10065
α-Amylase from Aspergillus oryzae
powder, ~30 U/mg
Synonym(s):
1,4-α-D-Glucan-glucanohydrolase
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About This Item
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
Recommended Products
form
powder
specific activity
~30 U/mg
mol wt
Mr ~51000
storage temp.
2-8°C
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General description
Microbial amylases are exoenzymes and are used in several industrial applications, such as production of bread, maltose syrups, and fermentation of soya sauce, miso etc. α-Amylase isolated from Aspergillus oryzae has been found to have molecular weights of 51kDa (sedimentation and diffusion) and 49kDa (gel filtration).
Application
α-Amylase has been used:
- as a control enzyme in agar plate-based and carboxymethylcellulose-based clearing assays to screen cellulase activity
- for the hydrolysis of starch to explore the the role of wheat starch in frozen dough
- to inhibit Staphylococcus aureus biofilms
Biochem/physiol Actions
Aspergillus oryzae α-amylase (Ao α-amylase) enzyme catalyzes the hydrolysis of the α-1,4 glycosidic bonds in soluble starches and related subsrates. These substrates are broken down to release short oligosaccharides and α-limit dextrins.
Unit Definition
1 U corresponds to the amount of enzyme which liberates 1 μmol maltose per minute at pH 6.0 and 25°C (starch acc. to Zulkowsky, Cat. No. 85642, as substrate).
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
For the determination of fats in food; Application in (selective) hydrolysis/condensation of glycosidic bonds.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Acute Tox. 4 Oral - Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
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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S Wirsel et al.
Molecular microbiology, 3(1), 3-14 (1989-01-01)
We have cloned three genes (amy1, amy2 and amy3) encoding alpha-amylase in the filamentous fungus Aspergillus oryzae. The established overall sequences have a very high degree of homology, showing divergences mainly in the 3'-untranslated regions. The positions and the sequences
P C Sehnke et al.
Proceedings of the National Academy of Sciences of the United States of America, 98(2), 765-770 (2001-01-10)
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