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10069

Sigma-Aldrich

α-Amylase aus Bacillus sp.

greener alternative

powder, yellow-brown, ~380 U/mg

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About This Item

CAS-Nummer:
9000-90-2
EC-Nummer:
3.2.1.1 (BRENDA, IUBMB)
EG-Nummer:
232-565-6
MDL-Nummer:
MFCD00081319
UNSPSC-Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

Biologische Quelle

Bacillus sp.

Qualitätsniveau

100

Form

powder

Spezifische Aktivität

~380 U/mg

Grünere Alternativprodukt-Eigenschaften

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

sustainability

Greener Alternative Product

Farbe

yellow-brown

Grünere Alternativprodukt-Kategorie

, Enabling

Lagertemp.

2-8°C

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Allgemeine Beschreibung

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.

Anwendung

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. Wirkung

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.

Einheitendefinition

1 U entspricht der Enzymmenge, die 1 μmol Maltose pro Minute bei pH 6.9 und 25°C freisetzt (Stärke nach Zulkowsky, Fluka®-Nr. 85642, als Substrat)

Sonstige Hinweise

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

Piktogramme

Health hazard
GHS08

Signalwort

Danger

H-Sätze

H334

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

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

Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

P.L. Chang Rupp et al.
Journal of Food Biochemistry, 12, 191-191 (1988)
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
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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