3.2.1.41: pullulanase
This is an abbreviated version!
For detailed information about pullulanase, go to the full flat file.
Word Map on EC 3.2.1.41
-
3.2.1.41
-
starch
-
pullulans
-
glycogen
-
klebsiella
-
amylose
-
maltotriose
-
alpha-amylase
-
isoamylase
-
lariat
-
glucoamylase
-
amylolytic
-
beta-amylase
-
oxytoca
-
cyclodextrins
-
dextrinase
-
amyloglucosidase
-
alpha-1,6
-
saccharification
-
beta-cyclodextrins
-
waxy
-
maltodextrins
-
aureobasidium
-
glucanotransferase
-
phytoglycogen
-
maltotetraose
-
aerobacter
-
synthesis
-
pilins
-
thermoanaerobacterium
-
branchpoints
-
starch-based
-
alpha-glucans
-
malto-oligosaccharides
-
starch-degrading
-
maltohexaose
-
anoxybacillus
-
industry
-
food industry
-
degradation
-
biotechnology
-
thermoleovorans
-
amylo-1,6-glucosidase
- 3.2.1.41
- starch
- pullulans
- glycogen
- klebsiella
- amylose
- maltotriose
- alpha-amylase
- isoamylase
-
lariat
- glucoamylase
-
amylolytic
- beta-amylase
- oxytoca
- cyclodextrins
-
dextrinase
- amyloglucosidase
-
alpha-1,6
-
saccharification
- beta-cyclodextrins
-
waxy
- maltodextrins
- aureobasidium
-
glucanotransferase
- phytoglycogen
- maltotetraose
-
aerobacter
- synthesis
- pilins
-
thermoanaerobacterium
-
branchpoints
-
starch-based
- alpha-glucans
- malto-oligosaccharides
-
starch-degrading
- maltohexaose
- anoxybacillus
- industry
- food industry
- degradation
- biotechnology
- thermoleovorans
- amylo-1,6-glucosidase
Reaction
Synonyms
1,4-alpha-D-glucan glucanohydrolase, Alpha-dextrin endo-1,6-alpha-glucosidase, amylase-pullulanase, amylopectin 6-glucanohydrolase, amylopullulanase, AmyX, Apu, ApuK885, ApuM957, Ask, BaPul13A, BDPulA324, BmPul, BNPulA324, CAC60157, debranching enzyme, EC 3.2.1.69, glucanohydrolase, amylopectin 6-, limit dextrinase, More, Nostoc punctiforme debranching enzyme, NPDE, PbPulA, Pcal-1616, PelBsp-PulA, PfAPU, Promozyme 200 L, PUL US105, Pul13A, Pul3YH5, PulA, PulASK, PulB, pulGT, Pullulan 6-glucanohydrolase, pullulan-6-glucanohydrolase, pullulanase, pullulanase type 1, pullulanase type I, pullulanase type II, PulWB42, R-enzyme, Saci_1162, TPApu, TTC1198, TTHpu, type II pullulanase, ZUP1
ECTree
3.2.1.41 pullulanaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.2.1.41 - pullulanase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
42-O-beta-D-galactosyl-maltose + beta-cyclodextrin
(Gal-G2)-beta-cyclodextrin + (Gal-G2)2-beta-cyclodextrin
-
analysis of reaction conditions and structural identification of products
-
-
r
amylopectin + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
cyclomaltooctaose + H2O
6,6-di-O-alpha-maltosyl-cG8
-
gamma-cyclodextrin
-
-
?
maltose + cG8
6-O-alpha-maltosyl-cG8
-
through the reversed action
-
-
r
pullulan + H2O
malto-2-4-oligosaccharide + ?
-
best substrate
-
-
?
pullulan + H2O
maltotriose + maltose + D-glucose
this enzyme can attack alpha-1,6- and alpha-1,4-glycosidic linkages in pullulan, and produce a mixture of maltotriose, maltose and glucose
-
-
?
soluble starch + H2O
maltotriose + maltose + maltooligosaccharides
12.8% of the activity with pullulan
-
-
?
starch + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
4-nitrophenyl alpha-D-maltoheptaoside + H2O
4-nitrophenol + alpha-D-maltoheptaose
-
hydrolyzed in an exo-fashion
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside + H2O
4-nitrophenol + alpha-D-maltoheptaose
-
hydrolyzed in an exo-fashion
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside + H2O
4-nitrophenol + alpha-D-maltoheptaose
-
hydrolyzed in an exo-fashion
-
-
?
4-nitrophenyl alpha-D-maltotrioside + H2O
4-nitrophenol + alpha-D-maltotriose
-
hydrolyzed in an exo-fashion
-
-
?
4-nitrophenyl alpha-D-maltotrioside + H2O
4-nitrophenol + alpha-D-maltotriose
-
hydrolyzed in an exo-fashion
-
-
?
6-O-alpha-maltosyl cyclodextrin + H2O
glucose + cyclodextrin
-
similar enzyme
-
-
?
6-O-alpha-maltosyl cyclodextrin + H2O
glucose + cyclodextrin
-
similar enzyme
-
-
?
6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
glucose + cyclodextrin
-
-
-
-
?
6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
glucose + cyclodextrin
-
similar enzyme
-
-
?
6-O-alpha-maltotriosyl cyclomaltohexaose + H2O
glucose + cyclodextrin
-
similar enzyme
-
-
?
6-O-alpha-maltotriosyl cyclomaltohexaose + H2O
glucose + cyclodextrin
-
similar enzyme
-
-
?
amylopectin + H2O
?
35% of activity compared to pullulan
-
-
?
amylopectin + H2O
?
the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides
-
-
?
amylopectin + H2O
?
Geobacillus thermocatenulatus DSMZ730
the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides
-
-
?
amylopectin + H2O
?
12% of the activity compared to pullulan
-
-
?
amylopectin + H2O
?
the enzyme prefers to debranch the DP6-12 side chains of amylopectin at pH 4.5 and 100°C
-
-
?
amylopectin + H2O
?
the enzyme prefers to debranch the DP6-12 side chains of amylopectin at pH 4.5 and 100°C
-
-
?
amylopectin + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
amylopectin + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
amylopectin + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
-
-
-
?
amylopectin + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
34.1% of the rate with pullulan
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
Thermoanaerobium sp.
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltotriose + maltose + ?
-
-
-
?
amylopectin + H2O
maltotriose + maltose + ?
-
-
-
?
amylopectin + H2O
maltotriose + maltose + maltooligosaccharides
6.0% of the activity with pullulan
-
-
?
amylopectin + H2O
maltotriose + maltose + maltooligosaccharides
6.0% of the activity with pullulan
-
-
?
amylopectin + H2O
maltotriose + maltotetraose + maltopentaose + maltohexaose
28% of the activity compared to pullulan, the enzyme hydrolyzes amylopectin to release mainly maltotriose, maltotetraose, maltopentaose and maltohexaose, and their contents reach to 0.0044, 0.0068, 0.0073, 0.025 and 0.035 mg/ml, respectively, after 2 h incubation
-
-
?
amylopectin + H2O
maltotriose + maltotetraose + maltopentaose + maltohexaose
Priestia megaterium WW1210
28% of the activity compared to pullulan, the enzyme hydrolyzes amylopectin to release mainly maltotriose, maltotetraose, maltopentaose and maltohexaose, and their contents reach to 0.0044, 0.0068, 0.0073, 0.025 and 0.035 mg/ml, respectively, after 2 h incubation
-
-
?
amylose + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylose + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylose + H2O
maltotriose + maltose
-
-
-
?
beta-cyclodextrin + H2O
?
21% of activity compared to pullulan
-
-
?
beta-cyclodextrin + H2O
?
in the initial stages, the ring-opening reactions of 6-O-glucosyl-beta-cyclodextrin, 6-O-maltosyl-beta-cyclodextrin and the debranching reactions of 6-O-maltooctaosyl-beta-cyclodextrin are firstly catalyzed. In the subsequent reactions, a serial of maltooligosaccharides are produced
-
-
?
beta-cyclodextrin + H2O
?
in the initial stages, the ring-opening reactions of 6-O-glucosyl-beta-cyclodextrin, 6-O-maltosyl-beta-cyclodextrin and the debranching reactions of 6-O-maltooctaosyl-beta-cyclodextrin are firstly catalyzed. In the subsequent reactions, a serial of maltooligosaccharides are produced
-
-
?
beta-limited dextrin + H2O
maltotriose + maltose + maltooligosaccharides
19.7% of the activity with pullulan
-
-
?
beta-limited dextrin + H2O
maltotriose + maltose + maltooligosaccharides
19.7% of the activity with pullulan
-
-
?
gamma-cyclodextrin + H2O
?
71% of activity compared to pullulan
-
-
?
gamma-cyclodextrin + H2O
?
in the initial stages, the ring-opening reactions of gamma-cyclodextrin is firstly catalyzed. In the subsequent reactions, a serial of maltooligosaccharides are produced
-
-
?
glycogen + H2O
?
-
hydrolyzed slowly. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
glycogen + H2O
?
the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
-
-
?
glycogen + H2O
?
the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
-
-
?
glycogen + H2O
?
-
hydrolyzed slowly. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
glycogen + H2O
?
-
hydrolyzed slowly. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
6.3% of the rate with pullulan
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
-
-
?
glycogen + H2O
maltotriose + maltose + maltooligosaccharides
6.1% of the activity with pullulan
-
-
?
glycogen + H2O
maltotriose + maltose + maltooligosaccharides
6.1% of the activity with pullulan
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
maltoheptaose + H2O
maltotriose + maltose + D-glucose
-
-
-
-
?
maltoheptaose + H2O
maltotriose + maltose + D-glucose
-
-
-
-
?
maltohexaose + H2O
maltotriose + maltose + D-glucose + maltotetraose
-
-
-
-
?
maltohexaose + H2O
maltotriose + maltose + D-glucose + maltotetraose
-
-
-
-
?
maltohexaose + H2O
maltotriose + maltose + D-glucose + maltotetraose
-
-
-
-
?
maltotetraose + H2O
maltose + glucose + maltotriose
-
-
-
-
?
pullulan + H2O
?
-
substrate from Aureobasidium pullulans strain FB-1
-
-
?
pullulan + H2O
?
-
pullalan synthesized by Aureobasidium pullulans strain AP329 as exopolysaccharide and purified, development of a colorimetric assay method for pullalan quantification, overview
-
-
?
pullulan + H2O
maltotriose + ?
EPZ37738
soluble enzyme is highly reactive towards pullulan but was unable to degrade short branches in starch
-
-
?
pullulan + H2O
maltotriose + ?
Anoxybacillus ayderensis DSM 28779
EPZ37738
soluble enzyme is highly reactive towards pullulan but was unable to degrade short branches in starch
-
-
?
pullulan + H2O
maltotriose + ?
-
preparation of maltotriose by hydrolyzing of pullulan with pullulanase, overview
-
-
?
pullulan + H2O
maltotriose + ?
-
complete conversion to maltotriose
-
?
pullulan + H2O
maltotriose + ?
-
complete conversion to maltotriose
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
specific for pullulan 1,6-glycosidic linkages
-
-
?
pullulan + H2O
maltotriose + ?
-
specific for pullulan 1,6-glycosidic linkages
-
-
?
pullulan + H2O
maltotriose + ?
the enzyme exhibits strict substrate specificity towards pullulan, but shows relatively low activity towards amylopectin and no activity towards other tested polysaccharides
-
-
?
pullulan + H2O
maltotriose + ?
the enzyme hydrolyzes pullulan to yield mainly maltotriose, more than 95%
-
-
?
pullulan + H2O
maltotriose + ?
Priestia megaterium WW1210
the enzyme hydrolyzes pullulan to yield mainly maltotriose, more than 95%
-
-
?
pullulan + H2O
maltotriose + ?
-
higher specific activity against pullulan than against starch. Enzyme attacks only the alpha-1,6 linkages in pullulan
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
higher specific activity against pullulan than against starch. Enzyme attacks only the alpha-1,6 linkages in pullulan
-
-
?
pullulan + H2O
maltotriose + ?
-
higher specific activity against pullulan than against starch. Enzyme attacks only the alpha-1,6 linkages in pullulan
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch + H2O
?
17% of the activity with pullulan
-
-
?
soluble starch + H2O
?
the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides
-
-
?
soluble starch + H2O
?
Geobacillus thermocatenulatus DSMZ730
the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides
-
-
?
soluble starch + H2O
maltotriose + maltose
-
-
-
?
soluble starch + H2O
maltotriose + maltose
-
-
-
?
starch + H2O
?
-
together with amylase, both enzymes immobilized on calcium alginate beads
-
-
?
starch + H2O
?
-
higher specific activity against pullulan than against starch. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
starch + H2O
?
-
higher specific activity against pullulan than against starch. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
starch + H2O
?
-
higher specific activity against pullulan than against starch. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
starch + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
-
-
-
?
starch + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
-
-
-
?
starch + H2O
maltotriose + oligosaccharides
EPZ37738
following immobilization through covalent attachment to three epoxides (ReliZyme EP403/M, ImmobeadIB-150P, and Immobead IB-150A) and an amino-epoxide (ReliZyme HFA403/M), all PulASK derivatives are active on both short and long branches in starch producing reducing sugars (predominantly maltotriose) and oligosaccharides (chain lenght G8 and higher), respectively, a feature that is absent in the free enzyme. Individual or coimmobilization causes changes in the product specificity, presumably due to changes in the enzyme binding pocket caused by the influence of carrier surface properties (hydrophobicor hydrophilic) and the lengths of the spacer arms
-
-
?
starch + H2O
maltotriose + oligosaccharides
Anoxybacillus ayderensis DSM 28779
EPZ37738
following immobilization through covalent attachment to three epoxides (ReliZyme EP403/M, ImmobeadIB-150P, and Immobead IB-150A) and an amino-epoxide (ReliZyme HFA403/M), all PulASK derivatives are active on both short and long branches in starch producing reducing sugars (predominantly maltotriose) and oligosaccharides (chain lenght G8 and higher), respectively, a feature that is absent in the free enzyme. Individual or coimmobilization causes changes in the product specificity, presumably due to changes in the enzyme binding pocket caused by the influence of carrier surface properties (hydrophobicor hydrophilic) and the lengths of the spacer arms
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EPZ37738
the enzyme preferably debranches long branches at alpha-1,6 glycosidic bonds of starch, producing amylose, linear or branched oligosaccharides, but is nonreactive against short branches. In addition, the enzyme acts as limit dextrinase, reaction of EC 3.2.1.142, releasing maltotriose, maltotetraose and maltopentaose from limit dextrin
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EPZ37738
the enzyme preferably debranches long branches at alpha-1,6 glycosidic bonds of starch, producing amylose, linear or branched oligosaccharides, but is nonreactive against short branches. In addition, the enzyme acts as limit dextrinase, reaction of EC 3.2.1.142, releasing maltotriose, maltotetraose and maltopentaose from limit dextrin
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pullulanase is a debranching enzyme which hydrolyses the alpha-1,6-glucosidic linkages in pullulan and other amylaceous polysaccharides
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pullulanase effectively hydrolyzes pullulan, soluble starch and dextran
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the BaPul13A active centre in which hydrolysis of alpha-1,6 linkages occurs with net retention of anomeric configuration, via a covalent glycosyl-enzyme intermediate. Complete starch hydrolysis requires a consortium of enzymes including endo-amylases, glucoamylases and alpha-glucosidases as well as diverse alpha-1,6 cleaving enzymes including pullulanases
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the enzyme hydrolyzes alpha-1,6-glucosidic linkages in polysacchrides
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with glycogen and branched beta-cyclodextrins as substrates, pullulanase shows high-level specificity for the hydrolysis of the outer side chains of glycogen with three to five glucosyl residues. Debranching of the outer side chain of glycogen by pullulanase AmyX
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with glycogen and branched beta-cyclodextrins as substrates, pullulanase shows high-level specificity for the hydrolysis of the outer side chains of glycogen with three to five glucosyl residues. Debranching of the outer side chain of glycogen by pullulanase AmyX
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no substrates: maltotriose, maltose
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no substrates: maltotriose, maltose
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no substrates: maltotriose, maltose
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no substrates: maltotriose, maltose
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negligible activity on wheat flour and maltodextrin, no activity on amylose
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the enzyme has no activity toward alpha-1,4-glycosidic linkages
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the enzyme has no activity toward alpha-1,4-glycosidic linkages
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Geobacillus thermocatenulatus DSMZ730
the enzyme has no activity toward alpha-1,4-glycosidic linkages
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NPDE exhibits a unique catalytic preference for longer malto-oligosaccharides with more than 8 monomers, performing hydrolysis without the transgylcosylation or CD-hydrolyzing activities of other GH-13 enzymes
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NPDE hydrolyzes both alpha-1,4- and alpha-1,6-glucosidic linkages with a substrate specificity in descending order of pullulan, amylopectin, starch, amylose. NPDE has no specificity for alpha-, beta-, and gamma-cyclodextris, and hydrolyzes alpha-1,6-glucosidic linkages more rapidly than alpha-1,4-glucosidic linkages. NPDE hydrolyzes the alpha-1,6 glycosidic linkages of malto-oligosaccharides, molecular basis for the substrate specificity and the catalytic properties, overview
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enzyme exhibits alpha-glucosyltransfer activity and produces an alpha-(1-6) linked compound of two maltotriose molecules from pullulan
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the enzyme does not show activity towards amylose, maltoheptaose, maltohexaose, maltopentaose and maltotetraose
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the enzyme does not show activity towards amylose, maltoheptaose, maltohexaose, maltopentaose and maltotetraose
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Priestia megaterium WW1210
the enzyme does not show activity towards amylose, maltoheptaose, maltohexaose, maltopentaose and maltotetraose
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hydrolyzes the alpha-1,6 linkage in pullulan, alpha-1,4 linkages in amylose and soluble starch. No activity against maltohexaose or other smaller alpha-1,4-linked oligosaccharides
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the enzyme also hydrolyzes oligosaccharides but much slower. The longer the oligosaccharide chain, the higher the hydrolysis rate
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the enzyme also hydrolyzes oligosaccharides but much slower. The longer the oligosaccharide chain, the higher the hydrolysis rate
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hydrolysis of freeze-dried waxy maize starch nanocrystals by pullulanase isoamylase as debranching enzymes and by beta-amylase, cleavage profile, overview
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PulA knock-out strains display decreased binding to epithelial cells
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the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
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the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
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the enzyme cleaves both alpha-1,4- and alpha-1,6-glycosidic linkages in starch, pullulan, amylopectin, and other related oligosaccharides
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the enzyme cleaves both alpha-1,4- and alpha-1,6-glycosidic linkages in starch, pullulan, amylopectin, and other related oligosaccharides
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the enzyme cleaves both alpha-1,4- and alpha-1,6-glycosidic linkages in starch, pullulan, amylopectin, and other related oligosaccharides
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hydrolyzes the alpha-1,6 linkage in pullulan, alpha-1,4 linkages in amylose and soluble starch. No activity against maltohexaose or other smaller alpha-1,4-linked oligosaccharides
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hydrolyzes the alpha-1,6 linkage in pullulan, alpha-1,4 linkages in amylose and soluble starch. No activity against maltohexaose or other smaller alpha-1,4-linked oligosaccharides
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amylopullulanases (type II pullulanases) are able to degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch
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amylopullulanases (type II pullulanases) are able to degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch
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amylopullulanases (type II pullulanases) are able to degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch
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no substrate: amylose. Enzyme displays transglycosylation activity, transferring the maltotriosyl residue of pullulan to aesculin by forming alpha-1,6-glucosidic linkages
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no substrate: amylose. Enzyme displays transglycosylation activity, transferring the maltotriosyl residue of pullulan to aesculin by forming alpha-1,6-glucosidic linkages
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enzyme requires at least two glucose units in linear chain to be released by cleavage of an alpha-1,6-linkage
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