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10069

Sigma-Aldrich

α-Amylase from Bacillus sp.

greener alternative

powder, yellow-brown, ~380 U/mg

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

biological source

Bacillus sp.

Quality Level

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.

color

yellow-brown

greener alternative category

storage temp.

2-8°C

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This Item
A6380A1031A0521
α-Amylase from Bacillus sp. powder, yellow-brown, ~380 U/mg

10069

α-Amylase from Bacillus sp.

α-Amylase from Bacillus sp. Type II-A, lyophilized powder, ≥1,500 units/mg protein (biuret)

A6380

α-Amylase from Bacillus sp.

α-Amylase from human saliva Type XIII-A, lyophilized powder, 300-1,500 units/mg protein

A1031

α-Amylase from human saliva

α-Amylase from human saliva Type IX-A, lyophilized powder, 1,000-3,000 units/mg protein

A0521

α-Amylase from human saliva

specific activity

~380 U/mg

specific activity

≥1,500 units/mg protein (biuret)

specific activity

300-1,500 units/mg protein

specific activity

1,000-3,000 units/mg protein

form

powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

100

Quality Level

200

Quality Level

200

Quality Level

200

color

yellow-brown

color

-

color

-

color

-

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


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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
Chase M Watters et al.
Infection and drug resistance, 9, 71-78 (2016-05-14)
Enzymatic debridement is a therapeutic strategy used clinically to remove necrotic tissue from wounds. Some of the enzymes utilized for debridement have been tested against bacterial pathogens, but the effectiveness of these agents in dispersing clinically relevant biofilms has not
P Colonna et al.
Biotechnology and bioengineering, 31(9), 895-904 (1988-06-05)
Native starch granules from wheat have been subjected to enzymatic depolymerization with an alpha-amylase from Bacillus subtilis. Crystallites made from short-chain amylose and residues from mild acid hydrolysis have been also tested. Electron microscopy, particle size analysis, DSC, and x-ray
J.E. Anderson et al.
Journal of Food Science, 48, 1622-1622 (1983)
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)

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