Cultivation at 6-10 degrees C is an effective strategy to overcome the insolubility of recombinant proteins in Escherichia coli SCIE SCOPUS

Cited 40 time in WEB OF SCIENCE Cited 47 time in Scopus
Title
Cultivation at 6-10 degrees C is an effective strategy to overcome the insolubility of recombinant proteins in Escherichia coli
Author(s)
Song, Jung Min; An, Young Jun; Kang, Mee Hye; Lee, Youn-Ho; Cha, Sun-Shin
KIOST Author(s)
An, Young Jun(안영준)Lee, Youn Ho(이윤호)
Alternative Author(s)
송정민; 안영준; 강미혜; 이윤호; 차선신
Publication Year
2012-04
Abstract
Protein expression in Escherichia coli at 15-25 degrees C is widely used to increase the solubility of recombinant proteins. However, many recombinant proteins are insolubly expressed even at those low temperatures. Here, we show that recombinant proteins can be expressed as soluble forms by simply lowering temperature to 6-10 degrees C without cold adapted chaperon systems. By using E. coli Rosetta-gami2(DE3), we obtained 1.8 and 0.9 mg of Ctyptopygus antarticus mannanase (CaMan) and cellulase (CaCel) from 11 culture grown at 6 and 10 degrees C, respectively. Cultivation at 10 degrees C also led to successful expression of EM3L7 (a lipase isolated from a metagenomic library) in a soluble form in E. coli BL21(DE3). Consequently, E. coli cultivation at 6-10 degrees C is an effective strategy for overcoming a major hurdle of the inclusion body formation. (C) 2012 Elsevier Inc. All rights reserved.
ISSN
1046-5928
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/3603
DOI
10.1016/j.pep.2012.01.020
Bibliographic Citation
PROTEIN EXPRESSION AND PURIFICATION, v.82, no.2, pp.297 - 301, 2012
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Subject
MINIMAL TEMPERATURE; EXPRESSION; PURIFICATION; GROWTH; BINDING; GENES
Keywords
Protein expression; E. coli; Extremely low temperature
Type
Article
Language
English
Document Type
Article
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
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