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[Denaturation stabilization of alpha-amylase from Aspergillus oryzae]

https://arctichealth.org/en/permalink/ahliterature13264
Source
Ukr Biokhim Zh. 1975 Jul-Aug;47(4):453-7
Publication Type
Article
Author
O S Tsyperovych
I P Halych
L O Kloesnyk
H H Artyukh
Source
Ukr Biokhim Zh. 1975 Jul-Aug;47(4):453-7
Language
Ukrainian
Publication Type
Article
Keywords
Amylases - isolation & purification - metabolism
Aspergillus - enzymology
Aspergillus oryzae - enzymology
Binding Sites
Calcium - pharmacology
Drug Stability
English Abstract
Heat
Kinetics
Protein Binding
Protein Denaturation
Urea - pharmacology
Abstract
Denaturation of alpha-amylase from Aspergillus oryzae was studied under the effect of heating urea and some other denaturating agents. Inhibition in the enzyme denaturation, deviation from the first order equation and, consequently, establishment of the false equilibrium in the system are shown. The values are calculated for the reaction rate constants of alpha-amylase denaturation under the effect to heat (40 degrees C) and urea. A method is developed for isolating native amylase stabilized by heating at 40 degrees C during the period of inactivation slowing down and preservation to the 50-70% activity in the system. It is shown that in the presence of calcium ions the stability of the isolated native enzyme is 13.0 +/- 2.5% hihger on the average to heating up to 40 degrees C, 28.4 %/- 7.2% higher - to the effect of 5.5 M urea and 18.4 +/- 3.6% higher - to 18% alcohol.
PubMed ID
1209773 View in PubMed
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