Operational stability of high initial activity protease catalysts in organic solvents

被引：19

作者：

Fernandes, JFA ^{[1
]}

Halling, PJ ^{[1
]}

机构：

[1] Univ Strathclyde, Dept Pure & Appl Chem, Glasgow G1 1XW, Lanark, Scotland

来源：

BIOTECHNOLOGY PROGRESS | 2002年 / 18卷 / 06期

关键词：

D O I：

10.1021/bp020098g

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：

The first studies on the operational stability of cross-linked enzyme crystals (CLECs) in organic media are described. Although these catalysts display high initial specific activity, they inactivate rapidly, losing more than 50% of the initial activity within the first 4 h under continuous flow. Furthermore, the inactivation is not reversible when returned to an aqueous medium. The same rapid inactivation occurs with adsorbed protease preparations that show similar high initial specific activity (propanol-rinsed enzyme preparations (PREPs) of subtilisin and alpha-chymotrypsin).

引用

页码：1455 / 1457

页数：3