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A2986

Amylase, maltogen aus Bacillus sp.

greener alternative

Synonym(e):

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

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10 G

€ 67,10

50 G

€ 182,00

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Über diesen Artikel

UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
EG-Nummer:
3.2.1.133 (BRENDA, IUBMB)
Biological source:
Bacillus sp.

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Unterstützung erhalten

biological source

Bacillus sp.

form

solid

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greener alternative category

Enabling,

storage temp.

2-8°C

Quality Level

200

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Dieser Artikel
A4551A759510070
Amylase, Maltogenic from Bacillus sp.

Sigma-Aldrich

A2986

Amylase, Maltogenic from Bacillus sp.

α-Amylase from Bacillus licheniformis lyophilized powder, 500-1,500 units/mg protein, 93-100% (SDS-PAGE)

Sigma-Aldrich

A4551

α-Amylase from Bacillus licheniformis

α-Amylase from Bacillus amyloliquefaciens liquid, ≥250 units/g

Sigma-Aldrich

A7595

α-Amylase from Bacillus amyloliquefaciens

α-Amylase from Bacillus sp. powder, yellow-brown, ~50 U/mg

Sigma-Aldrich

10070

α-Amylase from Bacillus sp.

biological source

Bacillus sp.

biological source

Bacillus licheniformis

biological source

-

biological source

-

form

solid

form

lyophilized powder

form

liquid

form

powder

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

100

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

sustainability

Greener Alternative Product

sustainability

Greener Alternative Product

sustainability

Greener Alternative Product

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 [1].

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 [1].

Lagerklasse

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Hier finden Sie alle aktuellen Versionen:

Analysenzertifikate (COA)

Lot/Batch Number
0000507536
0000507536
0000498444
0000498444
0000381846

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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
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
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
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
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