KINETICS AND STABILITY OF AN IMMOBILIZED ORSELLINATE DEPSIDE HYDROLASE IN POLYACRYLAMIDE-GEL

被引:10
作者
GARCIAJUNCEDA, E
CAMBON, C
VICENTE, C
机构
[1] Laboratory of Plant Physiology, Faculty of Biology, Complutense University of Madrid, Madrid
关键词
IMMOBILIZED ENZYMES; IMMOBILIZATION; ORSELLINATE DEPSIDE HYDROLASE; LICHENS; EVERNIA-PRUNASTRI;
D O I
10.1016/0141-0229(91)90142-W
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
Orsellinate depside hydrolase (EC.3.1.1.40) is produced by lichen cells, in which it hydrolyses depsides to monocyclic phenols. The hydrolase, which uses evernic acid as a substrate, has been purified 40-fold and entrapped in 20% polyacrylamide gel. The K(m) value of immobilized enzyme was 7.5 mM for the substrate. The entrapped hydrolase has a pH optimum of 6.5 and is highly thermostable. Orcinol, a well-known inhibitor of free hydrolase, does not have any significant effect on the entrapped enzyme. After 2 months of storage at 25-degrees-C, the immobilized enzyme retains about one-half the initial activity.
引用
收藏
页码:275 / 279
页数:5
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