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10069

Sigma-Aldrich

α-Amylase from Bacillus sp.

greener alternative

powder, yellow-brown, ~380 U/mg

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About This Item

Numéro CAS:
9000-90-2
Numéro de classification (Commission des enzymes):
3.2.1.1 (BRENDA, IUBMB)
Numéro CE :
232-565-6
Numéro MDL:
MFCD00081319
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Source biologique

Bacillus sp.

Niveau de qualité

100

Forme

powder

Activité spécifique

~380 U/mg

Caractéristiques du produit alternatif plus écologique

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

sustainability

Greener Alternative Product

Couleur

yellow-brown

Autre catégorie plus écologique

, Enabling

Température de stockage

2-8°C

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Description générale

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

Actions biochimiques/physiologiques

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.

Définition de l'unité

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)

Autres remarques

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

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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)
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
P.L. Chang Rupp et al.
Journal of Food Biochemistry, 12, 191-191 (1988)
Slavica Djonović et al.
PLoS pathogens, 9(3), e1003217-e1003217 (2013-03-19)
Pseudomonas aeruginosa strain PA14 is a multi-host pathogen that infects plants, nematodes, insects, and vertebrates. Many PA14 factors are required for virulence in more than one of these hosts. Noting that plants have a fundamentally different cellular architecture from animals
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