A generic system for the Escherichia coli cell-surface display of lipolytic enzymes

被引：71
作者：
Becker, S
Theile, S
Heppeler, N
Michalczyk, A
Wentzel, A
Wilhelm, S
Jaeger, KE
Kolmar, H
机构：
[1] Univ Gottingen, Inst Mikrobiol & Genet, Abt Mol Genet & Praparat Mol Biol, D-37077 Gottingen, Germany
[2] Univ Dusseldorf, Inst Mol Enzymtechnol, D-52426 Julich, Germany
来源：
FEBS LETTERS | 2005年 / 579卷 / 05期
关键词：
bacterial surface display; EstA; lipase; cutinase; autotransporter; type V(a) secretion;
D O I：
10.1016/j.febslet.2004.12.087
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：
EstA is an outer membrane-anchored esterase from Pseudomonas aeruginosa. An inactive EstA variant was used as an anchoring motif for the Escherichia coli cell-surface display of lipolytic enzymes. Flow cytometry analysis and measurement of lipase activity revealed that Bacillus subtilis lipase LipA, Fusarium solani pisi cutinase and one of the largest lipases presently known, namely Serratia marcescens lipase were all efficiently exported by the EstA autotransporter and also retained their lipolytic activities upon cell surface exposition. EstA provides a useful tool for surface display of lipases including variant libraries generated by directed evolution thereby enabling the identification of novel enzymes with interesting biological and biotechnological ramifications. (C) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：1177 / 1182
页数：6
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