Functional display of Pseudomonas and Burkholderia lipases using a translocator domain of EstA autotransporter on the cell surface of Escherichia coli

被引:23
作者
Yang, Taek Ho [2 ]
Kwon, Min-A. [1 ]
Song, Jae Kwang [1 ]
Pan, Jae Gu [3 ]
Rhee, Joon Shick [2 ]
机构
[1] Korea Res Inst Chem Technol, Chem Biotechnol Res Ctr, Taejon 305600, South Korea
[2] Korea Adv Inst Sci & Technol, Dept Biol Sci, Taejon 305701, South Korea
[3] GenoFocus Inc, Natl Res Lab Microbial Display, Taejon 305811, South Korea
关键词
Autotransporter; Burkholderia lipase; Cell surface display; Lipase-specific foldase; Pseudomonas lipases; INDUSTRIAL APPLICATIONS; EXPRESSION LEVELS; DEPENDENT LIPASE; ABC TRANSPORTER; COLI; FLUORESCENS; SECRETION; PROTEINS; OVEREXPRESSION; IMMOBILIZATION;
D O I
10.1016/j.jbiotec.2010.01.022
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
Functional expression of the industrially important Pseudomonas and Burkholderia lipases, such as those from P. aeruginosa, B. cepacia and P. fluorescens, was achieved on the cell surface of Escherichia coli using the C-terminal translocator moiety (EstATu) of autotransporter protein (EstA) from P. putida. In particular, lipases which required a lipase-specific foldase (Lif) for their proper folding were for the first time displayed in the active form by coexpression of the Lit protein. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码:126 / 129
页数:4
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