Protein Engineering of Carboxyl Esterases by Rational Design and Directed Evolution

被引：0
|
作者：
Schmidt, M. [1 ]
Boettcher, D. [1 ]
Bornscheuer, U. T. [1 ]
机构：
[1] Ernst Moritz Arndt Univ Greifswald, Inst Biochem, Dept Biotechnol & Enzyme Catalysis, D-17487 Greifswald, Germany
来源：
PROTEIN AND PEPTIDE LETTERS | 2009年 / 16卷 / 10期
关键词：
ITERATIVE SATURATION MUTAGENESIS; THROUGHPUT-SCREENING METHOD; TERTIARY ALCOHOLS; BACILLUS-SUBTILIS; PSEUDOMONAS-FLUORESCENS; ENANTIOSELECTIVE HYDROLASES; FUNCTIONAL EXPRESSION; BURKHOLDERIA-GLADIOLI; HYDROLYTIC ENZYMES; KINETIC RESOLUTION;
D O I：
暂无
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：
In the past few years a considerable number of mutagenesis methods and high-throughput screening (HTS) systems have been developed and improved. In parallel, computer programs or software packages for molecular modeling have been further investigated. Thus, the number of examples for successful directed evolution and rational design is increasing constantly. In this review the essential mutagenesis methods and HTS systems, especially for esterases, are described and various examples for the application of these protein engineering tools are provided.
引用
收藏
页码：1162 / 1171
页数：10
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