PRODUCTION AND PARTIAL-PURIFICATION OF A LIPASE FROM PSEUDOMONAS-PUTIDA 3SK

被引：115

作者：

LEE, SY ^{[1
]}

RHEE, JS ^{[1
]}

机构：

[1] KOREA ADV INST SCI & TECHNOL,DEPT BIOTECHNOL,373-1 KUSONG DONG,YUSONG KU,TAEJON 305701,SOUTH KOREA

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1993年 / 15卷 / 07期

关键词：

PSEUDOMONAS-PUTIDA; 3SK; LIPASE; ISOOCTANE; 2-PHASE BIOCATALYSIS;

D O I：

10.1016/0141-0229(93)90026-X

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：

Extracellular lipase was produced by the solvent-resistant strain Pseudomonas putida 3SK during the late logarithmic growth phase. The enzyme was purified 21-fold with 5.3% recovery by ion exchange chromatography and gel filtration chromatography. The molecular weight of the purified enzyme by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was shown to be 45 kDa. The lipase had an optimum pH range of 8.0-9.0 and was stable within the pH range 4.0-10.0. The optimal temperature was 37-degrees-C and it was stable up to 75-degrees-C. When the effects of organic solvents were tested, isooctane was most suitable for enzymatic fat hydrolysis in the two-phase system, Enzyme activity was inhibited by mercury ions and sodium dodecyl sulfate, whereas calcium ion and taurocholic acid stimulated its activity.

引用

页码：617 / 623

页数：7

共 34 条

[11] PURIFICATION AND CHARACTERIZATION OF A THERMOSTABLE LIPASE FROM NEWLY ISOLATED PSEUDOMONAS SP KWI-56 [J].