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A2771

Sigma-Aldrich

α-Amylase from barley malt

greener alternative

Type VIII-A, powder

Synonym(s):

1,4-α-D-Glucan-glucanohydrolase

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About This Item

CAS Number:
9000-90-2
Enzyme Commission number:
3.2.1.1 (BRENDA, IUBMB)
EC Number:
232-565-6
MDL number:
MFCD00081319
UNSPSC Code:
12352204

type

Type VIII-A

form

powder

α-amylase activity

≥1 unit/mg solid

β-amylase activity

≥1 unit/mg solid

contains

lactose as extender

greener alternative product characteristics

Waste Prevention: Greener alternative product characteristics
Learn more about the Principles of Green Chemistry.

greener alternative category

Enabling

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 waste prevention when used in starch ethanol research. For more information see the article in biofiles.

Packaging

Package size based on α-amylase activity

Unit Definition

One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.

Other Notes

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

substrate

Product No.
Description
Pricing

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P342 + P311

Hazard Classifications

Resp. Sens. 1

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Sigma-Aldrich

G5003

α-Glucosidase from Saccharomyces cerevisiae

André M N Silva et al.
Archives of biochemistry and biophysics, 530(1), 23-31 (2012-12-19)
The study of protein damage by oxidative processes and its influence on protein activity is central to understanding the deleterious effects of oxidative stress on biological systems. This paper will focus on the study of enzyme inactivation by oxidative modifications
Jie-Lun Hu et al.
International journal of biological macromolecules, 54, 264-269 (2012-12-19)
Effects of a novel polysaccharide (PLP) from the seeds of Plantago asiatica L. on intestinal function were investigated in vitro. Results showed that PLP had notable influence on slowing down glucose diffusion and inhibiting α-amylase activity. These might help prolong
Jean-Luc Da Lage et al.
BMC evolutionary biology, 13, 40-40 (2013-02-15)
Increasing genome data show that introns, a hallmark of eukaryotes, already existed at a high density in the last common ancestor of extant eukaryotes. However, intron content is highly variable among species. The tempo of intron gains and losses has
Gang-hua Lang et al.
Bioscience, biotechnology, and biochemistry, 77(1), 126-131 (2013-01-08)
The influence of different extraction solutions on the proteins extracted from rice grains was investigated. The largest amounts of salt-soluble proteins were extracted with solutions supplemented with Tris-HCl at pH 8.0. Rice allergens were analyzed by multiplex immunodetection. Except for
Simone Holligan et al.
Comparative biochemistry and physiology. Part D, Genomics & proteomics, 8(1), 65-71 (2013-01-01)
We used a proteomics-based approach to investigate potential regulatory proteins in the pancreas of domestic cattle (Bos taurus) that were associated with differences in pancreatic α-amylase activity. Two groups of 48 and 45 crossbred steers in years 1 and 2
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