THE ESTERASE PROFILE OF A LIPASE FROM CANDIDA-CYLINDRACEA

被引：52

作者：

BRAHIMIHORN, MC ^{[1
]}

GUGLIELMINO, ML ^{[1
]}

ELLING, L ^{[1
]}

SPARROW, LG ^{[1
]}

机构：

[1] CSIRO,DIV WOOL TECHNOL,PARKVILLE LAB,PARKVILLE,VIC 3052,AUSTRALIA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1042卷 / 01期

关键词：

(C. cylindracea); Esterase; Hydrophobic interaction chromatography; Lipase;

D O I：

10.1016/0005-2760(90)90055-3

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：

A commercial preparation of a lipase produced by Candida cylindracea catalysed the hydrolysis of both long- and short-chain esters of p-nitrophenol. Six major bands of hydrolytic activity to α-naphthyl acetate were detected on polyacrylamide gel electrophoresis and two on isoelectric focusing. The esterase activity fractionated into two major peaks of activity on ion-exchange chromatography and into several peaks of activity on hydrophobic interaction chromatography. These esterase activities showed different substrate specificities to p-nitrophenyl esters, tributyrin and cetyl palmitate. © 1990.

引用

页码：51 / 54

页数：4

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