MODELING OF LIPASE CATALYZED TRANSESTERIFICATION REACTIONS

被引：7

作者：

MUKESH, D ^{[1
]}

SALUNKE, R ^{[1
]}

BANERJI, AA ^{[1
]}

BEVINAKATTI, HS ^{[1
]}

机构：

[1] ALCHEM RES CTR, THANA 400601, MAHARASHTRA, INDIA

来源：

BIOCATALYSIS | 1992年 / 6卷 / 02期

关键词：

LIPASE CATALYSIS; MATHEMATICAL MODELING; SUBSTRATE INHIBITION; TRANSESTERIFICATION;

D O I：

10.3109/10242429209014891

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Transesterification of substituted ethanols with ethyl acetate is studied in the presence of two different lipases. The steric bulk of the substituent group plays a more important role than the electronic factors in the reaction. The reversible reaction is modelled mathematically, and the rate parameters in the model estimated by a transient parameter estimation procedure. The effect of lipase quantity, reaction temperature and substrate concentration on the reaction is studied independently. Product quantity exhibits a maxima for increasing substrate concentration which is modelled successfully with a substrate product inhibition model, and compared with the experimental data © 1992 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.

引用

页码：151 / 159

页数：9

共 9 条

[1] KINETICS OF PRODUCT INHIBITION IN ALCOHOL FERMENTATION [J].