Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions

被引：93

作者：

Dalal, Sohel ^{[1
]}

Kapoor, Manah ^{[1
]}

Gupta, Munishwar N. ^{[1
]}

机构：

[1] Indian Inst Technol, Dept Chem, New Delhi 110016, India

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2007年 / 44卷 / 3-4期

关键词：

alpha-amylase; glutaraldehyde cross-linking; lipase; combi-CLEA; phospholipase A(2); thermal stability;

D O I：

10.1016/j.molcatb.2006.10.003

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 novel cross-linked enzyme aggregates (CLEA) concept called combi-CLEA has been described. It is based upon the fact that CLEA can be made from heterogeneous populations of proteins/enzymes. Porcine pancreatic acetone powder crude extract was used for preparing CLEA in such a way that lipase, alpha-amylase, phospholipase A(2) activities were retained upto 100%. The lipase present in the CLEA showed greater thermal stability at 50 degrees C as compared to free enzyme. For lipase and phospholipase A(2), V-max/K-m showed no significant change upon combi-CLEA formation but decreased significantly for alpha-amylase activity from 190 to 114 min(-1). The lipase activity and alpha-amylase activity in CLEA were completely retained upto three cycles of use. The scanning electron microscopic (SEM) studies showed that morphology of CLEA changed upon inactivation by reuses. (c) 2006 Elsevier B.V. All rights reserved.

引用

页码：128 / 132

页数：5

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