柱孢假丝酵母脂肪酶的酯酶图谱

The esterase profile of a lipase from Candida cylindracea.

作者信息

Brahimi-Horn M C, Guglielmino M L, Elling L, Sparrow L G

机构信息

Commonwealth Scientific and Industrial Research Organization, Division of Wool Technology, Parkvill Laboratory, Australia.

出版信息

Biochim Biophys Acta. 1990 Jan 16;1042(1):51-4. doi: 10.1016/0005-2760(90)90055-3.

DOI:10.1016/0005-2760(90)90055-3

PMID:2297523

Abstract

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 alpha-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.

摘要

一种由柱形假丝酵母产生的脂肪酶的商业制剂催化了对硝基苯酚的长链和短链酯的水解。在聚丙烯酰胺凝胶电泳上检测到对醋酸α-萘酯有水解活性的六个主要条带，在等电聚焦上检测到两个。酯酶活性在离子交换色谱上分离为两个主要活性峰，在疏水相互作用色谱上分离为几个活性峰。这些酯酶活性对对硝基苯酯、三丁酸甘油酯和十六烷基棕榈酸酯表现出不同的底物特异性。