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Sigma-Aldrich

α-Amylase from Aspergillus oryzae

powder, ~30 U/mg

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Synonym(s):
1,4-α-D-Glucan-glucanohydrolase
Enzyme Commission number:
3.2.1.1 (BRENDA, IUBMB)
EC Number:
232-588-1
MDL number:
MFCD00081319
eCl@ss:
32160410
NACRES:
NA.54

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.

Pictograms

Exclamation markHealth hazard
GHS07,GHS08

Signal Word

Danger

Hazard Statements

H302 - H334

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

Regulatory Information

常规特殊物品

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Han Tao et al.
Food chemistry, 190, 588-593 (2015-07-28)
The wheat dough was subjected to freezing/thawing treatment for 0, 3, 7, and 10 cycles and fractionated into non-gluten proteins and starch. High-performance liquid chromatography revealed changes in molecular mass distribution occurred for the extracted non-gluten proteins. As for the
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)
In higher plants the production of starch is orchestrated by chloroplast-localized biosynthetic enzymes, namely starch synthases, ADP-glucose pyrophosphorylase, and starch branching and debranching enzymes. Diurnal regulation of these enzymes, as well as starch-degrading enzymes, influences both the levels and composition
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
C E Daugherty et al.
Journal - Association of Official Analytical Chemists, 66(4), 927-932 (1983-07-01)
A chloroform-methanol extraction method (complete extraction of fat in 3 min) for determining fat in processed and prepared foods has been studied collaboratively. Fourteen collaborators reported single replicate fat results on 7 samples representative of various food types and 2
Han Tao et al.
Food chemistry, 265, 18-22 (2018-06-10)
Properties of starches isolated from soft and hard wheat dough after freezing/thawing (F/T) treatment were investigated. Significance of results was observed between isolated hard wheat starch (HWS) and soft wheat starch (SWS), but both cultivars showed an increase in the
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