Immobilization, stability and esterification studies of a lipase from a Bacillus sp.

被引：71

作者：

Dosanjh, NS ^{[1
]}

Kaur, J ^{[1
]}

机构：

[1] Panjab Univ, Dept Biotechnol, Chandigarh 160014, India

来源：

BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY | 2002年 / 36卷 / 01期

关键词：

enzymic reaction; ester synthesis; half-life; thermostability;

D O I：

10.1042/BA20010070

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：

In the present paper a comparative account of the immobilization of a Bacillus lipase on different solid supports with different surface properties and their thermostability is presented. Immobilization enhanced the thermostability of lipase. At higher temperatures, lipase immobilized and cross-linked on a hydrophobic surface showed the maximum thermostability. The optimum temperature for immobilized lipase was 9 degreesC higher than for the free enzyme, while the pH optima were the same. The half-life of soluble lipase at 50 degreesC was calculated to be 4.5 h, while immobilized lipase did not lose any activity even after 8 h. The temperature stability (for 1 h) of immobilized enzyme was enhanced from 50 to 60 degreesC in comparison with non-immobilized enzyme. Applications of immobilized lipase for esterification are also presented.

引用

页码：7 / 12

页数：6

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