IMPROVED ACTIVITY OF A LIPASE BY VACUUM DRYING ON TO A HYDROPHOBIC MICROPOROUS SUPPORT

被引：7

作者：

HUANG, FC

JU, YH

机构：

[1] Department of Chemical Engineering, National Taiwan Institute of Technology, Taipei

来源：

BIOTECHNOLOGY TECHNIQUES | 1994年 / 8卷 / 11期

关键词：

D O I：

10.1007/BF00152892

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Lipase from Rhizopus arrhizus was immobilized by physical adsorption on hydrophobic microporous polypropylene supports. The immobilized enzyme catalyst was employed for the hydrolysis of palm kernel olein in the presence of n-hexane. The initial rate of lipolysis for vacuum dried immobilized lipase is nearly double that of air dried. The initial rate of lipolysis declines with increase of drying time. Immobilized lipase clearly reveals a relatively high initial rate after 30 days of storage at 4 degrees C. Stability of the immobilized lipase in buffer could be enhanced up to three-fold that of the free lipase.

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页码：827 / 830

页数：4

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