Production of recombinant proteins by high cell density culture of Escherichia coli

被引：231
作者：
Choi, JH
Keum, KC
Lee, SY
机构：
[1] Korea Adv Inst Sci & Technol, Dept Chem & Biomol Engn, Metab & Biomol Engn Res Lab,BioProc Engn Res Ctr, Dept Biosyst,Bioinformat Res Ctr, Taejon 305701, South Korea
[2] Korea Adv Inst Sci & Technol, Ctr Ultramicrochem Proc Syst, Taejon 305701, South Korea
[3] Yonsei Univ, Coll Med, Dept Radiat Oncol, Seoul 120752, South Korea
来源：
CHEMICAL ENGINEERING SCIENCE | 2006年 / 61卷 / 03期
关键词：
high cell density culture; transcriptomics; proteomics; systems biology; Escherichia coli; recombinant protein;
D O I：
10.1016/j.ces.2005.03.031
中图分类号：
TQ [化学工业];
学科分类号：
0817 ;
摘要：
Escherichia coli has been the most widely used host for the production of recombinant proteins because it is the best characterized system in every aspect. Furthermore, the high cell density culture of recombinant E. coli has allowed production of various proteins with high yield and high productivities. Various cultivation strategies employing different host strains and expression systems have been successfully employed for the production of recombinant proteins. New strategies for strain improvement towards the goal of enhanced protein production are actively being developed based on high-throughput omics approaches such as transcriptomics and proteomcs. This paper reviews recent advances in the production of recombinant proteins by high cell density culture of E. coli. (c) 2005 Elsevier Ltd. All rights reserved.
引用
收藏
页码：876 / 885
页数：10
相关论文
共 64 条
[1]   Production of interferon-α in high cell density cultures of recombinant Escherichia coli and its single step purification from refolded inclusion body proteins [J].
Babu, KR ;
Swaminathan, S ;
Marten, S ;
Khanna, N ;
Rinas, U .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2000, 53 (06) :655-660
[2]   Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm [J].
Bessette, PH ;
Åslund, F ;
Beckwith, J ;
Georgiou, G .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (24) :13703-13708
[3]  
BOWDEN GA, 1990, J BIOL CHEM, V265, P16760
[4]   High production of heterologous proteins in Escherichia coli using the thermo-regulated T7 expression system [J].
Chao, YP ;
Law, WS ;
Chen, PT ;
Hung, WB .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2002, 58 (04) :446-453
[5]   Constitutive expression of protective antigen gene of Bacillus anthracis in Escherichia coli [J].
Chauhan, V ;
Singh, A ;
Waheed, SM ;
Singh, S ;
Bhatnagar, R .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2001, 283 (02) :308-315
[6]   Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS) [J].
Chen, G ;
Hayhurst, A ;
Thomas, JG ;
Harvey, BR ;
Iverson, BL ;
Georgiou, G .
NATURE BIOTECHNOLOGY, 2001, 19 (06) :537-542
[7]   Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp endoxylanase signal sequence [J].
Choi, JH ;
Jeong, KJ ;
Kim, SC ;
Lee, SY .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2000, 53 (06) :640-645
[8]   Secretory and extracellular production of recombinant proteins using Escherichia coli [J].
Choi, JH ;
Lee, SY .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2004, 64 (05) :625-635
[9]   Enhanced production of insulin-like growth factor I fusion protein in Escherichia coli by coexpression of the down-regulated genes identified by transcriptome profiling [J].
Choi, JH ;
Lee, SJ ;
Lee, SJ ;
Lee, SY .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2003, 69 (08) :4737-4742
[10]   MUTATIONS THAT ALLOW DISULFIDE BOND FORMATION IN THE CYTOPLASM OF ESCHERICHIA-COLI [J].
DERMAN, AI ;
PRINZ, WA ;
BELIN, D ;
BECKWITH, J .
SCIENCE, 1993, 262 (5140) :1744-1747
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