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A4862

Sigma-Aldrich

α-Amylase from Bacillus sp.

liquid

Sinónimos:

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

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About This Item

Número de CAS:
9000-85-5
Comisión internacional de enzimas:
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

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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)
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)
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)
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Protocolos

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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