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4-nitrophenyl alpha-D-maltohexaoside + H2O
4-nitrophenol + maltohexaose
I3RE04
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
poor substrate
-
-
?
4-nitrophenyl maltopyranoside + H2O
4-nitrophenol + maltose
excellent substrate
-
-
?
acarbose + alpha-D-glucose
isoacarbose
acarbose + H2O
acarviosine-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
acarbose + H2O
alpha-maltose + ?
acarbose + H2O
D-glucose + acarviosine-glucose
acarbose + H2O
glucose + acarviosine-glucose
-
-
-
-
?
alpha-(1,4)-glycosidic linked cyclodextrins + H2O
maltooligosaccharide
-
main depolymerization of outer amylopectin branches
-
-
?
alpha-cyclodextrin + H2O
?
alpha-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
molar ratio 10:1
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
-
-
?
alpha-Schardinger dextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
amylopectin + H2O
alpha-maltose + ?
-
hydrolytic release of maltose residues, wild-type, double and triple mutant enzymes studied to determine substrate size and geometric shape of catalytic site
-
-
?
amylopectin + H2O
fragments of amylopectin
-
main depolymerization of outer amylopectin branches
mainly short amylopectin chains from degradation of outer branches, inhibiting amylopectin retrogradation, and therefore, amorphous starch network and week amylose network of freshly baked bread are retained
-
?
amylopectin + H2O
fragments of amylopectin + dextrin
-
main depolymerization of outer amylopectin branches
mainly short amylopectin chains from degradation of outer branches, inhibiting amylopectin retrogradation, and therefore, amorphous starch network and week amylose network of freshly baked bread are retained
-
?
amylopectin + H2O
maltose + ?
amylopectin + H2O
maltose + alpha-D-glucose
-
-
in the initial stages of hydrolysis enzyme produces maltotetraose, maltotriose and maltose, as the reaction progresses, the maltotriose and maltotetraose disappears, glucose being formed by the splitting of maltotriose into equimolar amounts of maltose and glucose
?
amylopectin + H2O
maltose + D-glucose
amylopectin + H2O
maltose + maltotriose
amylose + H2O
alpha-maltose + ?
-
substrate size and geometric shape of catalytic site analyzed, wild-type, double and triple mutant enzymes tested, wild-type enzyme hydrolyzed amylose more favourably than amylopectin
-
-
?
amylose + H2O
maltose + ?
amylose + H2O
maltose + D-glucose
azurine cross-linked amylose + H2O
maltose + ?
-
-
-
-
?
beta-cyclodextrin + H2O
?
beta-cyclodextrin + H2O
alpha-maltose + ?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
beta-cyclodextrin + H2O
alpha-maltose + glucose
beta-cyclodextrin + H2O
D-glucose + maltose + maltotriose + maltooligosaccharides
100% activity
-
-
?
beta-cyclodextrin + H2O
maltooligosaccharide
-
-
-
-
?
beta-cyclodextrin + H2O
maltose
beta-cyclodextrin + H2O
maltose + ?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
-
?
cyclomaltodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
D-tagatose + maltotriose
maltosyl-tagatose
-
transglycosylation
-
-
?
gamma-cyclodextrin + H2O
?
gamma-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
maximal activity (100%)
-
-
?
gelatinised starch + H2O
maltose + ?
-
-
-
-
?
gelatinised waxy maize starch + H2O
alpha-maltose + ?
-
-
main product
-
?
gelatinized corn starch + H2O
?
-
-
-
-
?
gelatinized rice starch + H2O
maltose + ?
-
-
-
-
?
glycogen + H2O
maltose + ?
maize starch + H2O
maltose + ?
-
-
-
-
?
maltoheptaose + H2O
maltose + ?
-
-
-
-
?
maltoheptaose + H2O
maltose + D-glucose
-
-
mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (32.8%) as well as maltose
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
maltose + ?
-
-
-
-
?
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
alpha-maltose + ?
-
-
-
-
?
maltopentaose + H2O
maltose + D-glucose
maltose + H2O
D-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
alpha-maltose + ?
-
-
-
-
?
maltotetraose + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
maltotetraose + H2O
maltose
I3RE04
-
-
-
?
maltotetraose + H2O
maltose + D-glucose
-
-
mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (24.8%) as well as maltose
-
?
maltotriose + H2O
alpha-maltose + alpha-D-glucose
maltotriose + H2O
isomaltose + isopanose + panose + branched glucooligosaccharides
-
-
transfer products of transglycosylation
-
?
maltotriose + H2O
maltose + D-glucose
polished rice grain + H2O
maltose + ?
-
-
-
-
?
puerarin + beta-cyclodextrin
daidzein 8-C-glucosyl-(alpha-glucosyl)n-1
-
transglycosylation activity
-
-
?
pullulan + H2O
alpha-maltose + ?
pullulan + H2O
maltose + D-glucose + panose
-
relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9
mainly maltose and glucose with relatively minor quantity of panose and other maltooligosaccharides
-
?
pullulan + H2O
panose + ?
rice meal + H2O
maltose + ?
-
-
-
-
?
simmondsin + acarviosine-glucose
acarviosine-simmondsin + alpha-D-glucose
-
transglycosylation
novel compound in which acarviosine is attached to the glucose-moiety of simmondsin by an alpha-(1,6)-glycosidic linkage, with both antiobesity and hypoglycemic activity
?
soluble starch + H2O
maltose + ?
starch + H2O
alpha-maltose
starch + H2O
alpha-maltose + ?
starch + H2O
maltooligosaccharide
-
-
-
-
?
wheat starch + H2O
maltose + ?
-
-
-
-
?
additional information
?
-
acarbose + alpha-D-glucose

isoacarbose
-
transglycosylation
-
-
?
acarbose + alpha-D-glucose
isoacarbose
-
-
-
-
?
acarbose + alpha-D-glucose
isoacarbose
-
transglycosylation
-
-
?
acarbose + H2O

acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
hydrolysis
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
hydrolysis
-
-
?
acarbose + H2O

alpha-maltose + ?
-
-
-
-
?
acarbose + H2O
alpha-maltose + ?
-
-
-
-
?
acarbose + H2O

D-glucose + acarviosine-glucose
-
-
-
-
?
acarbose + H2O
D-glucose + acarviosine-glucose
-
-
-
-
?
acarbose + H2O
D-glucose + acarviosine-glucose
-
-
-
?
alpha-cyclodextrin + H2O

?
80% activity compared to beta-cyclodextrin
-
-
?
alpha-cyclodextrin + H2O
?
high specificity for alpha-cyclodextrin
-
-
?
alpha-cyclodextrin + H2O
?
-
-
-
?
alpha-cyclodextrin + H2O
?
-
-
-
?
alpha-cyclodextrin + H2O
?
-
64.7% activity compared to gamma-cyclodextrin
-
-
?
amylopectin + H2O

?
less than 2% activity compared to beta-cyclodextrin
-
-
?
amylopectin + H2O
?
less than 2% activity compared to beta-cyclodextrin
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
the maltogenic Bacillus stearothermophilus alpha-amylase preferentially hydrolyses the exterior chains of amylopectin. However, during the later phases, the enzyme also hydrolyses inner chains, presumably with a high multiple attack action
-
-
?
amylopectin + H2O

maltose + ?
-
-
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin + H2O
maltose + ?
I3RE04
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant. Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
amylopectin + H2O
maltose + ?
I3RE04
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant. Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
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 + ?
-
-
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin + H2O

maltose + D-glucose
-
-
-
?
amylopectin + H2O
maltose + D-glucose
-
-
-
?
amylopectin + H2O

maltose + maltotriose
-
-
wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% maltotriose of mutant F188L/D261G/T288P, wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% matotriose of mutant F188L/D261G/T288P
-
?
amylopectin + H2O
maltose + maltotriose
-
-
wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% maltotriose of mutant F188L/D261G/T288P, wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% matotriose of mutant F188L/D261G/T288P
-
?
amylose + H2O

?
45% activity compared to beta-cyclodextrin
-
-
?
amylose + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
amylose + H2O

maltose + ?
-
-
-
-
?
amylose + H2O
maltose + ?
-
-
-
?
amylose + H2O
maltose + ?
-
high preference toward amylose compared to amylopectin
-
-
?
amylose + H2O
maltose + ?
-
-
-
?
amylose + H2O

maltose + D-glucose
-
-
-
?
amylose + H2O
maltose + D-glucose
-
-
-
?
beta-cyclodextrin + H2O

?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
78.1% activity compared to gamma-cyclodextrin
-
-
?
beta-cyclodextrin + H2O

alpha-maltose + ?
Q68KL3
main product alpha-maltose
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
Q68KL3
main product alpha-maltose
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
beta-cyclodextrin + H2O

alpha-maltose + alpha-D-glucose
highest catalytic efficiency
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
highest catalytic efficiency
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
molar ratio 3:1
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
hydrolytic activity
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
high thermostability, substrate preference dependent on oligomeric state
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
high thermostability, substrate preference dependent on oligomeric state
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
prefers cyclodextrins to starch or pullulan as substrate
-
-
?
beta-cyclodextrin + H2O

alpha-maltose + glucose
substrate determination for recombinant enzyme MAUS149
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + glucose
substrate determination for recombinant enzyme MAUS149
-
-
?
beta-cyclodextrin + H2O

maltose
-
-
mainly hydrolyzed to maltose
-
?
beta-cyclodextrin + H2O
maltose
-
-
mainly hydrolyzed to maltose
-
?
beta-cyclodextrin + H2O

maltose + ?
-
relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9
-
-
?
beta-cyclodextrin + H2O
maltose + ?
-
-
-
-
?
gamma-cyclodextrin + H2O

?
10% activity compared to beta-cyclodextrin
-
-
?
gamma-cyclodextrin + H2O
?
10% activity compared to beta-cyclodextrin
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
?
gamma-cyclodextrin + H2O
?
-
-
-
?
glycogen + H2O

?
-
-
-
?
glycogen + H2O

maltose + ?
I3RE04
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
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 + ?
-
-
-
?
maltopentaose + H2O

maltose + D-glucose
I3RE04
-
-
-
?
maltopentaose + H2O
maltose + D-glucose
I3RE04
-
-
-
?
maltotriose + H2O

?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
maltotriose + H2O
?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
maltotriose + H2O
?
-
-
-
-
?
maltotriose + H2O

alpha-maltose + alpha-D-glucose
-
-
-
-
?
maltotriose + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
maltotriose + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
maltotriose + H2O

maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
I3RE04
highest hydrolysis activities are on the alpha-1,4-glycosidic linkage of maltotriose (1.25 U/mg) and the alpha-1,6-glycosidic bond of 6-O-maltosyl-beta-cyclodextrin
-
-
?
maltotriose + H2O
maltose + D-glucose
I3RE04
highest hydrolysis activities are on the alpha-1,4-glycosidic linkage of maltotriose (1.25 U/mg) and the alpha-1,6-glycosidic bond of 6-O-maltosyl-beta-cyclodextrin
-
-
?
maltotriose + H2O
maltose + D-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
-
-
-
?
potato starch + H2O

?
-
-
-
-
?
potato starch + H2O
?
-
-
-
-
?
pullulan + H2O

?
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O

alpha-maltose + ?
substrate determination for recombinant enzyme MAUS149
-
-
?
pullulan + H2O
alpha-maltose + ?
substrate determination for recombinant enzyme MAUS149
-
-
?
pullulan + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
pullulan + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
pullulan + H2O
alpha-maltose + ?
-
-
-
-
?
pullulan + H2O

panose
-
-
-
-
?
pullulan + H2O
panose
-
-
-
-
?
pullulan + H2O
panose
-
-
mainly hydrolyzed to panose
-
?
pullulan + H2O
panose
-
-
mainly hydrolyzed to panose
-
?
pullulan + H2O
panose
-
-
-
-
?
pullulan + H2O
panose
-
-
-
-
?
pullulan + H2O

panose + ?
Q68KL3
main product panose
-
-
?
pullulan + H2O
panose + ?
Q68KL3
main product panose
-
-
?
soluble starch + H2O

?
45% activity compared to beta-cyclodextrin
-
-
?
soluble starch + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
soluble starch + H2O

maltose + ?
-
-
-
-
?
soluble starch + H2O
maltose + ?
the enzyme displays less hydrolytic action on raw starches than on soluble starch
-
-
?
soluble starch + H2O
maltose + ?
-
relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9
-
-
?
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
-
-
?
starch + H2O

?
-
-
-
-
?
starch + H2O
?
-
the enzyme shows a substrate hydrolysis preference for cyclodextrins over starch
-
-
?
starch + H2O

alpha-maltose
-
-
-
?
starch + H2O
alpha-maltose
substrate determination for recombinant enzyme MAUS149
-
-
?
starch + H2O
alpha-maltose
substrate determination for recombinant enzyme MAUS149
-
-
?
starch + H2O
alpha-maltose
-
-
-
?
starch + H2O
alpha-maltose
-
-
-
-
?
starch + H2O
alpha-maltose
-
carbohydrate metabolism in the cytoplasm
-
?
starch + H2O
alpha-maltose
-
-
-
-
?
starch + H2O
alpha-maltose
-
carbohydrate metabolism in the cytoplasm
-
?
starch + H2O
alpha-maltose
-
-
-
?
starch + H2O
alpha-maltose
-
-
-
?
starch + H2O
alpha-maltose
-
exo-acting maltogenic alpha-amylase, removes maltose units from the non-reducing chain ends
-
?
starch + H2O
alpha-maltose
-
-
-
-
?
starch + H2O
alpha-maltose
-
-
-
-
?
starch + H2O
alpha-maltose
-
-
-
-
?
starch + H2O
alpha-maltose
-
-
-
?
starch + H2O
alpha-maltose
-
-
-
?
starch + H2O
alpha-maltose
-
-
-
?
starch + H2O
alpha-maltose
-
-
-
?
starch + H2O
alpha-maltose
-
catalyzes the hydrolysis of starch material, central role in carbohydrate metabolism
-
?
starch + H2O

alpha-maltose + ?
maltogenic amylase from Bacillus sp.
-
-
?
starch + H2O
alpha-maltose + ?
maltogenic amylase from Bacillus sp.
-
-
?
starch + H2O
alpha-maltose + ?
Q68KL3
-
-
-
?
starch + H2O
alpha-maltose + ?
Q68KL3
-
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
?
starch + H2O
alpha-maltose + ?
utilization of BSMA for production of highly branched amylopectin and amylose from enzymatically modified rice starch, branching by transglycosylation mediated by BSMA, increased number of branched side chains in modified amylopectin clusters determined
-
-
?
starch + H2O
alpha-maltose + ?
-
wild-type LGMA and recombinant rLGMA, reaction products determined by thin-layer chromatography and gel filtration
-
-
?
starch + H2O
alpha-maltose + ?
-
wild-type LGMA and recombinant rLGMA, reaction products determined by thin-layer chromatography and gel filtration
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O
alpha-maltose + ?
-
transglycosylation pattern opposite to that of bacterial maltogenic amylases, predominant formation of alpha-1,4-glycosidic linked transfer products than of alpha-1,6-linked products
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O
alpha-maltose + ?
-
transglycosylation pattern opposite to that of bacterial maltogenic amylases, predominant formation of alpha-1,4-glycosidic linked transfer products than of alpha-1,6-linked products
-
-
?
starch + H2O
alpha-maltose + ?
-
-
-
-
?
starch + H2O

maltose
-
the enzyme shows higher affinity to the starch at negative pressure (-200 mbar) compared to the atmospheric pressure
-
-
?
starch + H2O
maltose
-
-
mainly hydrolyzed to maltose
-
?
starch + H2O
maltose
-
-
mainly hydrolyzed to maltose
-
?
starch + H2O

maltose + ?
I3RE04
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
starch + H2O
maltose + ?
I3RE04
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant.Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
additional information

?
-
-
BSMA preferentially hydrolyzes longer branch chains, releasing maltose and glucose from the non-reducing end of the branch chains, and transfers the resulting maltooligosaccharides to the non-reducing ends of the shorter branch chains by forming alpha-1,6-glucosidic linkages
-
-
-
additional information
?
-
-
the enzyme forms highly branched products from branched glucan and branching enzyme-treated tapioca starch
-
-
-
additional information
?
-
the dimeric enzyme transglycosylates hydrolytic products of G4/G5 and acarbose, while the monomeric form does not because of the lack of extra sugar-binding space formed due to dimerization
-
-
-
additional information
?
-
-
enzyme shows hydrolytic activity towards alpha-1,6-glycosidic linkage
-
-
-
additional information
?
-
I3RE04
an exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a G2 unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off G2 unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points
-
-
-
additional information
?
-
-
acarbose is not cleaved by the enzyme
-
-
-
additional information
?
-
-
the enzyme hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner
-
-
-
additional information
?
-
I3RE04
an exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a G2 unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off G2 unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points
-
-
-
additional information
?
-
-
acarbose is not cleaved by the enzyme
-
-
-
additional information
?
-
-
the enzyme hydrolyzes both alpha-1,4-glucosidic and alpha-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner
-
-
-
additional information
?
-
-
maltooligosaccharides G3-G7 show 5.4-24.1% relative activity compared to gamma-cyclodextrin
-
-
-
additional information
?
-
does not hydrolyze cyclodextrin, pullulan and acarbose
-
-
-
additional information
?
-
-
exhibits dual activity of alpha-D-(1,4)- and alpha-D-(1,6)- glycosidic bond cleavages, shows activity of alpha-D(1,4)- to alpha-D-(1,3), alpha-D-(1,4), or alpha-D-(1,6)-transglycosylation and cleaves acarbose, a pseudotetrasaccharide competitive inhibitor of alpha-amylases
-
-
-
additional information
?
-
-
nearly indistinguishable from cyclomaltodextrinase from Bacillus sp. and Bacillus stearothermophilus neopullulanase, distinguished from typicsl alpha-amylases by containing a novel N-terminal domain and exhibiting preferential substrate specificities for cyclomaltodextrins over starch
-
-
-
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0.43
alpha-cyclodextrin
pH and temperature not specified in the publication
0.05 - 2.03
beta-cyclodextrin
2.68
gamma-cyclodextrin
pH and temperature not specified in the publication
4.1 - 13
soluble starch
-
additional information
additional information
-
0.426
acarbose

-
pH 6.0, 60°C, hydrolysis, wild-type
0.545
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332D
1
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332Q
1.08
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332H
0.05
beta-cyclodextrin

-
pH 6.0, 60°C, hydrolysis, variant DM
0.09
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 4B74
0.128
beta-cyclodextrin
-
-
0.16
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type and variants 3C71, 4B78 and 4A48
0.17
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variants 1B76, 1B100
0.174
beta-cyclodextrin
-
pH 6.0, 60°C, wild-type
0.19
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 2A39
0.263
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type
0.308
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl
0.36
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA DELTA124, 1M KCl
0.461
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124
1.48
beta-cyclodextrin
pH and temperature not specified in the publication
2.03
beta-cyclodextrin
-
pH 6.0, 60°C, mutant W47A
1.5
maltoheptaose

-
kinetic parameters for C14-labelled maltooligosaccharides
8.18
maltoheptaose
-
50°C, pH 6.0, mutant enzyme A290I
9.21
maltoheptaose
-
50°C, pH 6.0, wild-type enzyme
3.8
maltohexaose

-
kinetic parameters for C14-labelled maltooligosaccharides
7.16
maltohexaose
-
50°C, pH 6.0, wild-type enzyme
7.53
maltohexaose
-
50°C, pH 6.0, mutant enzyme A290I
3.5
maltopentaose

-
50°C, pH 6.0, mutant enzyme A290I
3.97
maltopentaose
-
50°C, pH 6.0, wild-type enzyme
4.4
maltopentaose
-
kinetic parameters for C14-labelled maltooligosaccharides
16.2
maltopentaose
pH 5.0, 85°C
21.2
maltopentaose
-
pH 5.0, 90°C
63.43
maltose

-
50°C, pH 6.0, wild-type enzyme
427
maltose
-
50°C, pH 6.0, mutant enzyme A290I
1.6
maltotetraose

-
kinetic parameters for C14-labelled maltooligosaccharides
2.95
maltotetraose
-
50°C, pH 6.0, mutant enzyme A290I
3.38
maltotetraose
-
50°C, pH 6.0, wild-type enzyme
18.2
maltotetraose
pH 5.0, 85°C
18.8
maltotetraose
-
pH 5.0, 90°C
1.13
maltotriose

-
50°C, pH 6.0, wild-type enzyme
2.52
maltotriose
-
50°C, pH 6.0, mutant enzyme A290I
3.6
maltotriose
-
kinetic parameters for C14-labelled maltooligosaccharides
4.25
maltotriose
pH 5.0, 85°C
8.4
maltotriose
-
pH 5.0, 90°C
4.1
soluble starch

-
estimated for monomeric conformation, in presence of 1 M NaCl
-
13
soluble starch
-
estimated for the high oligomer conformation
-
additional information
additional information

-
Km 49.7 mg/ml, starch as substrate, pH 6.0, 60°C, wild-type, 1 M KCl; Km 5.34 mg mL-1, starch as substrate, pH 6.0, 60°C, hydrolysis, truncated mutant ThMA-DELTA124; Km 61.0 mg/ml, starch as substrate, pH 6.0, 60°C, hydrolysis, wild-type; Km 7.72 mg/ml, starch as substrate, pH 6.0, 60°C, truncated mutant ThMA-DELTA124, 1M KCl
-
additional information
additional information
-
Km 131 mg/ml, starch as substrate, mutant W47A; Km 73.5 mg/ml, starch as substrate, wild-type
-
additional information
additional information
-
lower affinity for binding of amylopectin but higher affinity for amylose in mutant enzymes demonstrated, sterospecific substrate binding properties of triple mutant enzyme determined by molecular modelling
-
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0.1 - 500
alpha-cyclodextrin
0.005 - 15.38
amylopectin
0.00000343 - 280.8
beta-cyclodextrin
29.1 - 225.6
gamma-cyclodextrin
0.0017 - 197
maltopentaose
0.0033 - 574.1
maltotetraose
0.037 - 652.5
maltotriose
0.021 - 9.9
soluble starch
-
18.7
acarbose

-
pH 6.0, 60°C, hydrolysis, mutant E332H
41.4
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332Q
45.4
acarbose
-
pH 6.0, 60°C, hydrolysis, mutant E332D
67.8
acarbose
-
pH 6.0, 60°C, hydrolysis, wild-type
0.1
alpha-cyclodextrin

monomeric enzyme form, at pH 7.0 and 80°C
0.75
alpha-cyclodextrin
mutant enzyme D109A, at pH 7.0 and 80°C
1.39
alpha-cyclodextrin
mutant enzyme D109E, at pH 7.0 and 80°C
1.45
alpha-cyclodextrin
pH and temperature not specified in the publication
2.78
alpha-cyclodextrin
dimeric enzyme form, at pH 7.0 and 80°C
500
alpha-cyclodextrin
in sodium-acetate buffer (50 mM, pH 6.0), at 60°C
0.005
amylopectin

mutant enzyme D109E, at pH 7.0 and 80°C
0.04
amylopectin
dimeric enzyme form, at pH 7.0 and 80°C
0.1
amylopectin
mutant enzyme D109A, at pH 7.0 and 80°C
0.17
amylopectin
monomeric enzyme form, at pH 7.0 and 80°C
0.8
amylopectin
pH and temperature not specified in the publication
4.01
amylopectin
-
at pH 5.5 and 90°C
15.38
amylopectin
in sodium-acetate buffer (50 mM, pH 6.0), at 60°C
0.022
amylose

mutant enzyme D109E, at pH 7.0 and 80°C
0.04
amylose
dimeric enzyme form, at pH 7.0 and 80°C
0.13
amylose
mutant enzyme D109A, at pH 7.0 and 80°C
0.21
amylose
monomeric enzyme form, at pH 7.0 and 80°C
0.59
amylose
pH and temperature not specified in the publication
4.21
amylose
-
at pH 5.5 and 90°C
62.82
amylose
in sodium-acetate buffer (50 mM, pH 6.0), at 60°C
0.00000343
beta-cyclodextrin

-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA-DELTA124
0.00000367
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124, 1 M KCl
0.12
beta-cyclodextrin
monomeric enzyme form, at pH 7.0 and 80°C
0.49
beta-cyclodextrin
mutant enzyme D109A at pH 7.0 and 80°C
0.66
beta-cyclodextrin
mutant enzyme D109E at pH 7.0 and 80°C
1.33
beta-cyclodextrin
dimeric enzyme form, at pH 7.0 and 80°C
5.36
beta-cyclodextrin
pH and temperature not specified in the publication
12.5
beta-cyclodextrin
at pH 7.0 and 40°C
20
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variants DM and 4B74
110
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 4B78
120
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 3C71
126
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl
126
beta-cyclodextrin
-
-
130
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 4A48
160
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type
167
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, wild-type
170
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 2A39
180
beta-cyclodextrin
-
pH 6.0, 60°C, mutantW47A
190
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 1B100
200
beta-cyclodextrin
-
pH 6.0, 60°C, hydrolysis, variant 1B76
280.8
beta-cyclodextrin
in sodium-acetate buffer (50 mM, pH 6.0), at 60°C
29.1
gamma-cyclodextrin

pH and temperature not specified in the publication
225.6
gamma-cyclodextrin
in sodium-acetate buffer (50 mM, pH 6.0), at 60°C
2
maltoheptaose

-
50°C, pH 6.0, mutant enzyme A290I
42.5
maltoheptaose
-
50°C, pH 6.0, wild-type enzyme
72.08
maltoheptaose
-
50°C, pH 6.0, mutant enzyme A290I
384.1
maltoheptaose
-
50°C, pH 6.0, wild-type enzyme
9.2
maltohexaose

-
50°C, pH 6.0, wild-type enzyme
20 - 50
maltohexaose
-
50°C, pH 6.0, mutant enzyme A290I
88.45
maltohexaose
-
50°C, pH 6.0, mutant enzyme A290I
160.3
maltohexaose
-
50°C, pH 6.0, wild-type enzyme
0.0017
maltopentaose

-
pH 5.0, 90°C
3.85
maltopentaose
pH 5.0, 85°C
69.01
maltopentaose
-
50°C, pH 6.0, mutant enzyme A290I
197
maltopentaose
-
50°C, pH 6.0, wild-type enzyme
0.04
maltose

-
50°C, pH 6.0, mutant enzyme A290I
0.29
maltose
-
50°C, pH 6.0, wild-type enzyme
0.0033
maltotetraose

-
pH 5.0, 90°C
3.95
maltotetraose
pH 5.0, 85°C
29.8
maltotetraose
-
50°C, pH 6.0, wild-type enzyme
173.5
maltotetraose
-
50°C, pH 6.0, mutant enzyme A290I
574.1
maltotetraose
-
50°C, pH 6.0, wild-type enzyme
0.037 - 0.23
maltotriose

-
50°C, pH 6.0, mutant enzyme A29I
6.35
maltotriose
-
pH 5.0, 90°C
11.45
maltotriose
pH 5.0, 85°C
79.07
maltotriose
-
50°C, pH 6.0, mutant enzyme A29I
652.5
maltotriose
-
50°C, pH 6.0, wild-type enzyme
0.021
soluble starch

mutant enzyme D109E, at pH 7.0 and 80°C
-
0.04
soluble starch
dimeric enzyme form, at pH 7.0 and 80°C
-
0.12
soluble starch
mutant enzyme D109A, at pH 7.0 and 80°C
-
0.2
soluble starch
monomeric enzyme form, at pH 7.0 and 80°C
-
9.9
soluble starch
at pH 7.0 and 40°C
-
0.000245
starch

-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124
0.000332
starch
-
pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124, 1 M KCl
249
starch
-
pH 6.0, 60°C, wild-type
301
starch
-
pH 6.0, 60°C, hydrolysis, wild-type
335
starch
-
pH 6.0, 60°C, mutant W47A
457
starch
-
pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl
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0.2
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variant DM
0.3
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 4B74
1
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 4B78
1.25
-
pH 5.0, 90°C, substrate: maltotriose
1.5
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, wild-type
1.7
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variants 2A39, 4A48 and 3C71
2
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 1B100
2.1
-
pH 6.0, 60°C, beta-cyclodextrin as substrate, variant 1B76
5.4
-
beta-cyclodextrin as substrate, dimer
14.2
-
starch as substrate
21.1
-
starch as substrate, 0.2 M KCl
24
-
starch as substrate, 0.4 M KCl
26
-
starch as substrate, 0.6 M KCl
26.3
-
starch as substrate, 0.8 M KCl
27.6
-
starch as substrate, 1.0 M KCl
30.5
-
soluble starch as substrate, monomer
58.7
-
hydrolysis of beta-cyclodextrin
91
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CuCl2
93.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM HgCl2
95.2
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM ZnCl2
98.5
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM FeSO4
177.4
-
cell extract, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5)
194.1
-
beta-cyclodextrin as substrate, monomer
206.8
-
beta-cyclodextrin as substrate, 1.0 M KCl
210
-
beta-cyclodextrin as substrate, 0.8 M KCl
227.2
-
beta-cyclodextrin as substrate, 0.6 M KCl
242.9
-
beta-cyclodextrin as substrate, 0.4 M KCl
257.8
-
beta-cyclodextrin as substrate, 0.2 M KCl
268.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM MnCl2
278
-
beta-cyclodextrin as substrate
342.7
-
beta-cyclodextrin as substrate, dimer
413.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM BaCl2
535.1
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5)
558.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) methanol
568.8
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CoCl2
592.9
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) DMSO
604.7
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 10% (v/v) ethanol
695.6
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM MgCl2
728.8
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM CaCl2
785.5
-
after 3fold purification, using gamma-cyclodextrin as substrate, at 90°C in 50 mM sodium acetate buffer (pH 5.5), with 5 mM AlCl3
additional information

kinetic mechanism for recombinant enzyme MAUS149 shown, determined by measuring the amount of reducing sugars released during incubation with starch using the dinitrosalicylic acid method, substrate concentrations ranging from 1 to 7.5 g/ml for starch and from 0.5 to 4 g/l for cyclodextrin and pullulan
additional information
Q68KL3
kinetic properties determined in wild-type and mutant enzymes, relative activity indicated for several mutants from different lineages of DNA shuffling
additional information
kinetic properties determined by amount of reducing sugars, assayed according to the dinitrosalicylic acid method
additional information
-
catalytic activity of wild-type LGMA and recombinant rLGMA tested in liquid and solid media, kinetic properties determined by amount of reducing sugars, assayed according to the dinitrosalicylic acid method, reaction at pH 6.5 for 13.5 h at 50°C, yields of 53.1% obtained
additional information
-
specific activity of starch hydrolysis estimated for the high oligomer conformation is about 7 U/mg and for monomeric state about 110 U/mg
additional information
-
kinetic properties determined towards amylose and amylopectin in wild-type, double and triple mutant enzymes, bicinchonimate method, determination of reducing sugars
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-20 - 40
the enzyme retains more than 50% of its activity at 40°C and 30°C for 10 min. The half-lives of the enzyme are 239.02 h, 126.03 h and 108.30 h at -20°C, 4°C and 20°C, respectively. However, the half-lives are dramatically reduced to 0.37 h and 0.04 h at 30°C and 40°C, respectively
20 - 70
-
the enzyme shows 80% of the initial activity after an incubation time of 30 min without substrate in the temperature range of 20-70°C
40 - 70
-
the enzyme is stable up to 40°C at atmospheric pressure, but the activity of the maltogenic alpha-amylase is drastically reduced above 40°C. Hhigher temperatures (60 and 70°C) are destructive to the enzyme even in the presence of substrate starch
55
-
half-life at 55°C is about 15 min
55 - 75
the enzyme remains stable for up to 60 min at 55°C, after 60 min at 60 and 65°C the enzyme shows 75% activity, while after 20 min at 70 and 75°C the enzyme is inactive
60 - 70
-
stable at pH 5.5 at 60°C, 25% loss of activity at 70°C
64
-
Tm of Novamyl wild-type at pH 4.0
67
melting temperature at pH 4.0
77
-
Tm-value at pH 8 is 76.7°C
78
Q68KL3
half-life of mutant III-1 about 20 times greater than half-life of the wild-type at 78°C
82
-
Tm-value of mutant R26Q/S169N/I333V/A398V/Q411L/P453L is 81.5°C
83
-
Tm of Novamyl wild-type at pH 5.0
85 - 100
-
purified enzyme is extremely thermostable with a half-life of 60 min at an optimal temperature of 95°C. The enzyme retains about 80% relative activity after 60 min of incubation at 85°C and 90°C, about 50% relative activity after 60 min of incubation at 95°C, and about 25% relative activity after 60 min of incubation at 100°C
85
-
Tm-value of mutant enzyme R26Q/I152N/S153N/S169N/I333V/A398V/Q411L/P453L, Tm-value decreases to 79.9°C in presence of EDTA. Tm-value increases to 87.4°C in presence of CaCl2
88
-
TD of variant NM447 at pH 4.0, an increase of 10°C relative to the wild-type Novamyl
90
the half-life values of the monomeric enzyme at 80, 90 and 100°C are 35.7, 8.2 and 3.12 h, respectively. The half-life values of the dimeric enzyme at 80, 90 and 100°C are 55.7, 12.63 and 3.58 h, respectively
91
melting temperature at pH 5.0
95
-
Tm of variant NM447 at pH 5.0
105
melting temperature at pH 6.0
109
109°C melting temperature with enzymatic activity under acidic conditions (pH 3.5-5.0)
210
-
baking at 210°C for 40 min leaves the enzyme active
50 - 55

-
after incubation for 2 h at 50°C, the wild type enzyme retains 35% of its initial activity. The wild type enzyme has a half-life of 15 min at 55°C
50 - 55
-
the half-life times for the wild type enzyme at 50°C and 55°C are 30 min and 13 min, respectively
60

-
truncated mutant ThMA-DELTA124 unstable
60
-
the enzyme is rapidly inactivated at temperature above 60°C and is totally inactivated at 60°C within 60 min in the absence of the substrate. However, in the presence of 1% (w/v) of soluble starch, the half time rises from approximately 10 to 60 min at 60°C
75

-
Tm of variant NM447 at pH 4.0
80

-
the variants NM447 and NM319 retain 67 and 40% specific activity following a 25-min incubation, respectively
80
Q68KL3
half-life of mutant III-2 is 568 min, half-life of the wild-type is below 1 min at 80°C
80
-
ThMA-DM, highly thermostable mutant enzyme, half-life 172 min, wild type enzyme completely inactivated in less than 1 min
85

-
half-life: 72 min
85
the half-life is 69 min, 225 min, and 255 min at pH 5.0, pH 6.0, and pH 7.0
additional information

kinetics shown, stable at 45°C for 90 min, half-life duration of 18 min at 55°C
additional information
-
NM404 and NM398 has modest improvements in thermal stability, whereas NM326 shows no significant improvement in thermal stability
additional information
Q68KL3
half-lives determined at 75°C, 78°C, 80°C, and 85°C, melting temperatures of mutants III-1 and III-2 determined by differential scanning calorimetry increased by 6.1°C and 11.4°C, respectively, hydrogen bonding, hydrophobic interaction, electrostatic interaction, proper packing, and deamidation predicted as mechanisms for enhanced thermostability in the mutant enzymes
additional information
-
high thermostability, half-lives of thermal inactivation and melting temperature tested
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D30A/K40R/D261G
-
Novamyl variant NM398, similar to wild-type at pH 4.0; variant NM398, medium thermotolerance due to D261G mutation
D46G
-
the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The Km values of the mutant for all substrates are strongly increased compared to the wild type enzyme
D46N
-
the mutant behaves similar to the wild type enzyme regarding kinetic parameters, thermoactivity, thermostability and pH profile
D46V
-
the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The affinity and catalytic efficiency of the mutant toward beta-cyclodextrin are increased 5fold as compared with the wild type enzyme
D46V/P78L/V145A/K548E
-
the half-life times for the mutant at 50°C and 55°C are 70 min and 25 min, compared to 30 min and 13 min for the wild type, respectively
F188L/D261G/T288P
-
Novamyl variant NM447, outperform wild-type Novamyl in bread at pH 4.3. Wild-type Novamyl requires a nearly 30fold protein dosage increase over NM447 to obtain anti-staling bread properties. NM447 appears to have a broad pH functionality profile and performs better than wild-type Novamyl in standard bread to pH 5.9. It seems to be be generally tehrmally stabilized, both at pH 4.0 and 5.0.; variant NM447, most thermotolerant, probably due to F188L mutation, but reduced activity, medium thermotolerance due to D261G mutation, improved anti-staling performance in application test, about 70% activity retained after incubation at 80°C at pH 4.3 for 25 min
G312A
-
the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
G312A/K436R
-
the half-life time at 55°C increase from 15 to 25 min for the double mutant
K436R
-
the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
N115D/F188L
-
Novamyl variant NM319, similar to wild-type at pH 4.0, at pH 5.5 the variant outperform wild-type Novamyl, significantly more thermally stable that wild-type; variant NM319, most thermotolerant, probably due to F188L mutation, but reduced activity, improved anti-staling performance in application test, about 40% activity retained after incubation at 80°C at pH 4.3 for 25 min
T142A
-
Novamyl variant NM326, similar to wild-type at pH 4.0; variant NM326, inducing 20% activity increase and 50% thermal stability increase
T142A/D261G/N327S/K425E/K520R/N5951
-
variant NM404, medium thermotolerance due to D261G mutation
T142A/D261G/N327S/K425E/K520R/N595I
-
Novamyl variant NM404, similar to wild-type at pH 4.0
F188L/D261G/T288P
-
Novamyl variant NM447, outperform wild-type Novamyl in bread at pH 4.3. Wild-type Novamyl requires a nearly 30fold protein dosage increase over NM447 to obtain anti-staling bread properties. NM447 appears to have a broad pH functionality profile and performs better than wild-type Novamyl in standard bread to pH 5.9. It seems to be be generally tehrmally stabilized, both at pH 4.0 and 5.0.; variant NM447, most thermotolerant, probably due to F188L mutation, but reduced activity, medium thermotolerance due to D261G mutation, improved anti-staling performance in application test, about 70% activity retained after incubation at 80°C at pH 4.3 for 25 min
-
T142A
-
Novamyl variant NM326, similar to wild-type at pH 4.0; variant NM326, inducing 20% activity increase and 50% thermal stability increase
-
D46G
-
the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The Km values of the mutant for all substrates are strongly increased compared to the wild type enzyme
-
D46N
-
the mutant behaves similar to the wild type enzyme regarding kinetic parameters, thermoactivity, thermostability and pH profile
-
D46V
-
the mutant behaves similar to the wild type enzyme regarding thermoactivity, thermostability and pH profile. The affinity and catalytic efficiency of the mutant toward beta-cyclodextrin are increased 5fold as compared with the wild type enzyme
-
D46V/P78L/V145A/K548E
-
the half-life times for the mutant at 50°C and 55°C are 70 min and 25 min, compared to 30 min and 13 min for the wild type, respectively
-
G312A
-
the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
-
G312A/K436R
-
the half-life time at 55°C increase from 15 to 25 min for the double mutant
-
K436R
-
the mutant has an optimal temperature of 45°C instead of the 40°C for the wild type enzyme
-
N147D/F195L/N263S/D311G/A344V/F397S/N508D
Q68KL3
mutant III-1, seven mutations, generated by random mutagenesis after three rounds of DNA shuffling and recombination, lineage of shuffling mutants indicated
N147D/F195L/N263S/D311G/A344V/F397S/N508D/M375T
Q68KL3
additional exchange M375T of mutant III-2 responsible for decreased specific activity, lineage of shuffling mutants shown
N147D/F195L/N263S/D311G/A344V/F397S/N508D
-
mutant III-1, seven mutations, generated by random mutagenesis after three rounds of DNA shuffling and recombination, lineage of shuffling mutants indicated
-
N147D/F195L/N263S/D311G/A344V/F397S/N508D/M375T
-
additional exchange M375T of mutant III-2 responsible for decreased specific activity, lineage of shuffling mutants shown
-
D109A
the mutant shows increased affinity towards amylose, amylopectin and starch, and a decreased affinity towards alpha- and beta-cyclodextrin
D109E
the mutant does not show any effect on the binding affinity and substrate hydrolytic efficiency towards alpha- and beta-cyclodextrin but a strong decline in the affinity and substrate hydrolytic efficiency of the mutant enzyme towards amylopectin
E580Q
-
strongly reduced activity compared to the wild type enzyme
F218A
-
the mutant shows wild type activity with alpha-1,6-glycosidic bond hydrolysis and about 4fold increased activity with alpha-1,4-glycosidic bond hydrolysis compared to the wild type enzyme
W453A
-
strongly reduced activity compared to the wild type enzyme
E580Q
-
strongly reduced activity compared to the wild type enzyme
-
F218A
-
the mutant shows wild type activity with alpha-1,6-glycosidic bond hydrolysis and about 4fold increased activity with alpha-1,4-glycosidic bond hydrolysis compared to the wild type enzyme
-
W453A
-
strongly reduced activity compared to the wild type enzyme
-
A290I
-
mutant enzyme A290I produces mostly maltose from maltotetraose, while wild-type enzyme produces glucose as well as maltose. kcat/KM of mutant enzyme 290I for maltose is 48times less than that of wild-type enzyme. kcat/Km for maltotriose is 18.5fold lower than wild-type enzyme. kcat/Km for maltotetraose is 2.9fold lower than wild-type enzyme. kcat/Km for maltopentaose is 2.5fold lower than wild-type enzyme. kcat/Km for maltohexaose is 1.9fold lower than wild-type enzyme. kcat/Km for maltoheptaose is 4.7fold lower than wild-type enzyme
A330G/N331C/E332C
-
F-18, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331G/E332C
-
C-20, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331G/E332G
-
G-91, strong reduction of all substrate hydrolyzing activities, higher relative specificity to beta-cyclodextrin than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: high amount of branched tetraose and pentaose
A330G/N331G/E332S
-
G-22, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331P/E332G
-
C-43, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330G/N331V/E332G
-
G-90, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330M/N331G/E332C
-
B-96, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A330S/N331A
-
F-80, strong reduction of all substrate hydrolyzing activities, higher relative specificity to beta-cyclodextrin and pullulan than to starch compared to wild-type, lower relative specificity to maltotriose than to acarbose compared to wild-type, transglycosylation: high amount of branched tetraose and pentaose
A330S/N331G/E332T
-
K-37, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodexxtrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type
A398V
-
random mutagenesis, using DNA shuffling
E332D
-
site-directed mutagenesis, significantly decreased transglycosylation activity
E332H
-
site-directed mutagenesis, replacing Glu 332 with histidine reduces transglycosylation activity significantly, but enhances hydrolysis activity on alpha-(1,3)-, alpha-(1,4)- and alpha-(1,6) glycosidic bonds relative to the wild-type
E332Q
-
site-directed mutagenesis
E357L
-
site-directed mutagenesis
G50I/D109E
-
double mutation, two main residues of the catalytic binding pocket, site-directed mutagenesis
G50I/D109E/V431I
-
triple mutation of three main residues of the catalytic binding pocket, site-directed mutagenesis
I333V
-
random mutagenesis, using DNA shuffling
M375T
-
random mutagenesis, using DNA shuffling
N331S/E332G
-
I-69, strong reduction of all substrate hydrolyzing activities, lower relative specificity to beta-cyclodextrin and pullulan than to starch and to maltotriose than to acarbose compared to wild-type