10069
α-Amylase from Bacillus sp.
powder, yellow-brown, ~380 U/mg
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About This Item
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biological source
Bacillus sp.
form
powder
specific activity
~380 U/mg
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
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sustainability
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color
yellow-brown
greener alternative category
, Enabling
storage temp.
2-8°C
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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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
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
J.E. Anderson et al.
Journal of Food Science, 48, 1622-1622 (1983)
Amylase enzyme from Bacillus subtilis S8-18: a potential desizing agent from the marine environment.
Balu Jancy Kalpana et al.
Biotechnology and applied biochemistry, 61(2), 134-144 (2013-05-11)
The present study is aimed at developing an economical medium for the production of α-amylase from Bacillus subtilis S8-18, a marine sediment isolate from Palk Bay, with various agricultural by-products that are cheap and rich in starch. These products include
Chase M Watters et al.
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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
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