Genetic engineering modification and fermentation optimization for extracellular production of recombinant proteins using Escherichia coli
Abstract
As a common expression host, Escherichia coli has received more and more attention due to the recently developed secretory expression system, which offers advantages like reduced downstream bioprocesses and improved product quality. These advantages, coupled with high-density fermentation technology, make it a preferred system for large-scale production of many proteins utilized in industry and agriculture at a reduced process cost. To improve the secretion efficiency of target proteins, various strategies, including signal peptide optimization, periplasmic leakage, and chaperones co-expression have been developed. In addition, the optimization of the fermentation conditions such as temperature, inducer, and medium were also taken into account for the extracellular production in the high-density fermentation to reduce the cost of production. Here, these strategies ranging from genetic engineering to fermentation optimization were summarized for the future guidance of extracellular production of recombinant proteins using E. coli.
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The choice of signal peptide sequence and co-expression with chaperones can affect secretion and folding.
“Additionally, the choice of the signal peptide sequence [146,147,148,149] and the co-expression with chaperons can affect the secretion and folding (see Figure 1).”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [148]
Extracellular secretion can be successfully achieved by optimizing the induction starting point and by adding chemical agents that promote outer cell membrane permeability.
“The extracellular secretion can be successfully achieved by optimizing the induction starting point and by adding chemical agents that promote outer cell membrane permeability [131,148,173].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [148]
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Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments
Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works
- Authors
- Zhou, Y., Lu, Z., Wang, X., Selvaraj, J. N., & Zhang, G.
- Affiliations
- Hubei University (CN)
- Corresponding author
- Zhang, Guimin
- Venue
- Applied Microbiology and Biotechnology
- Published
- 2017-12-21
- Volume
- 102
- Issue
- 4
- Pages
- 1545-1556
- ISSN
- 0175-7598 (ISSN-L)
- 1432-0614
- OpenAlex
- W2780448671
- Cited by
- 97
- References
- 3
- Citations by year
- 2026: 15 · 2025: 7 · 2024: 13 · 2023: 14 · 2022: 13 · 2021: 13 · 2020: 8 · 2019: 7 · 2018: 5
- FWCI
- 0.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Applied Microbiology and Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (31670069)
- echnical Innovation Special Fund of Hubei Province (2017ACA171)
- Wuhan Yellow Crane Talents
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- recombinant protein secretion, Escherichia coli, chaperone co-expression, high cell density fermentation, fermentation optimization, culture medium optimization, extracellular protein production
- MeSH terms
- Culture Media, Escherichia coli, Fermentation, Industrial Microbiology, Recombinant Proteins, Temperature, Metabolic Engineering
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