable substrates, some activity against native starch, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
starch + H2O
?
-
highest activity, exo-acting enzyme, no production of glucose
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
highest activity, exo-acting enzyme, no production of glucose
-
-
?
starch + H2O
?
the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
beta-maltose
-
-
-
-
?
starch + H2O
beta-maltose
-
-
-
-
?
starch + H2O
beta-maltose
-
-
-
?
starch + H2O
beta-maltose
-
beta-amylase is involved in starch degradation during mango ripening, which is clearly triggered by detachment from the mother-plant
-
-
?
starch + H2O
beta-maltose
-
best substrate, pure and low quality starches, maize starch, tapioca starch
maltose is the major end product, traces of maltooligosaccharides, no glucose as product
-
?
starch + H2O
beta-maltose
-
best substrate, pure and low quality starches, maize starch, tapioca starch
maltose is the major end product, traces of maltooligosaccharides, no glucose as product
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
soluble starch
-
-
?
starch + H2O
maltose + ?
enzyme induction upon a cold shock at 4°C leads to starch-dependent maltose accumulation, which might be required for protection of the photosynthetic electron transport chain and sensitization of PSII during freezing, maltose influences the carbohydrate metabolism, overview
-
-
?
starch + H2O
maltose + ?
-
role of beta-amylase in starch breakdown during temperature stress, product maltose acts as a cryoprotectant and precursor of soluble sugar metabolism, overview
-
-
?
starch + H2O
maltose + ?
the isozyme is involved in leaf starch degradation
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
soluble
-
-
?
starch + H2O
maltose + ?
catalyzes the release of maltose residues, starch and amylopectin are better substrates than amylose
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
millet starch, gelatinization temperature is 61.1-68.7°C
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
in roots during storage, the starch hydrolysis at low temperatures is required for improvement of gustative quality of roots from tuberous-rooted chervil, at higher storage temperature the alpha-amylase activity is increased
-
-
?
starch + H2O
maltose + ?
-
soluble
-
-
?
starch + H2O
maltose + ?
-
raw starch from wheat, corn, potato and rice
-
-
?
starch + H2O
maltose + ?
Dioscorea batatus
-
soluble
beta-maltose
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
soluble
-
?
starch + H2O
maltose + ?
-
soluble
-
?
starch + H2O
maltose + ?
-
soluble
-
-
?
starch + H2O
maltose + ?
-
-
main product
-
?
starch + H2O
maltose + ?
-
-
main product
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
soluble
-
?
starch + H2O
maltose + ?
-
soluble
-
-
?
starch + H2O
maltose + ?
-
soluble
beta-maltose
?
starch + H2O
maltose + ?
-
soluble starch, depolymerization, reaction scheme
-
-
?
starch + H2O
maltose + ?
-
waxy from maize
-
-
?
starch + H2O
maltose + ?
-
soluble
-
?
starch + H2O
maltose + ?
-
soluble
-
-
?
starch + H2O
maltose + ?
-
soluble
-
-
?
starch + H2O
maltose + ?
-
soluble
beta-maltose
?
starch + H2O
maltose + ?
-
soluble
-
-
?
starch + H2O
maltose + ?
-
potato starch
-
?
starch + H2O
maltose + ?
-
-
beta-maltose
?
starch + H2O
maltose + ?
-
soluble
-
-
?
starch + H2O
maltose + ?
-
raw starch from corn and potato
-
-
?
starch + H2O
maltose + ?
-
degradation of starch granules by the enzyme alone occurs at the equatorial grooves of lecticular granules
-
-
?
starch + H2O
maltose + ?
-
soluble
-
-
?
starch + H2O
maltose + ?
-
raw starch from corn and potato
-
-
?
starch + H2O
maltose + ?
-
degradation of starch granules by the enzyme alone occurs at the equatorial grooves of lecticular granules
-
-
?
starch + H2O
maltose + ?
-
-
beta-maltose
?
starch + H2O
maltose + ?
-
grains
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
soluble
beta-maltose
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
potato starch
-
?
starch + H2O
maltose + ?
Sorghum sp.
-
-
-
-
?
starch + H2O
maltose + ?
Sorghum sp.
-
Sorghum starch, gelatinization temperature is 70-75°C
-
-
?
starch + H2O
maltose + ?
-
boiled
-
-
?
starch + H2O
maltose + ?
-
soluble
-
-
?
starch + H2O
maltose + ?
-
gelatinized starch
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
soluble starch
-
-
?
starch + H2O
maltose + ?
-
soluble
-
-
?
additional information
?
-
-
plants mechanism of cold adaptation, enzyme regulation by phytohormones, light, and by abiotic stess, e.g. by osmotic, cold, salt, and drought stress, the enzyme is also regulated by the circadian clock, detailed overview
-
-
?
additional information
?
-
the isozyme TR-BAMY is redox- and thioredoxin-regulated involving residues C470 and C32 forming a disulfide bridge, the precursor enzyme conatining the transit pepetide is inactive
-
-
?
additional information
?
-
the isozyme TR-BAMY is redox- and thioredoxin-regulated involving residues C470 and C32 forming a disulfide bridge, the precursor enzyme conatining the transit pepetide is inactive
-
-
?
additional information
?
-
no hydrolysis of alpha-1,6-glucosidic linkages
-
-
?
additional information
?
-
-
no hydrolysis of alpha-1,6-glucosidic linkages
-
-
?
additional information
?
-
beta-amylase does not catalyze a transglycosylation reaction
-
-
?
additional information
?
-
-
beta-amylase does not catalyze a transglycosylation reaction
-
-
?
additional information
?
-
analysis of effect of hydroxypropylation and beta-amylase treatment on complexation of debranched starch with naringenin using potato starch and Hylon VII. An increase in hydroxypropylation level improves recovery of soluble complexes, while total recovery remains unchanged. The beta-amylase treatment further increases soluble complex recovery. For the same treatment, the naringenin content is greater in Hylon VII complexes than in potato starch complexes
-
-
?
additional information
?
-
rhizome beta-amylase is a cytoplasmic vegetative storage protein
-
-
?
additional information
?
-
-
rhizome beta-amylase is a cytoplasmic vegetative storage protein
-
-
?
additional information
?
-
beta-amylase exclusively catalyzes the release of beta-maltose from the non-reducing ends of alpha-1,4-linked oligo- and polyglucans, three-dimensional structure
-
-
?
additional information
?
-
-
beta-amylase exclusively catalyzes the release of beta-maltose from the non-reducing ends of alpha-1,4-linked oligo- and polyglucans, three-dimensional structure
-
-
?
additional information
?
-
Dioscorea batatus
-
no activity with cyclodextrins
-
-
?
additional information
?
-
-
no activity with pullulan
-
-
?
additional information
?
-
-
soybean trypsin inhibitor and beta-amylase induce rat alveolar macrophages to release nitrogen oxides
-
-
?
additional information
?
-
-
maltose is the main product of soluble starch hydrolysis
-
-
?
additional information
?
-
-
maltose is the main product of soluble starch hydrolysis
-
-
?
additional information
?
-
-
germination markedly increases the beta-amylase
-
-
?
additional information
?
-
-
starch gelatinization assay, overview
-
-
?
additional information
?
-
-
beta-amylase is an exo-enzyme that specifically binds to a double (1-4-alpha-D-glucopyranosyl-1-4-alpha-D-glucopyranosyl-) unit from the non-reducing ends of polymaltosidic polysaccharides, and sequentially cleaves glucose disaccharidic units until it encounters any structural variation, producing maltose as sole hydrolysis product
-
-
?
additional information
?
-
-
no hydrolysis of beta-limit dextrin
-
-
?
additional information
?
-
-
no activity with pullulan
-
-
?
additional information
?
-
-
no hydrolysis of beta-limit dextrin
-
-
?
additional information
?
-
-
no activity with maltotriose and cycloheptaose
-
-
?
additional information
?
-
-
cysteine, tryptophan and serine are essential amino acids for catalysis, not: maltotriose
-
-
?
additional information
?
-
-
cysteine, tryptophan and serine are essential amino acids for catalysis, not: maltotriose
-
-
?
additional information
?
-
-
moderately branched glucans are better substrates than less branched or non-branched or highly branched glucans
-
-
?
additional information
?
-
-
no hydrolysis of beta-limit dextrin
-
-
?
additional information
?
-
-
not: xylan, pullulan, cellulose, carboxymethyl cellulose
-
-
?
additional information
?
-
-
not: xylan, pullulan, cellulose, carboxymethyl cellulose
-
-
?
additional information
?
-
the enzyme does not hydrolyze starch, glycogen, pullulan or large maltooligosaccharides
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze starch, glycogen, pullulan or large maltooligosaccharides
-
-
?
additional information
?
-
-
germination markedly increases the beta-amylase
-
-
?
additional information
?
-
-
no activity with pullulan
-
-
?
additional information
?
-
-
-
-
-
?
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2,3-epoxypropyl-alpha-D-glucopyranoside
affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172, inactivation mechanism
2-mercaptoethanol
4%, 1h, activity is decreased to 53%
3,4-epoxybutyl-alpha-D-glucopyranoside
affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172
4-chloromercuribenzoate
-
inactivation, the enzyme can be reactivated by L-cysteine
5,5'-dithiobis-(2-nitrobenzoic acid)
-
chemical modification of the exposed sulfhydryl groups in beta-amylase from unmalted seeds with 5,5'-dithiobis-(2-nitrobenzoic acid) results in loss of activity. In the beta-amylase from malted seed the 5,5'-dithiobis-(2-nitrobenzoic acid) chemical modification results in the increase in the KM from 2.81 to 4.14 mg/ml
5,5'-dithiobis-2-nitrobenzoate
-
weak
acetic acid
-
75% inhibition at 10 mM, 16.3% inhibition at 1 mM
acetone
40%, relative activity is decreased to 87%
AgNO3
-
1 mM, 94% inhibition
Al2(SO4)3
-
1 mM, 57% inhibition
alpha-cyclohexaamylose
-
-
Bi(NO3)3
-
1 mM, 54% inhibition
Ca2+
-
binds at the active site
Citric acid
-
complete inhibition at 5-10 mM, 84.7% inhibition at 1 mM
Co2+
1 mM, 37% loss of activity
CuCl2
-
1 mM, 93% inhibition
CuSO4
-
over 94% inhibition at 1-10 mM
D-mannose
125 mM, 6% inhibition, p-nitrophenylmaltopentaoside hydrolysis
diethyl dicarbonate
-
complete inhibition
Isopropanol
40%, relative activity is decreased to 80%
K+
1 mM, 1% loss of activity
Lactic acid
-
complete inhibition at 10 mM, 58.3% inhibition at 1 mM
maltitol
behaves as a mixed-type or competitive inhibitor depending on the chain length of the substrate, inhibition mechanism, binds to Site2 in domain B and forms an abortive ESI complex when amylose is used as substrate
n-butanol
40%, relative activity is decreased to 85%
O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)D-xylopyranose
mode of binding in the active site cleft
O-alpha-D-xylopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranoside
mixed-type inhibition, two molecules bind to enzyme
p-chloromercuriphenyl sulfonic acid
-
-
p-hydroxymercuribenzoate
-
0.5 mM, 96% inhibition
p-methylsulfonylfluoride
-
3 mM, 100% inhibition
Phenylarsine oxide
-
complete inhibition
Phenylglyoxal
-
3 mM, 27% inhibition
potassium ferricyanide
-
oxidation of the sulfhydryl groups of the enzyme from malted seed in presence of urea results in formation of a dimeric enzyme. The oxidative dimerization leads to inactivation of the enzyme
salicylic acid
-
complete inhibition at 10 mM, 61.4% inhibition at 1 mM
Schardinger maltodextrins
-
partial
-
SDS
4%, 1 h, complete loss of activity
sodium deoxycholate
-
0.001%, 15% inhibition
Sodium dodecyl sulfate
-
0.001%, 57% inhibition
starch
-
at high concentration s
Tannic acid
-
complete inhibition at 10 mM, 81.8% inhibition at 1 mM
Tween 40
-
0.001%, 15% inhibition
Tween 80
4%, 1h, activity is decreased to 61%
Ag+
-
-
Ag+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Ag+
-
1 mM, almost complete inhibition of recombinant enzyme
alpha-cyclodextrin
-
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-cyclodextrin
-
-
Cd2+
-
-
Cd2+
-
1 mM, almost complete inhibition of barley enzyme and recombinant enzyme, less inhibitory towards mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Cd2+
-
1 mM, almost complete inhibition of recombinant enzyme
Cu2+
-
-
Cu2+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Cu2+
-
1 mM, almost complete inhibition of recombinant enzyme
Cu2+
-
1 mM CuSO4, 50% inhibition
Cu2+
-
5 mM, 37°C, 30 min, about 80% inhibition
cyclohexaamylose
alpha-CD, competitive inhibitor
cyclohexaamylose
iodine staining method, competitive inhibition
D-glucose
mode of binding in the active site cleft
D-glucose
p-nitrophenylmaltopentaoside hydrolysis: 125 mM, 87.5% inhibition, iodine staining method: mixed-type, weak inhibition compared with maltose and cyclohexaamylose
D-maltose
mode of binding in the active site cleft
EDTA
-
-
EDTA
-
non-competitive, Ca2+ fully restores activity
EDTA
1 mM, 42% loss of activity. 5-10 mM, complete loss of activity
Fe2+
-
-
Fe3+
-
-
FeCl3
-
complete inhibition at 1-10 mM
FeCl3
-
1 mM, 16% inhibition
Hg2+
-
HgCl2
Hg2+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Hg2+
-
1 mM, almost complete inhibition of recombinant enzyme
Hg2+
-
0.001-0.1 mM HgCl2
Hg2+
-
5 mM, 37°C, 30 min, about 80% inhibition
HgCl2
-
10 mM, 100% inhibition
HgCl2
-
1 mM, 93% inhibition
iodoacetamide
-
-
iodoacetic acid
-
-
iodoacetic acid
-
partial
maltose
p-nitrophenylmaltopentaoside hydrolysis: 125 mM, 87.5% inhibition, iodine staining method: competitive inhibition
maltose
-
inhibits light amylase
Mg2+
-
mild inhibitor
Mg2+
-
binds at the active site
Mg2+
1 mM, 14% loss of activity
Mn2+
-
mild inhibitor
Mn2+
-
5 mM, 37°C, 30 min, about 80% inhibition
N-bromosuccinimide
-
0.4 mM
N-bromosuccinimide
-
1 mM, 84% inhibition
N-ethylmaleimide
-
10 mM, 73% inhibition
N-ethylmaleimide
-
remarkably reduces activity
NEM
-
partial
Ni2+
-
-
Ni2+
1 mM, 28% loss of activity
p-chloromercuribenzoate
-
0.01 mM, 100% inhibition
p-chloromercuribenzoate
-
1 mM, 97% inhibition, exogenous thiols like dithiothreitol, 2-mercaptoethanol or cysteine HCl reactivate
PCMB
-
cysteine reactivates
PCMB
-
restored by mercaptoethanol or dithiothreitol
PCMB
-
0.1 mM, complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
PCMB
-
0.1 mM, complete inhibition of recombinant enzyme
PCMB
-
0.001-0.1 mM, inactivation is partly reversed by adding 10fold to 20fold excess of glutathione or 1,2-dithiopropanol
PCMB
-
cysteine reactivates
PCMB
-
0.5 mM, 75% loss of activity after 30 min at 22°C, cysteine reactivates
Tween 20
-
0.001%, 16% inhibition
Tween 20
4%, 1h, activity is decreased to 71%
Zn2+
-
mild inhibitor
Zn2+
-
1 mM, almost complete inhibition of barley enzyme and recombinant enzyme, less inhibitory towards mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Zn2+
-
1 mM, almost complete inhibition of recombinant enzyme
Zn2+
-
binds at the active site
ZnSO4
-
15% inhibition at 10 mM, no inhibition at 1 mM
ZnSO4
-
1 mM, 54% inhibition
additional information
the 41 amino acid transit peptide inhibits isozyme TR-BAMY
-
additional information
the 41 amino acid transit peptide inhibits isozyme TR-BAMY
-
additional information
-
no or poor effect by boric acid and urea at 1-10 mM
-
additional information
not inhibited by 250 mM lactose
-
additional information
-
not inhibited by 250 mM lactose
-
additional information
-
PMSF and 2-mercaptoethanol have no significant effect on the amylase activity
-
additional information
-
the synthesis of beta-amylase is repressed by glucose, fructose or sucrose as carbon source, not inhibited by EDTA
-
additional information
-
no inhibition by 4-chloromercuribenzoate, heavy metal ions, nor Schardinger dextrins
-
additional information
no considerable effect of organic solvents (ethanol, methanol, isopropanol, acetone and n-butanol) is observed on enzyme activity
-
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0.0827
4-nitrophenyl alpha-maltopyranoside
pH 7.0, 90°C
0.13 - 0.17
amylodextrin
-
chain lengths geater than 50
-
1.02 - 16.2
maltopentaose
4.17 - 18.2
maltotetraose
4.25
maltotriose
pH 5.0, 85°C
0.73
p-nitrophenylmaltopentaoside
-
-
additional information
additional information
-
0.26
amylopectin
pH 5.4, 37°C, recombinant mutant T342A
0.39
amylopectin
pH 5.4, 37°C, recombinant mutant T342S
0.47
amylopectin
37°C, recombinant mutant T47M/Y164E/T328N
0.73
amylopectin
37°C, recombinant wild-type enzyme
0.92
amylopectin
37°C, recombinant mutant Y164F
1.22
amylopectin
37°C, recombinant mutant Y164Q
1.24
amylopectin
37°C, recombinant mutant Y164E
1.84
amylopectin
pH 5.4, 37°C, recombinant mutant T342V
1.94
amylopectin
pH 5.4, 37°C, recombinant wild-type enzyme
2.63
amylopectin
37°C, recombinant mutant Y164H
0.491
amylose
-
DP = 17, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
0.6
amylose
pH 7, 25°C, DPn: 16, S235A/Y249A/W449F/W495F quadruple mutant
0.61
amylose
pH 7, 25°C, DPn: 16, W449F/W495F double mutant
0.65
amylose
pH 7, 25°C, DPn: 16, S235A/Y249A double mutant
0.7
amylose
pH 7, 25°C, DPn: 16, S235A mutant
0.71
amylose
pH 7, 25°C, DPn: 16, Y249A mutant
0.72
amylose
pH 7, 25°C, DPn: 16, wild-type enzyme
0.16
maltodextrin
-
with 50 glucose equivalents per chain
0.17
maltodextrin
-
with 98 glucose equivalents per chain
0.36
maltodextrin
-
with 31 glucose equivalents per chain
0.67
maltodextrin
-
with 16 glucose equivalents per chain
1.3
maltodextrin
-
with 9 glucose equivalents per chain
0.9
maltoheptaose
-
-
1.83
maltoheptaose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
0.89
maltohexaose
-
-
2
maltohexaose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
1.02
maltopentaose
-
-
1.94
maltopentaose
pH 5.4, 37°C, wild-type enzyme
2.02
maltopentaose
pH 5.4, 37°C, mutant E380Q
2.15
maltopentaose
pH 5.4, 37°C, mutant E186Q
2.83
maltopentaose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
16.2
maltopentaose
pH 5.0, 85°C
4.17
maltotetraose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
18.2
maltotetraose
pH 5.0, 85°C
0.00317
starch
-
pH 5, 40°C, soluble starch, V233A mutant of Sd1
0.0033
starch
-
pH 5, 40°C, soluble starch, wild-type Sd1
0.0036
starch
-
pH 5, 40°C, soluble starch, R115C mutant of Sd2L
0.00825
starch
-
pH 5, 40°C, soluble starch, V233A mutant of Sd2L
0.0083
starch
-
pH 5, 40°C, soluble starch, wild-type Sd2H and V233A/L347S double mutant of Sd2L
0.00831
starch
-
pH 5, 40°C, soluble starch, wild-type Sd2L
0.00834
starch
-
pH 5, 40°C, soluble starch, L347S mutant of Sd2L
0.00838
starch
-
pH 5, 40°C, soluble starch, V430A mutant of Sd2L
0.00856
starch
-
pH 5, 40°C, soluble starch, D165E mutant of Sd2L
5.64
starch
immobilized enzyme, pH 7.0, 40°C
7.49
starch
free enzyme, pH 7.0, 40°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
-
kinetics
-
additional information
additional information
-
Km: 1.25 mg/ml for starch
-
additional information
additional information
-
Km: 3 mg/ml for soluble starch
-
additional information
additional information
-
the Km-value for linear maltodextrins decreases with chain-lengths up to about 50 glucose units and with longer chain lengths it remains constant at about 0.14 mM
-
additional information
additional information
-
Km for soluble starch is 0.4%
-
additional information
additional information
-
5.9 mg/ml for soluble starch, light amylase. 6.8 mg/ml for soluble starch for soluble starch, heavy amylase
-
additional information
additional information
-
Km with amylase is 0.24%
-
additional information
additional information
-
Km: 2.25 mg/ml for amylopectin for isoenzyme 2, Km: 1.65 mg/ml for amylopectin, isoenzyme 6
-
additional information
additional information
-
Km: 2.29 mg/ml for soluble starch at 60°C, 1.68 mg/ml for soluble starch at 75°C
-
additional information
additional information
-
Km: 1.67 mg/ml for soluble starch
-
additional information
additional information
beta-amylase from germinated barley has a higher substrate binding affinity for starch than enzyme from mature grain, removal of the four C-terminal glycine-rich repeats enhances the substrate binding affinity, kinetic parameters for several deletion mutants
-
additional information
additional information
-
beta-amylase from germinated barley has a higher substrate binding affinity for starch than enzyme from mature grain, removal of the four C-terminal glycine-rich repeats enhances the substrate binding affinity, kinetic parameters for several deletion mutants
-
additional information
additional information
binding parameters of wild-type and mutant enzymes to raw corn starch
-
additional information
additional information
-
binding parameters of wild-type and mutant enzymes to raw corn starch
-
additional information
additional information
kinetic parameters for wild-type and mutant SBA
-
additional information
additional information
-
kinetic parameters for wild-type and mutant SBA
-
additional information
additional information
-
Km for starch is 4.34 mg/ml at 60°C
-
additional information
additional information
-
the 3 allelic forms of beta-amylase Sd1, Sd2H and Sd2L exhibit different kinetic properties, an R115C mutation is responsible for this difference
-
additional information
additional information
-
kinetics, isothermal titration microcalorimetric method
-
additional information
additional information
kinetics, recombinant wild-type andmutant enzymes
-
additional information
additional information
-
kinetics, recombinant wild-type andmutant enzymes
-
additional information
additional information
-
13.6 mg/l, starch as substrate
-
additional information
additional information
-
Km and Vmax values are 79.37mg/ml and 5.13 U/ml, respectively, at 50°C, pH 6.0, Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics and Lineweaver-Burk plots, Km and Vmax values at 50°C are estimated to be 2.81 mg/ml and 10.62 U/min, respectively
-
additional information
additional information
Michaelis-Menten kinetics, modelling
-
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shoot tip of the bud
brenda
-
-
brenda
isozyme TR-BAMY
brenda
germinated barley, of Sd1 and Sd2L barley varieties
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
tissue culture
brenda
isozyme TR-BAMY
brenda
-
-
brenda
resting, localized in the cortex and the pith of rhizomes, but not in vascular tissues, pericycle, endodermis and rhizodermis
brenda
-
-
brenda
-
-
brenda
-
beta-amylase activity is uniformly shared by endosperm and bran
brenda
-
beta-amylase activity is uniformly shared by endosperm and bran
brenda
-
beta-amylase activity is uniformly shared by endosperm and bran
brenda
mature, of Sd1 and Sd2L barley varieties
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
BMY is stored in seeds bound to starchy endosperm possibly through S-S bridges, during germination the enzyme is released by proteolytic cleavage resulting in a smaller enzyme form
brenda
-
endosperm-specific isozyme beta-amylase1, Bmy1
brenda
-
-
brenda
-
beta-amylase activity is uniformly shared by endosperm and bran
brenda
-
beta-amylase activity is uniformly shared by endosperm and bran
brenda
-
beta-amylase activity is uniformly shared by endosperm and bran
brenda
-
-
brenda
banana beta-amylase activity is highly correlated to a decrease in starch, being primary up-regulated by de novo synthesis
brenda
-
-
brenda
-
brenda
isozyme TR-BAMY
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
beta-amylase activity is uniformly shared by endosperm and bran
brenda
-
beta-amylase activity is uniformly shared by endosperm and bran
brenda
-
beta-amylase activity is uniformly shared by endosperm and bran
brenda
-
-
brenda
isozyme TR-BAMY
brenda
-
-
brenda
-
tap root
brenda
isozyme TR-BAMY
brenda
-
the enzyme activity increases progressively during seed germination
brenda
-
malted and unmalted
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
BMY is stored in seeds bound to starchy endosperm possibly through S-S bridges, during germination the enzyme is released by proteolytic cleavage resulting in a smaller enzyme form
brenda
-
distribution of thermostable alleles/isozymes in worldwide seed collections, detailed overview
brenda
-
distribution of thermostable alleles/isozymes in worldwide seed collections, detailed overview
brenda
-
-
brenda
-
-
brenda
-
-
brenda
germinating
brenda
-
endosperm
brenda
-
germinating
brenda
Sorghum sp.
-
germinating, different activities during germination in the different Sorghum sp. varieties, overview
brenda
Sorghum sp.
-
the enzyme activity increases progressively during seed germination
brenda
-
-
brenda
-
malted
brenda
-
brenda
very low enzyme content in var. japonica
brenda
-
epicotyl of etiolated germinating seedlings
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
additional information
-
BAM4 is preferentially expressed in vascular tissues in source and sink organs
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
beta-amylase production starts from the post-exponential phase of bacterial growth and reached a maximum level during the early-stationary phase
brenda
additional information
-
beta-amylase production starts from the post-exponential phase of bacterial growth and reached a maximum level during the early-stationary phase
-
brenda
additional information
-
differentiation of beta-amylase phenotypes in cultivated barley from worldwide collections, geographical distribution, overview
brenda
additional information
-
tissue-ubiquitous isozyme beta-amylase2, Bmy2
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
analysis of the effects of carbon source, nitrogen source, and metal ions on cell growth and Bacillus aryabhattai beta-amylase production in recombinant Brevibacillus choshinensis. The optimal medium contains 7.5 g/l glucose, pig bone peptone (40.0 g/l), Mg2+ (0.05 mol/l), and trace metal elements, the beta-amylase yield reaches 925.4U /ml, which is 7.2fold higher than that obtained in the initial medium. A modified feeding strategy is proposed and applied in a 3-l fermentor fed with glucose achieving a dry cell weight of 15.4 g/l. Through this cultivation approached 30°C with 0 g/l initial glucose concentration, the maximum beta-amylase activity reaches 5371.8 U/ml which is 41.7fold higher than that obtained with the initial medium. Cell growth and protein synthesis reach a balance at 30°C
brenda
additional information
-
analysis of the effects of carbon source, nitrogen source, and metal ions on cell growth and Bacillus aryabhattai beta-amylase production in recombinant Brevibacillus choshinensis. The optimal medium contains 7.5 g/l glucose, pig bone peptone (40.0 g/l), Mg2+ (0.05 mol/l), and trace metal elements, the beta-amylase yield reaches 925.4U /ml, which is 7.2fold higher than that obtained in the initial medium. A modified feeding strategy is proposed and applied in a 3-l fermentor fed with glucose achieving a dry cell weight of 15.4 g/l. Through this cultivation approached 30°C with 0 g/l initial glucose concentration, the maximum beta-amylase activity reaches 5371.8 U/ml which is 41.7fold higher than that obtained with the initial medium. Cell growth and protein synthesis reach a balance at 30°C
-
brenda
additional information
-
enzyme is produced throughout exponential growth and during the early-stationary phase
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
optimal cultivation conditions, overview
-
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
optimal cultivation conditions, overview
brenda
additional information
-
beta-amylase activity is totally absent in the embryo/scutellum
brenda
additional information
-
beta-amylase activity is totally absent in the embryo/scutellum
brenda
additional information
-
beta-amylase activity is totally absent in the embryo/scutellum
brenda
additional information
-
optimal cultivation conditions, overview
brenda
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C148S
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
C206S
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
C261S
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
C32S
site-directed mutagenesis, the mutant shows 70% impaired redox sensitivity compared to the wild-type enzyme
C399S
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
C413S
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
C470S
site-directed mutagenesis, the mutant shows 70% impaired redox sensitivity compared to the wild-type enzyme
C506S
site-directed mutagenesis, the mutant shows a redox sensitivity similar to the wild-type enzyme
E380Q
-
structural modeling of BAM-9. BAM-4 and BAM-9 are also substituted at position 342 on the inner loop
E380R
-
structural modeling of the BAM-4 active site predicts an inactive protein. BAM-4 and BAM-9 are also substituted at position 342 on the inner loop
E172A/E367A
-
catalytic site double mutant, no hydrolytic activity, no rescue of activity by 2 M azide
E367A
-
catalytic site mutant, no hydrolytic activity in the absence of azide, in the presence of 2 M azide the mutant enzyme hydrolyzes maltopentaose at pH 7 and 25°C producing maltose, mechanism
S235A
binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 88% of wild-type activity with soluble starch as substrate
S235A/Y249A
double mutant, binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 63% of wild-type activity with soluble starch as substrate
S235A/Y249A/W449F/W495F
quadruple mutant, kinetic parameters for the hydrolysis of amylose, 51% of wild-type activity with soluble starch as substrate
T47M/Y164E/T328N
site-directed mutagenesis, the mutation of Y164 leads to disruption of the hydrogen bonding around the catalytic site, the mutant enzyme shows a shifted pH optimum and a 88% decreased kcat compared to the wild-type enzyme
W449F
binding parameters to raw corn starch
W449F/W495F
double mutant, binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 61% of wild-type activity with soluble starch as substrate
W495F
binding parameters to raw corn starch
Y164E
site-directed mutagenesis, the mutation of Y164 leads to disruption of the hydrogen bonding around the catalytic site, the mutant enzyme shows a shifted pH optimum and a 59% decreased kcat compared to the wild-type enzyme
Y164F
site-directed mutagenesis, the mutation of Y164 leads to disruption of the hydrogen bonding around the catalytic site, the mutant enzyme shows a shifted pH optimum and a 64% decreased kcat compared to the wild-type enzyme
Y164H
site-directed mutagenesis, the mutation of Y164 leads to disruption of the hydrogen bonding around the catalytic site, the mutant enzyme shows a shifted pH optimum and a 97% decreased kcat compared to the wild-type enzyme
Y164Q
site-directed mutagenesis, the mutation of Y164 leads to disruption of the hydrogen bonding around the catalytic site, the mutant enzyme shows a shifted pH optimum and a 83% decreased kcat compared to the wild-type enzyme
Y249A
binding parameters to raw corn starch, kinetic parameters for the hydrolysis of amylose, 80% of wild-type activity with soluble starch as substrate
D53A
mutant enzyme shows 13% of the wild-type activity towards maltoheptaose
E178Y
kinetic data, 43% of specific activity of wild-type SBA, the pH-optimum of mutant enzyme is shifted to pH 6, the hydrogen bond between Glu-380 and Asn-340 is completely disrupted, mutant SBA structure
E186Q
site-directed mutagenesis, mutation of catalytic residue, the mutant shows 16000fold decreased activity compared to the wild-type enzyme
E380Q
site-directed mutagenesis, mutation of catalytic residue, the mutant shows 37000fold decreased activity compared to the wild-type enzyme
M51T
kinetic data, 11% of specific activity of wild-type SBA, the pH-optimum of mutant enzyme is shifted to pH 6.5, the hydrogen bonds between Glu-380 and Asn-340 and between Glu-380 and Lys-295 are completely disrupted, mutant SBA structure
N340T
kinetic data, 32% of specific activity of wild-type SBA, the pH-optimum of mutant enzyme is shifted to pH 6.6, the hydrogen bond between Glu-380 and Asn-340 is completely disrupted, mutant SBA structure
T342A
site-directed mutagenesis, structural analysis of mutant active site conformation
T342S
site-directed mutagenesis, structural analysis of mutant active site conformation
T342V
site-directed mutagenesis, structural analysis of mutant active site conformation
W55R
mutant enzyme shows 20% of the wild-type activity towards maltoheptaose
L347S
-
Sd2L mutant, mutation increases the thermostability index T50 by 2.1°C by slowing thermal unfolding of enzyme during heating
M185L/S295A/I297V/S350P/S351P/Q352D/A376S
-
the mutant enzyme acquires enhanced thermostability, but its function as beta-amylase is unchanged. The mutant is stable at pH-values up to 12.5, while the original recombinant enzyme is unstable at pH-values above pH 9.5
R115C
-
Sd2L mutant, mutation is responsible for the difference in the kinetic properties of the allelic forms
V233A
-
Sd2L and Sd1 mutant, mutation increases the thermostability index T50 of Sd2L by 1.9°C, mutation causes an acceleration of the refolding after heating
V233A/L347S
-
Sd2L double mutation resulting in exactly the same sequence as Sd2H beta-amylase, mutation increases the thermostability index T50 of Sd2L by 4°C
D170Q/L172F/Y173L
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
G48A/A51E
site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme
I74V
site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme
L135V
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
L172F/Y173L
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
L172F/Y173L/A174E
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
R118Q
site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme
R311P/I312L
site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme
R311P/I312L/S317A
site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme
S133N/L135V
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
S137T/K138A
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
S317A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
T116M
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
T116M/R118Q
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
T76V
site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme
T98K/Y99L/A100V/D101E
site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme
Y72D
site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme
Y72D/I74V/T76V
site-directed mutagenesis, the mutant shows increased thermostability at 60°C compared to the wild-type enzyme
L135V
-
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
-
S317A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
T116M
-
site-directed mutagenesis, the mutant shows reduced thermostability at 60°C compared to the wild-type enzyme
-
T76V
-
site-directed mutagenesis, the mutant shows similar thermostability at 60°C as the wild-type enzyme
-
E172A
catalytic site mutant
E172A
-
catalytic site mutant, no hydrolytic activity, no rescue of activity by 2 M azide
additional information
construction of BMY8 knockout plants, and of BMY8 RNAi plants, enzyme induction upon a cold shock leads to starch-dependent maltose accumulation, which can be prevented by RNA interference, phenotype and starch content of recombinant BMY8 RNAi plants, freezing tolerance of recombinant plants, overview
additional information
-
knockout plants of palstidic isozymes BMY6 and BMY8/CT-BMY leads to a starch-excess phenotype in leaves
additional information
-
bam1, T-DNA insertion mutation, has no elevated starch levels and no lower nighttime maltose levels than the wild type. Mutant bam2, T-DNA insertion mutation. Mutant bam3, formation of a mutant line via the Arabidopsis TILLING Program, has elevated starch levels and lower nighttime maltose levels than the wild type. Mutant bam4, T-DNA insertion mutation, has elevated starch levels. Double mutant bam1 bam3, more severe phenotype than bam3. Total beta-amylase activity is reduced in leaves of bam1 and bam3 mutants but not in bam2 and bam4 mutants
additional information
mutation of two of the three carbohydrate-binding sites aside from the active site: Site2 in domain B and Site1 in domain C
additional information
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mutation of two of the three carbohydrate-binding sites aside from the active site: Site2 in domain B and Site1 in domain C
additional information
engineering of the enzyme's pH optimum, conversion of the pH optimum from the bacterial type with pH 6.7 to the higher-plant type with pH 5.4, from soybean enzyme, overview
additional information
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engineering of the enzyme's pH optimum, conversion of the pH optimum from the bacterial type with pH 6.7 to the higher-plant type with pH 5.4, from soybean enzyme, overview
additional information
generation of different specific deletions at the C-terminal tail and complete deletion of the four C-terminal glycine-rich repeats, complete deletion enhances the thermostability, but the incomplete not, both enhance the substrate binding affinity
additional information
-
generation of different specific deletions at the C-terminal tail and complete deletion of the four C-terminal glycine-rich repeats, complete deletion enhances the thermostability, but the incomplete not, both enhance the substrate binding affinity
additional information
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Sd1 and Sd2L beta-amylase with a 46 amino acid deletion in the C-terminal tail
additional information
covalent immobilization of beta-amylase enzyme on the surface of modified magnetic nanoparticles (ZnFe2O4-SiO2-NH2). The magnetic nanoparticles of ZnFe2O4 are synthesized by chemical co-precipitation method, and then tetraethyl orthosilicate (TEOS) and 3-aminopropyltriethoxy silane (APTES) are used for modification of ZnFe2O4 nanoparticles with silica and amine groups (ZnFe2O4-SiO2-NH2, classical Stoeber method). The aminated surface of ZnFe2O4 nanoparticles is exposed to beta-amylase immobilization using trichlorotriazine (TCT) as covalent agent. The immobilized beta-amylase enzyme is characterized by techniques such as Fourier transform infrared (FT-IR), scanning electron microscopy (SEM), powder X-ray diffraction (XRD) and energy dispersive X-ray analysis (EDAX). The immobilized enzyme shows increased catalytic activity and efficiency, as well as thermal stability compared to free enzyme. Highest activity at pH 7.0 and 40°C. Method evaluation and kinetics, overview
additional information
construction of 18 mutants containing ancestral residues derived from a bacterial, common-ancestral beta-amylase sequence, inferred using a phylogenetic tree composed of higher plant and bacterial amylase sequences. Several of these mutants are more thermostable than that of the wild-type amylase, one mutant has both greater activity and greater thermostability. It is necessary to conserve the residues surrounding an ancestral residue if thermostability is to be improved by the ancestral mutation method
additional information
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construction of 18 mutants containing ancestral residues derived from a bacterial, common-ancestral beta-amylase sequence, inferred using a phylogenetic tree composed of higher plant and bacterial amylase sequences. Several of these mutants are more thermostable than that of the wild-type amylase, one mutant has both greater activity and greater thermostability. It is necessary to conserve the residues surrounding an ancestral residue if thermostability is to be improved by the ancestral mutation method
additional information
-
construction of 18 mutants containing ancestral residues derived from a bacterial, common-ancestral beta-amylase sequence, inferred using a phylogenetic tree composed of higher plant and bacterial amylase sequences. Several of these mutants are more thermostable than that of the wild-type amylase, one mutant has both greater activity and greater thermostability. It is necessary to conserve the residues surrounding an ancestral residue if thermostability is to be improved by the ancestral mutation method
-
additional information
a transposon-induced spontaneous mutation results in low beta-amylase content in rice, overview
additional information
Q6Z5B7
a transposon-induced spontaneous mutation results in low beta-amylase content in rice, overview
additional information
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analysis of the effects of carbon source, nitrogen source, and metal ions on cell growth and Bacillus aryabhattai beta-amylase production in recombinant Brevibacillus choshinensis. The optimal medium contains 7.5 g/l glucose, pig bone peptone (40.0 g/l), Mg2+ (0.05 mol/l), and trace metal elements, the beta-amylase yield reaches 925.4U /ml, which is 7.2fold higher than that obtained in the initial medium. A modified feeding strategy is proposed and applied in a 3-l fermentor fed with glucose achieving a dry cell weight of 15.4 g/l. Through this cultivation approached 30°C with 0 g/l initial glucose concentration, the maximum beta-amylase activity reaches 5371.8 U/ml which is 41.7fold higher than that obtained with the initial medium
additional information
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analysis of the effects of carbon source, nitrogen source, and metal ions on cell growth and Bacillus aryabhattai beta-amylase production in recombinant Brevibacillus choshinensis. The optimal medium contains 7.5 g/l glucose, pig bone peptone (40.0 g/l), Mg2+ (0.05 mol/l), and trace metal elements, the beta-amylase yield reaches 925.4U /ml, which is 7.2fold higher than that obtained in the initial medium. A modified feeding strategy is proposed and applied in a 3-l fermentor fed with glucose achieving a dry cell weight of 15.4 g/l. Through this cultivation approached 30°C with 0 g/l initial glucose concentration, the maximum beta-amylase activity reaches 5371.8 U/ml which is 41.7fold higher than that obtained with the initial medium
-
additional information
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chloroplast-localized enzyme downregulation by expression of antisense mRNA results in a starch-excess phenotype in leaves compared to wild-type plants
additional information
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a fusion gene that encodes a polypeptide of 1495 amino acids is constructed from the beta-amylase (BA) gene of Clostridium thermosulfurogenes and trehalose synthase (TS) gene of Thermus thermophilus. The fused gene is overexpressed in Escherichia coli, and a recombinant bifunctional fusion protein with beta-amylase at the N-terminal (BATS) or C-terminal (TSBA) of trehalose synthase having both beta-amylase and trehalose synthase activities with an apparent molecular mass of 164000 Da is obtained. BATS or TSBA catalyzes the sequential reaction in which maltose is formed from starch and then is converted into trehalose. The Km values of the BATS and TSBA fusion enzymes for the reaction from starch to trehalose are smaller than those of an equimolar mixture of BA and TS (BA/TS). The kcat value of BATS approximates that of the BA/TS mixture, but that of TSBA exceedes it. TSBA shows much higher sequential catalytic efficiency than the separately expressed BA/TS mixture. The catalytic efficiency of TSBA or BATS is 3.4 or 2.4times higher, respectively, than that of a mixture of individual enzymes. The thermal stability readings of the recombinant fusion enzymes BATS and TSBA are better than that of the mixture of individual recombinant enzymes
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100
2 h, 22% loss of activity. Ater 4 h of incubation, the relative activity of the enzyme is 45%
105
melting temperature at pH 6.0
20 - 60
-
purified native enzyme, 1 h, pH 6.0, stable
45
-
pH 7.5, 30 min, stable
52.6
T50, Sd2L, mature grain
54.7
T50, Sd1, mature grain
55.2
-
T50 value for wild-type Sd2L and its D165E mutant
55.3
-
T50 value for R115C and V430A mutants of Sd2L
57.1
-
T50 value for V233A mutant of Sd2L
57.3
-
T50 value for wild-type Sd1 and L347S mutant of Sd2L
59.2
-
T50 value for wild-type Sd2H and V233A/L347S double mutant of Sd2L
59.4
-
T50 value for V233A mutant of Sd1
63
-
30 min, 50% loss of activity
67
melting temperature at pH 4.0
69
-
30 min, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S, 50% inactivation
75
-
about 20% loss of activity
85
the half-life is 69 min, 225 min, and 255 min at pH 5.0, pH 6.0, and pH 7.0
91
melting temperature at pH 5.0
40
-
completely stable up to
40
-
thermal denaturation above
50
-
1 h, stable
50
-
10 min, stable below
50
-
pH 6.0, 30 min, native enzyme is stable up to
50
-
5 h, 45% loss of activity
50
-
10 min, stable below
50
2 h, purified enzyme retains 100 % relative activity. Ater 4 h of incubation, the relative activity of the enzyme is 80%
55
-
1 h, 20% loss of activity
55
-
2 h, in presence of substrate, stable
55
-
pH 6.0, 30 min, immobilized enzyme is stable up to
55
-
15 min, 50% loss of activity
55
-
30 min, 56% loss of activity
55
-
15 min, 50 mM NaOAc buffer, pH 6, stable up to
57
-
30 min, 50% loss of activity
57
-
30 min, recombinant enzyme, 50% loss of activity
57.5
-
30 min, analysis of isozyme thermostability of different species and subspecies, overview
57.5
-
30 min, analysis of isozyme thermostability of different cultivars, overview
60
-
40 min, stable
60
-
pH 5.4, 90 min, 38% loss of activity of isoenzyme 2, 55% loss of activity of isoenzyme 6
60
-
pH 4.8, half-life: 291 min for the first decay segment, 1790 min for the second decay segment
60
-
more than 2 h, 96% loss of activity
60
half-life of the wild-type enzyme is 6.4 min
60
-
in presence of 5% starch, entirely stable
60
-
10 min, about 70% loss of activity
60
-
30 min: 65% loss of activity, 60 min: 75% loss of activity, 90 min: 100% loss of activity
60
-
temperature optimum, but enzyme loses activity when exposed to 60°C, irreversible thermodenaturation, thermodenaturation kinetics, Mn2+ and exogenous thiols like dithiothreitol, 2-mercaptoethanol or cysteine HCl play a remarkable role in reactivation of thermally denatured enzyme
60
-
the thermoinactivated enzyme (exposed to 60°C for 10 min) could be partially reactivated by the addition of 1 mM 2-mercaptoethanol (7.3% increase) and 4 mM Mn2+ (14% increase)
60
2 h, purified enzyme retains 100 % relative activity. Ater 4 h of incubation, the relative activity of the enzyme is 80%
65
-
purified native enzyme, pH 6.0-6.5, stable up to
65
-
1.5 h, retains about 80% of its activity
70
10 min, complete inactivation
70
-
pH 4.8, half-life: 14.4 min for the first decay segment, 37.9 min for the second decay segment
70
-
2 h, stable in absence of substrate or Ca2+
70
2 h, purified enzyme retains 100 % relative activity. Ater 4 h of incubation, the relative activity of the enzyme is 72%
80
-
purified native enzyme, 1 h, pH 6.0, 80% activity remaining
80
-
unstable in absence of substrate or Ca2+, stable in presence of 5 mM Ca2+ or 1% substrate
80
-
pH 6.0, 10 min, about 50% loss of activity
80
2 h, purified enzyme retains 100 % relative activity. Ater 4 h of incubation, the relative activity of the enzyme is 63%
90
-
purified native enzyme, 1 h, pH 6.0, 5% activity remaining
90
2 h, 15% loss of activity. Ater 4 h of incubation, the relative activity of the enzyme is 54%
additional information
-
the 3 allelic forms of beta-amylase Sd1, Sd2H and Sd2L exhibit different thermostability, due to two amino acid substitutions, V233A and L347S, which increase the thermostability index T50 of Sd2L by 1.9°C and 2.1°C, respectively
additional information
-
the recombinant isozyme Bmy2 from cultivar Morex shows a slightly higher thermostability compared to the recombinant enzyme from cultivar Steptoe, T50 values, residues D238, M337, and Q362 are involved in the Morex Bmy2 thermostability, overview
additional information
-
thermal inactivation kinetics of the enzyme at different pressure/temperature conditions, mechanism, overview
additional information
-
immobilization of both native and modified enzymes on a amino silica results in thermostabilization of the enzyme
additional information
-
starch greatly enhances heat stability
additional information
-
increased thermoresistance of beta-amylase is achieved through stabilization of thiol groups present at the active site by manipulating the enzymes environment by the addition of Mn2+ and 2-mercaptoethanol, and through immobilization. Both of which would increase the enzymes practical importance and industrial utility
additional information
-
stability is greatly enhanced by addition of 5 mM CaCl2
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