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A4862

Sigma-Aldrich

α-Amylase from Bacillus sp.

liquid

Synonym(s):

1,4-α-D-glucan glucanohydrolase, 1,4-alpha-D-glucan glucanohydrolase, Termamyl® 300L, alpha-amylase, endoglucanase

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About This Item

CAS Number:
9000-85-5
Enzyme Commission number:
3.2.1.1 (BRENDA, IUBMB)
MDL number:
MFCD00081319
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Bacillus sp.

Quality Level

200

form

liquid

storage temp.

2-8°C

General description

α-Amylase belongs to glycosyl hydrolase family 13. It comprises of A, B and C domains. Domain A has two aspartic acid and a glutamic acid as catalytic residues. Domain B possesses Ca2+ and Na+ binding sites.

Application

α-Amylase from Bacillus sp. has been used in the digestion of lyophilized microalgae sample. It has also been used to evaluate α-amylase inhibitory activity in marine algae samples and Myrmecodia platytyrea.

Biochem/physiol Actions

α-Amylase hydrolyzes the polysaccharides starch, malto-oligosaccharides at the α-d-(1,4)-glucosidic linkages to α-anomeric products. It has wide applications in industries including food, pharmaceutical, textile and paper.

Unit Definition

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

Legal Information

A product of Novozyme Corp.
Termamyl is a registered trademark of Novozymes Corp.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000315139
0000315138
0000299793
0000299794
0000270126

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Microalgae Characterization for Consolidated and New Application in Human Food, Animal Feed and Nutraceuticals
Molino A, et al.
International Journal of Environmental Research and Public Health, 15(11), 2436-2436 (2018)
Crystal structure of Bacillus subtilis alpha-amylase in complex with acarbose
Kagawa M, et al.
Journal of Bacteriology, 185(23), 6981-6984 (2003)
Improving the reversibility of thermal denaturation and catalytic efficiency of Bacillus licheniformis alpha-amylase through stabilizing a long loop in domain B
Li Z, et al.
PLoS ONE, 12(3), e0173187-e0173187 (2017)
Snezana Agatonovic-Kustrin et al.
Marine drugs, 17(3) (2019-03-06)
Marine organisms produce an array of biologically active natural products, many of which have unique structures that have not been found in terrestrial organisms. Hence, marine algae provide a unique source of bioactive compounds. The present study investigated 19 marine
High-performance thin-layer chromatography-direct bioautography as a method of choice for alpha-amylase and antioxidant activity evaluation in marine algae
Agatonovic-Kustrin S and Morton DW
Journal of Chromatography A, 1530, 197-203 (2017)
View All Related Papers

Protocols

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

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