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Increasing recombinant protein production in Escherichia coli through metabolic and genetic engineering

Hendrik Waegeman and Wim Soetaert UGent (2011) JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY. 38(12). p.1891-1910
abstract
Different hosts have been used for recombinant protein production, ranging from simple bacteria, such as Escherichia coli and Bacillus subtilis, to more advanced eukaryotes as Saccharomyces cerevisiae and Pichia pastoris, to very complex insect and animal cells. All have their advantages and drawbacks and not one seems to be the perfect host for all purposes. In this review we compare the characteristics of all hosts used in commercial applications of recombinant protein production, both in the area of biopharmaceuticals and industrial enzymes. Although the bacterium E. coli remains a very often used organism, several drawbacks limit its possibility to be the first-choice host. Furthermore, we show what E. coli strains are typically used in high cell density cultivations and compare their genetic and physiological differences. In addition, we summarize the research efforts that have been done to improve yields of heterologous protein in E. coli, to reduce acetate formation, to secrete the recombinant protein into the periplasm or extracellular milieu, and to perform post-translational modifications. We conclude that great progress has been made in the incorporation of eukaryotic features into E. coli, which might allow the bacterium to regain its first-choice status, on the condition that these research efforts continue to gain momentum.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (review)
publication status
published
subject
keyword
INCLUSION-BODY PROTEINS, BACTERIAL EXPRESSION SYSTEMS, BETA-GALACTOSIDASE PRODUCTION, HIGH-LEVEL PRODUCTION, FED-BATCH CULTIVATION, YEAST PICHIA-PASTORIS, HIGH-CELL-DENSITY, Industrial enzyme, Biopharmaceutical, Engineering, Heterologous protein, Escherichia coli, Recombinant protein production, N-LINKED GLYCOSYLATION, EXTRACELLULAR PRODUCTION, ACETATE ACCUMULATION
journal title
JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
J. Ind. Microbiol. Biotechnol.
volume
38
issue
12
pages
1891 - 1910
Web of Science type
Review
Web of Science id
000300159300002
JCR category
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
JCR impact factor
2.735 (2011)
JCR rank
58/157 (2011)
JCR quartile
2 (2011)
ISSN
1367-5435
DOI
10.1007/s10295-011-1034-4
project
Biotechnology for a sustainable economy (Bio-Economy)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1906131
handle
http://hdl.handle.net/1854/LU-1906131
date created
2011-09-21 16:48:39
date last changed
2016-12-19 15:41:59
@article{1906131,
  abstract     = {Different hosts have been used for recombinant protein production, ranging from simple bacteria, such as Escherichia coli and Bacillus subtilis, to more advanced eukaryotes as Saccharomyces cerevisiae and Pichia pastoris, to very complex insect and animal cells. All have their advantages and drawbacks and not one seems to be the perfect host for all purposes. In this review we compare the characteristics of all hosts used in commercial applications of recombinant protein production, both in the area of biopharmaceuticals and industrial enzymes. Although the bacterium E. coli remains a very often used organism, several drawbacks limit its possibility to be the first-choice host. Furthermore, we show what E. coli strains are typically used in high cell density cultivations and compare their genetic and physiological differences. In addition, we summarize the research efforts that have been done to improve yields of heterologous protein in E. coli, to reduce acetate formation, to secrete the recombinant protein into the periplasm or extracellular milieu, and to perform post-translational modifications. We conclude that great progress has been made in the incorporation of eukaryotic features into E. coli, which might allow the bacterium to regain its first-choice status, on the condition that these research efforts continue to gain momentum.},
  author       = {Waegeman, Hendrik and Soetaert, Wim},
  issn         = {1367-5435},
  journal      = {JOURNAL OF INDUSTRIAL MICROBIOLOGY \& BIOTECHNOLOGY},
  keyword      = {INCLUSION-BODY PROTEINS,BACTERIAL EXPRESSION SYSTEMS,BETA-GALACTOSIDASE PRODUCTION,HIGH-LEVEL PRODUCTION,FED-BATCH CULTIVATION,YEAST PICHIA-PASTORIS,HIGH-CELL-DENSITY,Industrial enzyme,Biopharmaceutical,Engineering,Heterologous protein,Escherichia coli,Recombinant protein production,N-LINKED GLYCOSYLATION,EXTRACELLULAR PRODUCTION,ACETATE ACCUMULATION},
  language     = {eng},
  number       = {12},
  pages        = {1891--1910},
  title        = {Increasing recombinant protein production in Escherichia coli through metabolic and genetic engineering},
  url          = {http://dx.doi.org/10.1007/s10295-011-1034-4},
  volume       = {38},
  year         = {2011},
}

Chicago
Waegeman, Hendrik, and Wim Soetaert. 2011. “Increasing Recombinant Protein Production in Escherichia Coli Through Metabolic and Genetic Engineering.” Journal of Industrial Microbiology & Biotechnology 38 (12): 1891–1910.
APA
Waegeman, H., & Soetaert, W. (2011). Increasing recombinant protein production in Escherichia coli through metabolic and genetic engineering. JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY, 38(12), 1891–1910.
Vancouver
1.
Waegeman H, Soetaert W. Increasing recombinant protein production in Escherichia coli through metabolic and genetic engineering. JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY. 2011;38(12):1891–910.
MLA
Waegeman, Hendrik, and Wim Soetaert. “Increasing Recombinant Protein Production in Escherichia Coli Through Metabolic and Genetic Engineering.” JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY 38.12 (2011): 1891–1910. Print.