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Information on EC 3.2.1.133 - glucan 1,4-alpha-maltohydrolase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P19531
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3.2.1.133 glucan 1,4-alpha-maltohydrolaseIUBMB Comments
Acts on starch and related polysaccharides and oligosaccharides. The product is alpha-maltose; cf. EC 3.2.1.2 beta-amylase.
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Word Map
- 3.2.1.133
- amylases
-
baking
-
bake
- food industry
- synthesis
- cgtases
- maltooligosaccharide
- amylopectin
-
enzyme-total
- alpha-amylases
-
novozymes
-
staling
- beta-cds
-
crumb
-
stale
-
antistaling
- nutrition
- biotechnology
- medicine
- degradation
- pharmacology
The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
maase, novamyl, maltogenic alpha-amylase, nm404, thermus maltogenic amylase, maus149, gt-mamyiii, maltogenase l, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
maltogenic alpha-amylase
maltogenic alpha-amylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
transglycosylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan alpha-maltohydrolase
Acts on starch and related polysaccharides and oligosaccharides. The product is alpha-maltose; cf. EC 3.2.1.2 beta-amylase.
CAS REGISTRY NUMBER
COMMENTARY
160611-47-2
-
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
acarbose + alpha-D-glucose
isoacarbose
-
transglycosylation
-
-
?
alpha-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
molar ratio 10:1
?
alpha-Schardinger dextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
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
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 + 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
?
D-tagatose + maltotriose
maltosyl-tagatose
-
transglycosylation
-
-
?
gelatinised waxy maize starch + H2O
alpha-maltose + ?
-
-
main product
-
?
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
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
hydrolysis
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
molar ratio 3:1
?
starch + H2O
alpha-maltose + ?
-
exo-acting maltogenic alpha-amylase, removes maltose units from the non-reducing chain ends
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
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
-
?
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
-
-
?
starch + H2O
alpha-maltose + ?
-
exo-acting maltogenic alpha-amylase, removes maltose units from the non-reducing chain ends
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by sulfhydryl reagents, no inhibition with p-chloromercuribenzoate or Schardinger dextrins
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
kinetic properties determined by amount of reducing sugars, assayed according to the dinitrosalicylic acid method
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
hydrolysis of maltotriose, wild-type enzyme and mutant enzymes W177F, W177L, W177N, W177Y and W177S
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6.5
pH 4.0: about 65% of maximal activity, pH 6.5: about 60% of maximal activity, hydrolysis of maltotriose, wild-type enzyme
3.5 - 7
-
about 65% of activity maximum at pH 3.5, about 35% of activity maximum at pH 7.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
55
synthesis reaction performed for 12 h using 500 units/g substrate for transgylcosylation
60
hydrolysis of maltotriose, wild-type enzyme and mutant enzymes W177F, W177L, W177N, and W177S
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
30°C: about 40% of maximal activity, 70°C: about 65% of maximal activity, hydrolysis of maltotriose, mutant enzyme W177Y
50 - 80
50°C: about 70% of maximal activity, 80°C: about 40% of maximal activity, hydrolysis of maltotriose, wild-type enzyme
20 - 80
-
about 20% of activity maximum at 30°C, about 60% of activity maximum at 80°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
maltogenic alpha-amylase precursor, amyM gene
SwissProt
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W177F
transglycosylation activities of the mutant enzyme decreases by 18% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177L
transglycosylation activities of the mutant enzyme decreases by 37% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177N
transglycosylation activities of the mutant enzyme decreases by 45% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177S
transglycosylation activities of the mutant enzyme decreases by 52% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
W177Y
transglycosylation activities of the mutant enzyme decreases by 20% as the hydrophilicity of the residue at position 177 increases. The mutant enzyme exhibits notable enhancements in maltose production. The maltotriose content is substantially lower than that of the syrup produced using the wild-type enzyme
additional information
-
tapioca starch is modified using branching enzyme, BE, isolated from, Bacillus subtilis strain 168, and Bacillus stearothermophilus maltogenic amylase, BSMA. BE cleaves alpha-1,4 linkages of amylose and amylopectin, and moiety of glycosyl residues are transferred to another amylose and amylopectin to produce branched glucan and branching enzyme-treated tapioca starch by forming alpha-1,6 branch linkages. The product is further modified with BSMA to produce highly-branched tapioca starch with 9.7% of extra branch points, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
half-life: 325 h (wild-type enzyme), 95 h (mutant enzyme W177F), 250 h (mutant enzyme W177Y), 200 h (mutant enzyme W177L), 150 h (mutant enzyme W177N), 192 h (mutant enzyme W177S)
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
60 - 70
-
stable at pH 5.5 at 60°C, 25% loss of activity at 70°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterogenous expression in Bacillus subtilis host strain ISW1214
expressed in the periplasm of Escherichia coli BL21(DE3) cells
-
gene amyM cloned in Escherichia coli, transferred with plasmid pDN400 carrier to a Bacillus subtilis 168 host and expressed heterogenously
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
maltogenic alpha-amylase from Bacillus stearothermophilus immobilized onto poly(urethane urea) microparticles shows high storage and thermal stability and reusability for starch hydrolysis. It has a great potential for biotechnology
degradation
microcapsules from poly(vinyl alcohol) and hexamethylene diisocyanate, encapsulated with aqueous solution of maltogenic alpha-amylase from Bacillus stearothermophilus have potential application in biotechnology for saccharification of starch
food industry
maltogenic amylases are used to decrease the maltotriose content of high maltose syrups. However, due to the interplay between the hydrolysis and transglycosylation activities of maltogenic amylases, the maltotriose contents of these syrups are still greater than that necessary for pure maltose preparation. Mutant enzyme W177S, shows decreased transglycosylation activity and enhanced maltose production. It will deliver performance superior to that of the wild-type under industrial conditions
synthesis
production of highly branched amylopectin and amylose from enzymatically modified rice starch
food industry
medicine
-
pierarin (daidzein 8-C-glucoside), can be used to treat coronary heart disease, cardiac infarction, problems in ocular blood flow, sudden deafness, and alcoholism. However puerarin cannot be given by injection due to its low solubility in water. To increase its solubility, puerarin is transglycosylated using Bacillus stearothermophilus maltogenic amylase. Two major transfer products are alpha-D-glucosyl-(1,6)-puerarin and alpha-D-maltosyl-(1,6)-puerarin. The solubility of the transfer products is 14 and 168 times higher than that of puerarin, respectively
nutrition
pharmacology
-
increasing interest for pure maltose in the pharmaceutical industry, maltose may be used instead of D-glucose for intravenous feeding
synthesis
food industry
-
impact on crumb texture, and amylopectin recrystallization: reduction of bread firmness increase during storage compared to control or other amylases, bread firmness is slightly increased at day 0, firmness at day 6 is 9.00, 7.15, and 4.40 N (compared to 16.85 N in control) for BStA dosages of 5.05, 10.1, and 20.2 enzyme units/g flour, respectively, though highest dosage leads to sticky dough and low resilience. Enzyme unit = amount of enzyme releasing 1 micromol maltose/minute at 40°C, pH 6.0, 100 mM sodium maleate buffer with 5.0 mM CaCl2. BStA almost completely suppresses amylopectin recrystallization. Hot water extractable dextrin content is increased largely by BStA
food industry
-
the enzyme is used in baking and brewing industry
food industry
-
transglucosidase (TGAN) in combination with maltogenic alpha-amylase and beta-amylase appears to be advantageous to modulate sweet potato starch properties. The treatment increases the alpha-1, 6 glycosidic linkage ratio and short chain proportions. Decrease in chain length, molecular weight and long chain proportions is noticed. The initial C-type starch polymorphic structure transforms to B-type structure along with decreased crystallinity. Solubility increases substantially with concomitant decrease in viscosity, gelatinization temperature and melting enthalpy. The outcome is believed to open new pathways for regulating the physicochemical properties of sweet potato starch especially by enzyme modification to the design and development of novel sweet potato starch based products
nutrition
-
utilization of starch from corn, cereals, potatoes, sorghum and other plants as valuable raw material for the production of glucose, fructose, oligosaccharides, and alcohol
nutrition
-
production of isomaltosaccharides with various compositions and useful properties is in great demand in the starch industry, efficient process with cooperative action of maltogenic amylase and alpha-glucanotransferase from Thermotoga maritima
synthesis
-
thermostable maltogenic amylase with industrial potential, suitable for producing high maltose syrups from liquefied starch
synthesis
-
industrial processes use heat-stable alpha-amylase for degrading starch
synthesis
-
formation of maltosyl-tagatose from D-tagatose and maltotriose with maltogenic amylase. Glucosyl-tagatose is produced from maltosyl-tagatose by removal of a glucosyl moiety by glucoamylase. Glucosyl-tagatose has potential as a low-calorie sweetener and cryostabilizer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Outtrup, H.; Norman, B.E.
Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-DNA techniques
Starch Staerke
36
405-411
1984
Geobacillus stearothermophilus
-
Diderichsen, B.; Christiansen, L.
Cloning of a maltogenic alpha-amylase from Bacillus stearothermophilus
FEMS Microbiol. Lett.
56
53-60
1988
Geobacillus stearothermophilus, Geobacillus stearothermophilus C599
-
Dauter, Z.; Dauter, M.; Brzozowski, A.M.; Christensen, S.; Borchert, T.V.; Beier, L.; Wilson, K.S.; Davies, G.J.
X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution
Biochemistry
38
8385-8392
1999
Geobacillus stearothermophilus (P19531), Geobacillus stearothermophilus
Kim, J.S.; Cha, S.S.; Kim, H.J.; Kim, T.J.; Ha, N.C.; Oh, S.T.; Cho, H.S.; Cho, M.J.; Kim, M.J.; Lee, H.S.; Kim, J.W.; Choi, K.Y.; Park, K.H.; Oh, B.H.
Crystal structure of a maltogenic amylase provides insights into a catalytic versatility
J. Biol. Chem.
274
26279-26286
1999
Geobacillus stearothermophilus, Thermus sp.
Kim, M.J.; Lee, S.B.; Lee, H.S.; Lee, S.Y.; Baek, J.S.; Kim, D.; Moon, T.W.; Robyt, J.F.; Park, K.H.
Comparative study of the inhibition of alpha-glucosidase, alpha-amylase, and cyclomaltodextrin glucanosyltransferase by acarbose, isoacarbose, and acarviosine-glucose
Arch. Biochem. Biophys.
371
277-283
1999
Geobacillus stearothermophilus
Lee, H.S.; Auh, J.H.; Yoon, H.G.; Kim, M.J.; Park, J.H.; Hong, S.S.; Kang, M.H.; Kim, T.J.; Moon, T.W.; Kim, J.W.; Park, K.H.
Cooperative action of alpha-glucanotransferase and maltogenic amylase for an improved process of isomaltooligosaccharide (IMO) production
J. Agric. Food Chem.
50
2812-2817
2002
Geobacillus stearothermophilus
Li, D.; Park, S.H.; Shim, J.H.; Lee, H.S.; Tang, S.Y.; Park, C.S.; Park, K.H.
In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase
Carbohydr. Res.
339
2789-2797
2004
Geobacillus stearothermophilus
Roh, H.; Kang, S.; Lee, H.; Kim, D.; Byun, S.; Lee, S.; Park, K.
Transglycosylation of tagatose with maltotriose by Bacillus stearothermophilus maltogenic amylase (BSMA)
Tetrahedron
16
77-82
2005
Geobacillus stearothermophilus
-
Lee, C.K.; Le, Q.T.; Kim, Y.H.; Shim, J.H.; Lee, S.J.; Park, J.H.; Lee, K.P.; Song, S.H.; Auh, J.H.; Lee, S.J.; Park, K.H.
Enzymatic synthesis and properties of highly branched rice starch amylose and amylopectin cluster
J. Agric. Food Chem.
56
126-131
2008
Geobacillus stearothermophilus (P19531)
Goesaert, H.; Leman, P.; Bijttebier, A.; Delcour, J.A.
Antifirming effects of starch degrading enzymes in bread crumb
J. Agric. Food Chem.
57
2346-2355
2009
Geobacillus stearothermophilus
Li, D.; Park, J.T.; Li, X.; Kim, S.; Lee, S.; Shim, J.H.; Park, S.H.; Cha, J.; Lee, B.H.; Kim, J.W.; Park, K.H.
Overexpression and characterization of an extremely thermostable maltogenic amylase, with an optimal temperature of 100 degrees C, from the hyperthermophilic archaeon Staphylothermus marinus
New Biotechnol.
27
300-307
2010
Geobacillus stearothermophilus
Bijttebier, A.; Goesaert, H.; Delcour, J.
Hydrolysis of amylopectin by amylolytic enzymes: structural analysis of the residual amylopectin population
Carbohydr. Res.
345
235-242
2010
Geobacillus stearothermophilus
Miao, M.; Xiong, S.; Ye, F.; Jiang, B.; Cui, S.W.; Zhang, T.
Development of maize starch with a slow digestion property using maltogenic alpha-amylase
Carbohydr. Polym.
103
164-169
2014
Geobacillus stearothermophilus
Derde, L.J.; Gomand, S.V.; Courtin, C.M.; Delcour, J.A.
Characterisation of three starch degrading enzymes: thermostable beta-amylase, maltotetraogenic and maltogenic alpha-amylases
Food Chem.
135
713-721
2012
Geobacillus stearothermophilus
Van Steertegem, B.; Pareyt, B.; Brijs, K.; Delcour, J.A.
Combined impact of Bacillus stearothermophilus maltogenic alpha-amylase and surfactants on starch pasting and gelation properties
Food Chem.
139
1113-1120
2013
Geobacillus stearothermophilus
Samant, S.; Gupta, G.; Karthikeyan, S.; Haq, S.F.; Nair, A.; Sambasivam, G.; Sukumaran, S.
Effect of codon-optimized E. coli signal peptides on recombinant Bacillus stearothermophilus maltogenic amylase periplasmic localization, yield and activity
J. Ind. Microbiol. Biotechnol.
41
1435-1442
2014
Geobacillus stearothermophilus
Straksys, A.; Kochane, T.; Budriene, S.
Catalytic properties of maltogenic alpha-amylase from Bacillus stearothermophilus immobilized onto poly(urethane urea) microparticles
Food Chem.
211
294-299
2016
Geobacillus stearothermophilus (P19531)
Guo, L.; Tao, H.; Cui, B.; Janaswamy, S.
The effects of sequential enzyme modifications on structural and physicochemical properties of sweet potato starch granules
Food Chem.
277
504-514
2019
Geobacillus stearothermophilus
Sun, Y.; Duan, X.; Wang, L.; Wu, J.
Enhanced maltose production through mutagenesis of acceptor binding subsite +2 in Bacillus stearothermophilus maltogenic amylase
J. Biotechnol.
217
53-61
2016
Geobacillus stearothermophilus (P19531)
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