Relationship between surface hydrophilicity of a protein and its stability against denaturation by organic solvents

FEBS Letters

Belova, Alla B.²  Mozhaev, Vadim V.¹  Khmelnitsky, Yuri L.²  Levashov, Andrey V.¹ 

[1] Chemistry Department, Moscow State University, GSP 119899 Moscow, USSR;A.N. Bakh Institute of Biochemistry, Leninsky prosp. 33, 117071 Moscow, USSR

关键词: Chymotrypsin;    Organic solvent;    Enzyme denaturation;    Enzyme modification;   

DOI  :  10.1016/0014-5793(91)80700-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The stability of α-chymotrypsin covalently modified with a strongly hydrophilic modifier, pyromellitic dianhydride, against solvent-induced denaturation in water—organic solvent binary mixtures has been studied. It was found that the hydrophilization results in a strong stabilization of the enzyme against denaturation by organic solvents. The stabilizing effect is explained in terms of the enhanced ability of the hydrophilized enzyme to keep its hydration shell, which is indispensable for supporting the native protein conformation, from denaturing stripping by organic solvents

【 授权许可】

Unknown