PURIFICATION AND CHARACTERIZATION OF A THERMOSTABLE LIPASE FROM NEWLY ISOLATED PSEUDOMONAS SP KWI-56

被引：103

作者：

IIZUMI, T

NAKAMURA, K

FUKASE, T

机构：

[1] Kurita Central Laboratories, Kurita Water Industries Ltd, Morinosato, Atsugi-shi, 243-01

来源：

AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1990年 / 54卷 / 05期

关键词：

D O I：

10.1080/00021369.1990.10870128

中图分类号：

S3 [农学（农艺学）];

学科分类号：

0901 ;

摘要：

Newly isolated Pseudomonas sp. KWI-56 produced an extracellular thermostable lipase. The enzyme was purified 13.9-fold by acetone precipitation and gel nitration by HPLC with 2.9% recovery. The purified enzyme, which showed a single band on SDS-PAGE, had a molecular weight of 33,000. The thermostability was very high, such that more than 96% of initial activity remained after incubation at 60°C for 24 hr. The optimum temperature was 60°C and the maximum hydrolysis of beef tallow reached 95% at the reaction temperature of 50°C. © 1990 by the Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.

引用

页码：1253 / 1258

页数：6

共 18 条

[1] STUDIES ON LIPASE OF THERMOPHILIC FUNGUS HUMICOLA-LANUGINOSA .1. ISOLATION AND IDENTIFICATION OF LIPOLYTIC AND THERMOPHILIC FUNGUS [J].