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A2986

Sigma-Aldrich

Amylase, Maltogenic from Bacillus sp.

greener alternative

Synonym(s):

Novamyl 1000BG, Glucan 1,4-α-maltohydrolase, Maltogenic Amylase

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

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

Greener Alternative Product

greener alternative category

storage temp.

2-8°C

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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Tae-Yang Jung et al.
The Journal of biological chemistry, 287(11), 7979-7989 (2012-01-10)
Staphylothermus marinus maltogenic amylase (SMMA) is a novel extreme thermophile maltogenic amylase with an optimal temperature of 100 °C, which hydrolyzes α-(1-4)-glycosyl linkages in cyclodextrins and in linear malto-oligosaccharides. This enzyme has a long N-terminal extension that is conserved among
J L Uma Maheswar Rao et al.
Applied biochemistry and biotechnology, 142(2), 179-193 (2007-11-21)
The purified alpha-amylase of Geobacillus thermoleovorans had a molecular mass of 26 kDa with a pI of 5.4, and it was optimally active at 100 degrees C and pH 8.0. The T 1/2 of alpha-amylase at 100 degrees C increased
Jae-Hoon Shim et al.
Journal of bacteriology, 191(15), 4835-4844 (2009-05-26)
The physiological functions of two amylolytic enzymes, a maltogenic amylase (MAase) encoded by yvdF and a debranching enzyme (pullulanase) encoded by amyX, in the carbohydrate metabolism of Bacillus subtilis 168 were investigated using yvdF, amyX, and yvdF amyX mutant strains.
Jae-Hoon Shim et al.
Protein engineering, design & selection : PEDS, 17(3), 205-211 (2004-04-21)
In an effort to improve the properties of cyclodextrin glucanotransferase (CGTase) as an antistaling enzyme, error-prone PCR was used to introduce random mutations into a CGTase cloned from alkalophilic Bacillus sp. I-5 (CGTase I-5). A mutant CGTase[3-18] with the three
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

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