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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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T J Kim et al.
Biochemistry, 40(47), 14182-14190 (2001-11-21)
The relation between the quaternary structure and the substrate specificity of Thermus maltogenic amylase (ThMA) has been investigated. Sedimentation diffusion equilibrium ultracentrifugation and gel filtration analyses, in combination with the crystal structure determined recently, have demonstrated that ThMA existed in
Lili Kandra et al.
Carbohydrate research, 340(7), 1311-1317 (2005-04-28)
Synthesis of acarviosinyl-isomaltosyl-spiro-thiohydantoin in yields up to 20%, has been achieved by Bacillus stearothermophilus maltogenic amylase (BSMA). BSMA is capable of transferring the acarviosine-glucose residue from an acarbose donor onto glucopyranosylidene-spiro-thiohydantoin. Reactions were followed using HPLC and MALDI-TOF MS. 1H
Hee-Seob Lee et al.
The Journal of biological chemistry, 277(24), 21891-21897 (2002-03-30)
Over 20 enzymes denoted as cyclomaltodextrinase, maltogenic amylase, or neopullulanase that share 40-86% sequence identity with each other are found in public data bases. These enzymes are distinguished from typical alpha-amylases by containing a novel N-terminal domain and exhibiting preferential
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.
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

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