Cited by 841Protein purification and stabilityBacterial Genetics and BiotechnologyFungal and yeast genetics research

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Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

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Sørensen, Hans Peter, Mortensen, Kim Kusk·2005·Microbial Cell Factories

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Abstract

Pure, soluble and functional proteins are of high demand in modern biotechnology. Natural protein sources rarely meet the requirements for quantity, ease of isolation or price and hence recombinant technology is often the method of choice. Recombinant cell factories are constantly employed for the production of protein preparations bound for downstream purification and processing. Eschericia coli is a frequently used host, since it facilitates protein expression by its relative simplicity, its inexpensive and fast high density cultivation, the well known genetics and the large number of compatible molecular tools available. In spite of all these qualities, expression of recombinant proteins with E. coli as the host often results in insoluble and/or nonfunctional proteins. Here we review new approaches to overcome these obstacles by strategies that focus on either controlled expression of target protein in an unmodified form or by applying modifications using expressivity and solubility tags.

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Figure 1 Downstream applications employed to obtain soluble proteins from recombinant E. coli. As a common trait the in vivo strategies aims at lowering the metabolic burden associated with recombinant expression. Some of the mentioned strategies have therefore merely indirect influence on folding such as the use of tRNA complementation plasmids and stabilization of mRNA (see text and ref [1] for details).CC BY · PubMed Central

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Coninck, T. D., Vanhaeren, H., & Damme, E. J. M. V. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26188974

Authors: Sørensen, H. P., & Mortensen, K. K.
Affiliations: Aarhus University (DK)
Corresponding author: Mortensen, Kim Kusk
Venue: Microbial Cell Factories
Publisher: Springer Science and Business Media LLC
Published: 2005-01-04
Volume: 4
Issue: 1
Pages: 1-1
ISSN: 1475-2859 (ISSN-L)
DOI: 10.1186/1475-2859-4-1
PMC: PMC544838
OpenAlex: W1931534490
Cited by: 841
References: 83
Citations by year: 2026: 20 · 2025: 20 · 2024: 35 · 2023: 30 · 2022: 37 · 2021: 50 · 2020: 45 · 2019: 49 · 2018: 49 · 2017: 44 · 2016: 41 · 2015: 43 · 2014: 63 · 2013: 52 · 2012: 53
FWCI: 11.96
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/2.0/ (tdm)
creativecommons.org/licenses/by/2.0/ (vor)
Locations: Microbial Cell Factories (publishedVersion, cc-by)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
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: recombinant protein expression, soluble protein production, Escherichia coli, cytoplasmic expression, protein solubility, protein purification

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Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

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