A2986
Amylase, Maltogenic from Bacillus sp.
Synonym(s):
Novamyl 1000BG, Glucan 1,4-α-maltohydrolase, Maltogenic Amylase
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About This Item
Recommended Products
biological source
Bacillus sp.
Quality Level
form
solid
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
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greener alternative category
storage temp.
2-8°C
Related Categories
General description
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in starch ethanol research. For more information see the article in biofiles.
Application
Maltogenic amylases (MAse) are commonly used in the starch industry. They are used to hydrolyze starch, pullulan and cyclodextrin and to make novel carbohydrates .
Biochem/physiol Actions
Maltogenic amylase is in the amylolytic enzyme subfamily, which also consists of cyclomaltodextrinase, neopullulanase, and Thermoactinomyces vulgaris amylase II. These enzymes transfer the hydrolyzed sugar moiety to another sugar molecule. They have an (α/β)8 barrel and C domain as well as a 124-residue N domain, which is involved in homodimer formation .
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Aubrey Jones et al.
Journal of biotechnology, 134(3-4), 325-333 (2008-03-25)
Directed evolution coupled with a high-throughput robotic screen was employed to broaden the industrial use of the maltogenic alpha-amylase Novamyl from Bacillus sp. TS-25. Wild-type Novamyl is currently used in the baking industry as an anti-staling agent in breads baked
Sung-Hoon Park et al.
Biochimica et biophysica acta, 1751(2), 170-177 (2005-06-25)
The goal of this study was to develop a maltose-producing enzyme using protein engineering and to clarify the relation between the substrate specificity and the structure of the substrate-binding site of dimeric maltogenic amylase isolated from Thermus (ThMA). Ala290 at
Young-Wan Kim et al.
Applied and environmental microbiology, 69(8), 4866-4874 (2003-08-07)
The thermostability of maltogenic amylase from Thermus sp. strain IM6501 (ThMA) was improved greatly by random mutagenesis using DNA shuffling. Four rounds of DNA shuffling and subsequent recombination of the mutations produced the highly thermostable mutant enzyme ThMA-DM, which had
Dan Li et al.
New biotechnology, 27(4), 300-307 (2010-04-14)
A gene encoding a hyperthermostable maltogenic amylase of Staphylothermus marinus (SMMA) was cloned and overexpressed in Escherichia coli. SMMA consisted of 696 amino acids with a predicted molecular mass of 82.5 kDa. The enzyme was active in acidic conditions (pH
Deepika Mehta et al.
PloS one, 8(9), e73612-e73612 (2013-09-27)
Maltogenic amylases belong to a subclass of cyclodextrin-hydrolyzing enzymes and hydrolyze cyclodextrins more efficiently than starch unlike typical α-amylases. Several bacterial malto-genic amylases with temperature optima of 40-60°C have been previously characterized. The thermo-adaption, substrate preferences and transglycosylation aspects of
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