Tsyperovych O S, Halych I P, Kloesnyk L O, Artyukh H H
Ukr Biokhim Zh. 1975 Jul-Aug;47(4):453-7.
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.
研究了米曲霉α-淀粉酶在加热、尿素及其他一些变性剂作用下的变性情况。结果表明，酶变性受到抑制，偏离一级方程，从而在体系中建立了假平衡。计算了α-淀粉酶在加热（40℃）和尿素作用下变性反应速率常数的值。开发了一种方法，用于分离在失活减缓期间经40℃加热稳定且在体系中保留50 - 70%活性的天然淀粉酶。结果表明，在钙离子存在下，分离得到的天然酶对高达40℃加热的稳定性平均高13.0±2.5%，对5.5 M尿素作用的稳定性高28.4%±7.2%，对18%乙醇作用的稳定性高18.4±3.6%。
