10065
α-Amylase from Aspergillus oryzae
powder, ~30 U/mg
Synonyme(s) :
1,4-α-D-Glucane-glucanohydrolase
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A propos de cet article
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-588-1
NACRES:
NA.54
MDL number:
Specific activity:
~30 U/mg
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Laissez-nous vous aiderNom du produit
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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Catégories apparentées
Other Notes
Pour en savoir plus sur les enzymes utilisées dans l′analyse des glucides complexes, rendez-vous sur www.sigma-aldrich.com/enzymeexplorer.
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.
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).
signalword
Danger
hcodes
Hazard Classifications
Acute Tox. 4 Oral - Resp. Sens. 1
Classe de stockage
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
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
Mamadou Abdoulaye Konaré et al.
Plants (Basel, Switzerland), 12(2) (2023-01-22)
Currently, microencapsulation has become a viable method of nutrient delivery for the food industry. This work microencapsulated the bioactive compounds extracted from two neglected species (Balanites aegyptiaca and Ziziphus mauritiana) by freeze-drying. A combination of wall materials (whey protein and
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
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