Purification and characterization of a Penicillium sp lipase which discriminates against diglycerides

被引：23

作者：

Gulomova, K

Ziomek, E

Schrag, JD

Davranov, K

Cygler, M

机构：

[1] NATL RES COUNCIL CANADA, BIOTECHNOL RES INST, MONTREAL, PQ H4P 2R2, CANADA

[2] UZBEK ACAD SCI, INST MICROBIOL, TASHKENT, UZBEKISTAN

来源：

LIPIDS | 1996年 / 31卷 / 04期

关键词：

D O I：

10.1007/BF02522923

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 lipase was isolated from Penicillium sp. strain UZLM-4 and characterized. This lipase has a molecular weight of 27,344 (determined by mass spectrometry) and hydrolyzes triglycerides in preference to mono- and diglyceride substrates. Among various triglyceride substrates, tributyrin is hydrolyzed about four times faster than any other tested. The lipase has a preference for hydrolysis at the 1,3 positions of the lipids and shows a weak stereoselectivity for the S enantiomer. Unlike most other lipases, this lipase is stable and has a high activity at low surface pressures (5-10 mN/m).

引用

页码：379 / 384

页数：6

共 40 条

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