Kinetics denaturation of yeast alcohol dehydrogenase and the effect of temperature and trehalose. An isothermal microcalorimetry study

被引：18

作者：

Saboury, AA ^{[1
]}

Miroliae, M ^{[1
]}

Nemat-Gorgani, M ^{[1
]}

Moosavi-Movahedi, AA ^{[1
]}

机构：

[1] Univ Tehran, Inst Biochem & Biophys, Tehran, Iran

来源：

THERMOCHIMICA ACTA | 1999年 / 326卷 / 1-2期

关键词：

enzyme denaturation; enzyme inactivation; isothermal microcalorimetry; protein stability; yeast alcohol dehydrogenase;

D O I：

10.1016/S0040-6031(98)00588-7

中图分类号：

O414.1 [热力学];

学科分类号：

摘要：

The decrease in biological activity of alcohol dehydrogenase (YADH), due to its spontaneous denaturation, is accompanied by heat exchange of the enzyme solution. The spontaneous denaturation of YADH in 50 mM phosphate buffer, pH 7.8, at two temperatures of 27 degrees and 37 degrees C has been investigated by monitoring the heat exchange and residual activity of an enzyme solution with respect to time. The kinetics of denaturation was found to obey a first order law, depending on the concentration of YADH. The rate constants of denaturation were found to be 0.073 and 0.126 h(-1) at two temperatures of 27 degrees and 37 degrees C, respectively. These values decreased to 0.021 and 0.034 h(-1), respectively, in the presence of 1 M trehalose. Moreover, thermal denaturation study of YADH showed that trehalose leads to thermal stability enhancement. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：127 / 131

页数：5

共 41 条

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