Stability of immobilized alpha-chymotrypsin in supercritical carbon dioxide

被引：29

作者：

Lozano, P ^{[1
]}

Avellaneda, A ^{[1
]}

Pascual, R ^{[1
]}

Iborra, JL ^{[1
]}

机构：

[1] UNIV MURCIA,FAC QUIM,DEPT BIOQUIM & BIOLK MOL B & INMUNOL,E-30001 MURCIA,SPAIN

来源：

BIOTECHNOLOGY LETTERS | 1996年 / 18卷 / 11期

关键词：

D O I：

10.1007/BF00129968

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：

Inactivation of immobilized alpha-chymotrypsin in supercritical carbon dioxide was with a first-order kinetic behaviour. The increase in either the pressure or the temperature of the fluid enhanced the inactivation process of the enzyme. The fluid density was shown as a key parameter on the enzyme stability, enhancing the half-life time proportionally to the physical phase of CO2, as follows: liquid > supercritical > gas. However, the number of pressurization/depressurization cycles, and the water content of the derivative increased greatly the loss of activity.

引用

页码：1345 / 1350

页数：6

共 19 条

[1]

AALTONEN O, 1991, CHEMTECH, V21, P240

[2] GERANYL ACETATE SYNTHESIS BY LIPASE-CATALYZED TRANSESTERIFICATION IN SUPERCRITICAL CARBON-DIOXIDE [J].