Immobilization and characterization of porcine pancreas lipase

被引：84

作者：

Bagi, K ^{[1
]}

Simon, LM ^{[1
]}

Szajani, B ^{[1
]}

机构：

[1] ATTILA JOZSEF UNIV, DEPT BIOCHEM, SZEGED, HUNGARY

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 1997年 / 20卷 / 07期

关键词：

porcine pancreas lipase; immobilization; cross-linking; conformational stability;

D O I：

10.1016/S0141-0229(96)00190-1

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：

Porcine pancreas lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) was immobilized with the highest activity (2,187 U g(-1) solid) on polyacrylamide beads possessing carboxylic functional groups activated by a water-soluble carbodiimide. The optimum pH for catalytic activity was pH 8.9. The apparent optimum temperature for the immobilized enzyme was about 7 degrees C higher than that for the soluble enzyme. The immobilization stabilized the enzyme against heat and urea treatment. Cross-linking of the immobilized enzyme with glutaraldehyde or 3,5-difluoronitrobenzene improved the thermal stability. Application of the immobilized lipase for olive oil hydrolysis is also presented. (C) 1997 by Elsevier Science Inc.

引用

页码：531 / 535

页数：5

共 24 条

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