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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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Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
Hartl, F. U., & Hayer-Hartl, M. K. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,335
Miroux, B., & Walker, J. E. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0399 · Cited by 1,964
Strategies for achieving high-level expression of genes in Escherichia coli
Makrides, S. C. (1996) · Microbiological Reviews · doi:10.1128/mr.60.3.512-538.1996 · Cited by 1,287
Advanced genetic strategies for recombinant protein expression in Escherichia coli
Sørensen, H. P., & Mortensen, K. K. (2004) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2004.08.004 · Cited by 994
Self-citationKapust, R. B., & Waugh, D. S. (1999) · Protein Science · doi:10.1110/ps.8.8.1668 · Cited by 960
Rapid protein-folding assay using green fluorescent protein
Waldo, G. S., Standish, B. M., Berendzen, J., & Terwilliger, T. C. (1999) · Nature Biotechnology · doi:10.1038/10904 · Cited by 906
Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
Bessette, P. H., Åslund, F., Beckwith, J., & Georgiou, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13703 · Cited by 636
Stewart, E. J., Åslund, F., & Beckwith, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.19.5543 · Cited by 445
Kiefhaber, T., Rudolph, R., Kohler, H., & Büchner, J. (1991) · Nature Biotechnology · doi:10.1038/nbt0991-825 · Cited by 442
Research works printed but not linked: 1
- Held D, Yaeger K, Novy R: New coexpression vectors for expanded compatibilities in E. coli. InNovations. 2003, 18: 4-6.
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Song, J.-A., Koo, B., Chong, S.-H., Kim, K., Choi, D. K., Vu, T. T. T., Nguyen, M. T., Jeong, B., Ryu, H.-B., Kim, I., et al. (2014) · PLoS ONE · doi:10.1371/annotation/4b2acdb5-5bab-4bca-8fbc-f9f293b38ee0 · Cited by 2
Montano-Gutierrez, L. F., Sturrock, M., Farquhar, I., Correia, K., Shahrezaei, V., & Swain, P. S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.20.440667 · Cited by 2
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RetractedLi, J.-P., Zhang, H.-H., He, Z.-H., Tian, J.-B., Zheng, R., Tang, X., & Zheng, Y. (2026) · Chemical Engineering Journal · doi:10.1016/j.cej.2026.176120 · Cited by 1
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Ko, E., & Ahn, Y. (2018) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2018.03.003 · Cited by 1
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dos Santos, L. M., Cerqueira, M. P., Gaboardi, G. C., Magalhães, C. G., Donassolo, R. A., Rodrigues, R. R., Griep, E., Ferreira, M. R. A., Elefant, G. R., de Ávila, L. F. D. C., et al. (2020) · Brazilian Archives of Biology and Technology · doi:10.1590/1678-4324-2020190148 · Cited by 1
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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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