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Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
Open accessAbstract
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).](/paper-figures/a092193d30ab4934b23ea2eda9585c6e/soluble-expression-of-recombinant-proteins-in-the-cytoplasm-of-escherichia-coli-figure-1.jpg)
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“Several reports have reviewed cyanobacterial species capable of producing H2 (Abed et al. 2009; Das and Veziroglu 2001; Dutta et al. 2005) including at least 14 genera cultivated under different growth conditions.”
From Renewable energy from Cyanobacteria: energy production optimization by metabolic pathway engineering (2011) · cites this paper as Dutta et al. 2005
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“Among these genera it was shown that Anabaena spp. were able to produce the highest amount of H2 (68 μmol mg−1 chl a h−1).”
From Renewable energy from Cyanobacteria: energy production optimization by metabolic pathway engineering (2011) · cites this paper as Dutta et al. 2005
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“Differences in osmolarity, translational machinery, pH and molecular chaperone function are all possible reasons that have been attributed for failure of a protein to fold correctly in a heterologus host [161, 163].”
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Metadata
- Authors
- Sørensen, H. P., & Mortensen, K. K.
- Affiliations
- Aarhus University (DK)
- Corresponding author
- Mortensen, Kim Kusk
- Venue
- Microbial Cell Factories
- Published
- 2005-01-04
- Volume
- 4
- Issue
- 1
- Pages
- 1-1
- ISSN
- 1475-2859 (ISSN-L)
- 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
- 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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