3.2.1.133: glucan 1,4-alpha-maltohydrolase
This is an abbreviated version!
For detailed information about glucan 1,4-alpha-maltohydrolase, go to the full flat file.
Word Map on EC 3.2.1.133
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3.2.1.133
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amylases
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baking
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bake
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food industry
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synthesis
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cgtases
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maltooligosaccharide
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amylopectin
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enzyme-total
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alpha-amylases
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novozymes
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staling
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beta-cds
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crumb
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stale
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antistaling
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nutrition
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biotechnology
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medicine
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degradation
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pharmacology
- 3.2.1.133
- amylases
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baking
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bake
- food industry
- synthesis
- cgtases
- maltooligosaccharide
- amylopectin
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enzyme-total
- alpha-amylases
-
novozymes
-
staling
- beta-cds
-
crumb
-
stale
-
antistaling
- nutrition
- biotechnology
- medicine
- degradation
- pharmacology
Reaction
Synonyms
alpha-amylase, AmyB, BbmA, BSMA, BSTA, BTMA, CAZy-GH13, glucan 1,4-alpha-maltohydrolase, glucan-1,4-alpha-maltohydrolase, Gt-MamyIII, LGMA, MAase, MABS, MAG1, maltogenase L, maltogenic alpha-amylase, maltogenic amylase, maltose-forming alpha-amylase, MAmy, MAUS149, More, NM319, NM326, NM398, NM404, NM447, Novamyl, PSMA, Smar_0613, SMMA, TCMA, Thermus maltogenic amylase, ThMA, TK4MA
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Application
Application on EC 3.2.1.133 - glucan 1,4-alpha-maltohydrolase
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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
medicine
nutrition
pharmacology
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increasing interest for pure maltose in the pharmaceutical industry, maltose may be used instead of D-glucose for intravenous feeding
synthesis
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natural design of the transglycosylation activtiy of the enzyme at high concentrations of acceptor sugar molecules may now be altered for biotechnological applications to produce branched oligosaccharides with higher efficiency
biotechnology
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producing enzymes with modified substrate specificity, hydrolysis, and transglycosilation activities, as a way to produce specific functional carbohydrate materials
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
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Novamyl is currently used in the baking industry as an anti-staling agent in breads at neutral or near neutral pH. It is rapidly inactivated during the baking process. Relative to the Novamyl wild-type the variants exhibit more than 10°C increase in thermal stability at pH 4.5, improving the anti-staling effect
food industry
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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
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wild-type enzyme is not thermostable at low pH as encountered in recipes such as sourdough and rye dough, recombined variants increase thermal stability more than 10°C at pH 4.0-4.5, application test is performed with wheat flour dough at pH 5.5-5.9 and sourdough at pH 4.0-4.3 baked at 230°C for 22 min, firmness and elasticity tested at days 1, 3, and 7 after baking and vacuum packing
food industry
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the enzyme is used for the production of maltose syrup from starch
food industry
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the enzyme is used in baking and brewing industry
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
food industry
the enzyme has many potential applications in food processing
food industry
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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
food industry
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Novamyl is currently used in the baking industry as an anti-staling agent in breads at neutral or near neutral pH. It is rapidly inactivated during the baking process. Relative to the Novamyl wild-type the variants exhibit more than 10°C increase in thermal stability at pH 4.5, improving the anti-staling effect
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food industry
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wild-type enzyme is not thermostable at low pH as encountered in recipes such as sourdough and rye dough, recombined variants increase thermal stability more than 10°C at pH 4.0-4.5, application test is performed with wheat flour dough at pH 5.5-5.9 and sourdough at pH 4.0-4.3 baked at 230°C for 22 min, firmness and elasticity tested at days 1, 3, and 7 after baking and vacuum packing
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food industry
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the enzyme has many potential applications in food processing
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synthesis of acarvisione-simmondsin, a novel compound with both antiobesity and hypoglycemic activity
medicine
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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
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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
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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
nutrition
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transglycosylation activity of BbmA can be applied for the preparation of branched oligosaccharide mixtures, which are used as low calorie sweeteners or humectants
nutrition
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utilization of starch from corn, cereals, potatoes, sorghum and other plants as valuable raw material for the production of glucose, fructose, oligosaccharides, and alcohol
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nutrition
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transglycosylation activity of BbmA can be applied for the preparation of branched oligosaccharide mixtures, which are used as low calorie sweeteners or humectants
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thermostable maltogenic amylase with industrial potential, suitable for producing high maltose syrups from liquefied starch
synthesis
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industrial processes use heat-stable alpha-amylase for degrading starch
synthesis
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heterologous protein expression in Escherichia coli may contribute to better industrial production of maltogenic amylase
synthesis
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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
synthesis
production of highly branched amylopectin and amylose from enzymatically modified rice starch
synthesis
the purified enzyme is employed to catalyze genistin glycosylation using gamma-cyclodextrin as both glucosyl donor and solubilizer
synthesis
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industrial processes use heat-stable alpha-amylase for degrading starch
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synthesis
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heterologous protein expression in Escherichia coli may contribute to better industrial production of maltogenic amylase
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synthesis
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the purified enzyme is employed to catalyze genistin glycosylation using gamma-cyclodextrin as both glucosyl donor and solubilizer
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