KINETICS OF LIPASE-CATALYZED ESTERIFICATION IN SUPERCRITICAL CO2

被引:201
作者
MARTY, A [1 ]
CHULALAKSANANUKUL, W [1 ]
WILLEMOT, RM [1 ]
CONDORET, JS [1 ]
机构
[1] INST NATL SCI APPL,DEPT GENIE BIOCHIM & ALIMENTAIRE,CNRS,UA 540,F-31077 TOULOUSE,FRANCE
关键词
ENZYME; SUPERCRITICAL CO2; STABILITY; EFFECT OF WATER; COMPARISON WITH ORGANIC SOLVENT;
D O I
10.1002/bit.260390304
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
This study compares two solvents for enzymatic reactions: supercritical carbon dioxide (SCCO2) and organic solvent (n-hexane). The model reaction that was chosen was the esterification of oleic acid by ethanol catalyzed by an immobilized lipase from Mucor miehei (Lypozyme). The stability of the enzyme appeared to be quite good and similar in both media but was affected by the water content. Partition of water between solvents and immobilized enzyme has been calculated from experimental adsorption isotherms. The water content of the solid phase has a dramatic influence on the activity of the enzyme and its optimum value for activity was about 10% (w/w) in both media. A kinetic study enabled a Ping-Pong Bi-Bi reaction mechanism with inhibition by ethanol to be suggested. Despite some differences in kinetic constants, activity was in the same range in both media. Hypotheses for explaining the kinetic constant variations have been proposed and particular attention has been paid to the pH effects.
引用
收藏
页码:273 / 280
页数:8
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