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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:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Source biologique

Bacillus sp.

Niveau de qualité

Forme

powder

Activité spécifique

~380 U/mg

Caractéristiques du produit alternatif plus écologique

Waste Prevention
Design for Energy Efficiency
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sustainability

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Couleur

yellow-brown

Autre catégorie plus écologique

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

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

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

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
Shaomin Yan et al.
Microbial cell factories, 16(1), 124-124 (2017-07-21)
Amylase plays an important role in biotechnology industries, and Gram-positive bacterium Bacillus subtilis is a major host to produce heterogeneous α-amylases. However, the secretion stress limits the high yield of α-amylase in B. subtilis although huge efforts have been made
P.L. Chang Rupp et al.
Journal of Food Biochemistry, 12, 191-191 (1988)
Cold-water solubility, oil-adsorption and enzymolysis properties of amorphous granular starches
Fang C, et al.
Food Hydrocolloids, 117, 106669-106669 (2021)
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

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