Skip to Content
MilliporeSigma
All Photos(2)

Documents

10069

Sigma-Aldrich

α-Amylase from Bacillus sp.

greener alternative

powder, yellow-brown, ~380 U/mg

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

Bacillus sp.

form

powder

specific activity

~380 U/mg

greener alternative product characteristics

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

sustainability

Greener Alternative Product

color

yellow-brown

greener alternative category

storage temp.

2-8°C

Looking for similar products? Visit Product Comparison Guide

General description

α-Amylase (α-1,4-glucan-4-glucanohydrolase) belongs to the glycosyl hydrolase family 13. The two aspartic residues and one glutamic acid residue are the prime catalytic residues of α-amylase. All amylases have three domain regions, namely, domain A with a central (β/α)8 barrel, domain B, and β-structure with a Greek key motif encompassing domain C.
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 hydrolysis research. For more information see the article in biofiles.

Application

α-Amylase from Bacillus sp. has been used:
  • as a dispersal enzyme to test degradation of S. aureus biofilms,
  • in the enzymatic hydrolysis of tapioca starch
  • in the enzymolysis of plant-based native and the amorphous granular starches

Biochem/physiol Actions

α-Amylase mediates the hydrolysis of starch, malto-oligosaccharides, and glycogen at the α-D-(1,4)-glucosidic linkages. Bacillus sp. serve as an important cell factory for the heterogeneous production of α-amylase. An extracellular secreted thermostable amylase from the Bacillus subtilis strain has also been reported.

Unit Definition

One unit is the amount of enzyme which liberates 1 μmole of maltose per minute at pH 6.9 and 25°C (using Cat. No. 85642 as substrate)

Other Notes

Heat stability of bacterial α-amylases; Action pattern on sweet potato starch, amylose and amylopectin; Action on native wheat starch.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, 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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Masayuki Kagawa et al.
Journal of bacteriology, 185(23), 6981-6984 (2003-11-18)
The crystal structure of Bacillus subtilis alpha-amylase, in complex with the pseudotetrasaccharide inhibitor acarbose, revealed an hexasaccharide in the active site as a result of transglycosylation. After comparison with the known structure of the catalytic-site mutant complexed with the native
Junrong Huang et al.
Carbohydrate polymers, 163, 324-329 (2017-03-08)
After combined hydrolysis by α-amylase and β-amylase at room temperature, spherical blocklets in diameters of 27-60nm were observed on the surface of tapioca starch granules by scanning electron micrography (SEM). Tapioca starch (1%, w/w, db, distilled water) was heated by
Cold-water solubility, oil-adsorption and enzymolysis properties of amorphous granular starches
Fang C, et al.
Food Hydrocolloids, 117, 106669-106669 (2021)
P.L. Chang Rupp et al.
Journal of Food Biochemistry, 12, 191-191 (1988)
Hydrolysis of starches by the action of an alpha-amylase from Bacillus subtilis
Konsula Z and Liakopoulou-Kyriakides M
Process Biochemistry (Oxford, United Kingdom), 39, 1745-1749 (2004)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service