A KINETIC-STUDY OF IMMOBILIZED LIPASE CATALYZING THE SYNTHESIS OF ISOAMYL ACETATE BY TRANSESTERIFICATION IN NORMAL-HEXANE

被引：134

作者：

RIZZI, M

STYLOS, P

RIEK, A

REUSS, M

机构：

[1] Institut für Bioverfahrenstechnik, Universität Stuttgart

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1992年 / 14卷 / 09期

关键词：

IMMOBILIZED LIPASE; TRANSESTERIFICATION; ORGANIC SOLVENT; NORMAL-HEXANE; KINETIC STUDIES; PING-PONG BI-BI WITH INHIBITION;

D O I：

10.1016/0141-0229(92)90110-A

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：

Isoamyl acetate was synthesized by lipase-catalyzed transesterification of ethyl acetate in n-hexane. The selectivity and rates of ester formation decreased when water content of the immobilized enzyme exceeded 3% (w/w). Experimental observations clearly indicate that the substrates as well as the product (ethanol) act as dead-end inhibitors. A ping-pong bi-bi mechanism with competitive inhibition by substrates and predicts is proposed that predicts the experimental observation satisfactorily.

引用

页码：709 / 714

页数：6

共 12 条

[1] MECHANISM OF ACTION OF PROTEOLYTIC ENZYMES [J].