ACYLATION OF SUBTILISIN WITH LONG FATTY ACYL RESIDUES AFFECTS ITS ACTIVITY AND THERMOSTABILITY IN AQUEOUS-MEDIUM

被引:10
作者
PLOU, FJ
BALLESTEROS, A
机构
[1] Departamento de Biocatalisis, Instituto de Catálisis, CSIC
关键词
SUBTILISIN CARLSBERG; CHEMICAL MODIFICATION; ENZYME HYDROPHOBICITY; IN VITRO HYDROPHOBIZATION; ENZYME STABILIZATION;
D O I
10.1016/0014-5793(94)80415-X
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
Subtilisin Carlsberg has been artificially hydrophobized by acylation with octanoyl or palmitoyl chlorides. Samples with several degrees of substitution were obtained. Hydrophobization facilitates in some cases the binding of synthetic or natural substrates. Furthermore, derivatized subtilisins show improved thermal stability (15-fold at 45 degrees C) in aqueous solution. As a result, octanoyl-subtilisin exhibits enhanced thermostability without losing biological activity.
引用
收藏
页码:200 / 204
页数:5
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