Optimizing expression and solubility of proteins in E. coli using modified media and induction parameters
Abstract
The major goal of any protein expression experiment is to combine the maximum production per cell of soluble protein with the highest possible cell density to most efficiently obtain high yields of protein. A large number of parameters can be optimized in these experiments, but one of the most interesting parameters that have a strong effect on both per cell productivity and cell density is the cellular growth media coupled to the expression induction process. Using specialized media and testing multiple induction conditions, it is possible to significantly enhance the production of heterologous proteins from E. coli.
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E. coli has fast growth rate (doubling time 20 min), low cost, easiness of genetic manipulation, well-known molecular features, good productivity, and simple fermentation process development for manufacturing scale-up, making it an affordable expression system for recombinant protein.
“Given the fast growth rate (doubling time is 20 min), the low cost (the medium is inexpensive), the easiness of genetic manipulation, the well-known molecular features, the good productivity and the simple fermentation process development for manufacturing scale-up, this microorganism represents an affordable expression system for recombinant protein [43,44,45,46].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [45]
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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
- Taylor, T., Denson, J.-P., & Esposito, D.
- Affiliations
- Frederick National Laboratory for Cancer Research (US)
- Corresponding author
- Esposito, Dominic
- Venue
- Methods in Molecular Biology
- Publisher
- Springer New York
- Published
- 2017
- Volume
- 1586
- Pages
- 65-82
- ISSN
- 1064-3745 (ISSN-L)
- 1940-6029
- OpenAlex
- W2611685413
- Cited by
- 80
- References
- 0
- Citations by year
- 2026: 7 · 2025: 15 · 2024: 24 · 2023: 7 · 2022: 8 · 2021: 5 · 2020: 7 · 2019: 6 · 2017: 1
- FWCI
- 4.76
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Methods in molecular biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (HHSN261200800001E))
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- protein expression, soluble protein production, Escherichia coli, heterologous expression, growth media optimization, cell density, recombinant protein yield
- MeSH terms
- Animals, Cloning, Molecular, Culture Media, Escherichia coli, Humans, Recombinant Proteins, Solubility, Gene Expression, Cell Culture Techniques
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