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
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-588-1
NACRES:
NA.54
MDL number:
Product Name
α-Amylase from Aspergillus oryzae, powder, ~30 U/mg
form
powder
specific activity
~30 U/mg
mol wt
Mr ~51000
storage temp.
2-8°C
Quality Level
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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.
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).
Other Notes
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).
For the determination of fats in food; Application in (selective) hydrolysis/condensation of glycosidic bonds.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
signalword
Danger
hcodes
Hazard Classifications
Acute Tox. 4 Oral - Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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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
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
Bradford Craigen et al.
The open microbiology journal, 5, 21-31 (2011-07-16)
Staphylococcus aureus, a versatile human pathogen, is commonly associated with medical device infections. Its capacity to establish and maintain these infections is thought to be related to its ability to form adherent biofilms. In this study, commercially available α-amylase compounds
Jian Song et al.
ACS applied bio materials, 2(8), 3448-3457 (2019-08-19)
Solutions of manually purified gastric mucins have been shown to be promising lubricants for biomedical purposes, where they can efficiently reduce friction and wear. However, so far, such mucin solutions have been mostly tested in specific tribological settings, i.e., in
Hanne R Johnsen et al.
International journal of molecular sciences, 15(1), 830-838 (2014-01-15)
Reliable, rapid and inexpensive detection of cellulolytic enzymes that can be used for a wide variety of biological and environmental samples are currently in high demand. Here, a new cellulase detection protocol is described that circumvents problems observed with popular
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