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
[41]   Production and purification of refolded recombinant human IL-7 from inclusion bodies [J].
Ouellette, T ;
Destrau, S ;
Ouellette, T ;
Zhu, JW ;
Roach, JM ;
Coffman, JD ;
Hecht, T ;
Lynch, JE ;
Giardina, SL .
PROTEIN EXPRESSION AND PURIFICATION, 2003, 30 (02) :156-166
[42]   Novel high-level constitutive expression system, pHCE vector, for a convenient and cost-effective soluble production of human tumor necrosis factor-α [J].
Poo, H ;
Song, JJ ;
Hong, SP ;
Choi, YH ;
Yun, SW ;
Kim, JH ;
Lee, SC ;
Lee, SG ;
Sung, MH .
BIOTECHNOLOGY LETTERS, 2002, 24 (14) :1185-1189
[43]   A general strategy for the expression of recombinant human cytochrome P450s in Escherichia coli using bacterial signal peptides: Expression of CYP3A4, CYP2A6, and CYP2E1 [J].
Pritchard, MP ;
Ossetian, R ;
Li, DN ;
Henderson, CJ ;
Burchell, B ;
Wolf, CR ;
Friedberg, T .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1997, 345 (02) :342-354
[44]   FUNCTIONAL ANTIBODY SINGLE-CHAIN FRAGMENTS FROM THE CYTOPLASM OF ESCHERICHIA-COLI - INFLUENCE OF THIOREDOXIN REDUCTASE (TRXB) [J].
PROBA, K ;
GE, LM ;
PLUCKTHUN, A .
GENE, 1995, 159 (02) :203-207
[45]   THE COMPLETE GENERAL SECRETORY PATHWAY IN GRAM-NEGATIVE BACTERIA [J].
PUGSLEY, AP .
MICROBIOLOGICAL REVIEWS, 1993, 57 (01) :50-108
[46]  
Qiu J, 1998, APPL ENVIRON MICROB, V64, P4891
[47]  
SCHEIN CH, 1989, BIO-TECHNOL, V7, P1141
[48]   High-level production of soluble tumor necrosis factor-related apoptosis-inducing ligand (Apo2L/TRAIL) in high-density cultivation of recombinant Escherichia coli using a combined feeding strategy [J].
Shen, YL ;
Zhang, Y ;
Sun, AY ;
Xia, XX ;
Wei, DZ ;
Yang, SL .
BIOTECHNOLOGY LETTERS, 2004, 26 (12) :981-984
[49]   Enhanced production of human mini-proinsulin in fed-batch cultures at high cell density of Escherichia coli BL21(DE3)[pET-3aT2M2] [J].
Shin, CS ;
Hong, MS ;
Bae, CS ;
Lee, J .
BIOTECHNOLOGY PROGRESS, 1997, 13 (03) :249-257
[50]   Production of excreted human epidermal growth factor (hEGF) by an efficient recombinant Escherichia coli system [J].
Sivakesava, S ;
Xu, ZN ;
Chen, YH ;
Hackett, J ;
Huang, RC ;
Lam, E ;
Lam, TL ;
Siu, KL ;
Wong, RSC ;
Wong, WKR .
PROCESS BIOCHEMISTRY, 1999, 34 (09) :893-900
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