THERMOSTABILIZATION OF ERYTHROCYTE CARBONIC-ANHYDRASE BY POLYHYDRIC ADDITIVES

被引：13

作者：

CIOCI, F

机构：

[1] Department of Chemical Engineering, University of Rome La Sapienza, Rome

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1995年 / 17卷 / 07期

关键词：

CARBONIC ANHYDRASE; POLYHYDRIC ADDITIVES; THERMOSTABILIZATION; PROTEIN STABILITY;

D O I：

10.1016/0141-0229(94)00079-7

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

An experimental investigation was carried out on the influence of some polyhydric additives on the thermal behavior of erythrocyte carbonic anhydrase. The stability of the enzyme was analyzed by thermal unfolding and kinetic experiments. The results obtained showed a stabilizing effect of glycerol and sugars (fructose, glucose, sucrose, and sorbitol) whereas ethylene glycol was found to favor protein unfolding. An analysis of the thermodynamic behavior of the enzyme allowed us to determine the transition temperature and the changes in enthalpy, entropy, and free energy in pure buffer and in the presence of additives. The thermodynamic and kinetic results supported the hypothesis that thermal stabilization of carbonic anhydrase is a consequence of microenvironmental modifications, probably related to preferential exclusion phenomena, which strengthen the macromolecule and presence the biologic activity of the enzyme under thermally adverse conditions.

引用

页码：592 / 600

页数：9

共 37 条

[1] INCREASED THERMAL-STABILITY OF BACILLUS-LICHENIFORMIS ALPHA-AMYLASE IN THE PRESENCE OF VARIOUS ADDITIVES [J].