Activity and stability of Escherichia coli β-galactosidase in cosolvent systems

被引：9

作者：

Irazoqui, G ^{[1
]}

Villarino, A ^{[1
]}

Batista-Viera, F ^{[1
]}

Brena, BM ^{[1
]}

机构：

[1] Fac Quim, Catedra Bioquim, Montevideo, Uruguay

来源：

BIOTECHNOLOGY TECHNIQUES | 1998年 / 12卷 / 12期

关键词：

beta-galactosidase; biocatalysis; organic solvents;

D O I：

10.1023/A:1008809427293

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The kinetic parameters of E.coli beta-galactosidase were not altered by the addition of 2-propanol or ethyl acetate (1.6% v/v). While ethylene glycol (1.6% v/v) doubled the values of both K-M (0.29 mM) and k(cat) (1393 s(-1)), tetraethyleneglycoldimethylether (tetraglyme, 1.6% v/v) preserved K-M, but decreased k(cat). At 50 degrees C all the cosolvents dramatically shortened the enzymatic half life, and so did Tetraglyme and 2-propanol at 28 degrees C. At 28 degrees C, both ethyl acetate and ethylene glycol stabilised the enzyme 9- and 6-fold respectively. This fact, together with the activation effect of ethylene glycol may lead to practical applications.

引用

页码：885 / 888

页数：4

共 9 条

[1] THE ACTIVE-SITE AND MECHANISM OF THE BETA-GALACTOSIDASE FROM ESCHERICHIA-COLI [J].