Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

Sørensen, Hans Peter; Mortensen, Kim Kusk

doi:10.1186/1475-2859-4-1

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

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

DOI 10.1186/1475-2859-4-1PMC PMC544838

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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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At least 14 genera of cyanobacteria are capable of producing H2.
“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
Anabaena spp. were able to produce the highest amount of H2 (68 μmol mg−1 chl a h−1).
“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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Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096 · see citing works
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 · see citing works
Over-production of Proteins inEscherichia coli: Mutant Hosts that Allow Synthesis of some Membrane Proteins and Globular Proteins at High Levels
Miroux, B., & Walker, J. E. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0399 · Cited by 1,964 · see citing works
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 1,278 · see citing works
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 971 · see citing works
Self-citation
Escherichia coli maltose‐binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
Kapust, R. B., & Waugh, D. S. (1999) · Protein Science · doi:10.1110/ps.8.8.1668 · Cited by 960 · see citing works
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 · see citing works
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 · see citing works
Protein Aggregation in vitro and in vivo: A Quantitative Model of the Kinetic Competition between Folding and Aggregation
Kiefhaber, T., Rudolph, R., Kohler, H., & Büchner, J. (1991) · Nature Biotechnology · doi:10.1038/nbt0991-825 · Cited by 442 · see citing works
Chaperone Coexpression Plasmids: Differential and Synergistic Roles of DnaK-DnaJ-GrpE and GroEL-GroES in Assisting Folding of an Allergen of Japanese Cedar Pollen, Cryj2, in Escherichia coli
Nishihara, K., Kanemori, M., Kitagawa, M., Yanagi, H., & Yura, T. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.5.1694-1699.1998 · Cited by 440 · see citing works
Production of Soluble Recombinant Proteins in Bacteria
Schein, C. H. (1989) · Nature Biotechnology · doi:10.1038/nbt1189-1141 · Cited by 435 · see citing works
Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins
Stewart, E. J., Åslund, F., & Beckwith, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.19.5543 · Cited by 432 · see citing works
Preparative protein refolding
Middelberg, A. P. J. (2002) · Trends in biotechnology · doi:10.1016/s0167-7799(02)02047-4 · Cited by 370 · see citing works
Protein aggregation in recombinant bacteria: biological role of inclusion bodies
Villaverde, A., & Carrió, M. (2003) · Biotechnology Letters · doi:10.1023/a:1025024104862 · Cited by 346 · see citing works
Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
Hammarström, M., Hellgren, N., van den Berg, S., Berglund, H., & Härd, T. (2002) · Protein Science · doi:10.1110/ps.22102 · Cited by 333 · see citing works
Overexpression of Trigger Factor Prevents Aggregation of Recombinant Proteins in Escherichia coli
Nishihara, K., Kanemori, M., Yanagi, H., & Yura, T. (2000) · Applied and Environmental Microbiology · doi:10.1128/aem.66.3.884-889.2000 · Cited by 306 · see citing works
Directed enzyme evolution
Farinas, E. T., Bülter, T., & Arnold, F. H. (2001) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(01)00261-0 · Cited by 304 · see citing works
Chaperonins govern growth of Escherichia coli at low temperatures
Ferrer, M., Chernikova, T. N., Yakimov, M. M., Golyshin, P. N., & Timmis, K. N. (2003) · Nature Biotechnology · doi:10.1038/nbt1103-1266 · Cited by 266 · see citing works
Crystal structures of fusion proteins with large‐affinity tags
Smyth, D. R., Mrozkiewicz, M. K., McGrath, W. J., Listwan, P., & Kobe, B. (2003) · Protein Science · doi:10.1110/ps.0243403 · Cited by 254 · see citing works
The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3)
Dumon-Seignovert, L., Cariot, G., & Vuillard, L. M. (2004) · Protein Expression and Purification · doi:10.1016/j.pep.2004.04.025 · Cited by 251 · see citing works
Predicting the Solubility of Recombinant Proteins in Escherichia coli
Wilkinson, D. L., & Harrison, R. G. (1991) · Nature Biotechnology · doi:10.1038/nbt0591-443 · Cited by 250 · see citing works
Predicting the Solubility of Recombinant Proteins in Escherichia coli
Harrison, R. G., & Bagajewicz, M. J. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2205-5_23 · Cited by 241 · see citing works
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities.
Deuerling, E., Patzelt, H., Vorderwülbecke, S., Rauch, T., Kramer, G., Schaffitzel, E., Mogk, A., Schulze‐Specking, A., Langen, H., & Bukau, B. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03370.x · Cited by 203 · see citing works
Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini.
Silber, K. R., Keiler, K. C., & Sauer, R. T. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.1.295 · Cited by 201 · see citing works
Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies 1 1Edited by R. Huber
Bach, H., Mazor, Y., Shaky, S., Shoham-Lev, A., Berdichevsky, Y., Gutnick, D. L., & Benhar, I. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4914 · Cited by 178 · see citing works
Engineering soluble proteins for structural genomics
Pédelacq, J. D., Piltch, E. M., Liong, E. C., Berendzen, J., Kim, C., Rho, B., Park, M. S., Terwilliger, T. C., & Waldo, G. S. (2002) · Nature Biotechnology · doi:10.1038/nbt732 · Cited by 177 · see citing works
Expression of Aggregation-Prone Recombinant Proteins at Low Temperatures: A Comparative Study of theEscherichia coli cspAandtacPromoter Systems
Vasina, J. A., & Baneyx, F. (1997) · Protein Expression and Purification · doi:10.1006/prep.1996.0678 · Cited by 175 · see citing works
High‐throughput screening of soluble recombinant proteins
Shih, Y., Kung, W., Chen, J., Yeh, C.-H., Wang, A. H. ‐., & Wang, T. (2002) · Protein Science · doi:10.1110/ps.0205202 · Cited by 170 · see citing works
Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL.
Amrein, K. E., Takács, B., Stieger, M., Molnos, J., Flint, N. A., & Burn, P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.4.1048 · Cited by 167 · see citing works
Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over‐production of the b subunit of F1Fo ATP synthase
Aréchaga, I., Miroux, B., Karrasch, S., Huijbregts, R. P. H., KRUIJFF, B. D., Runswick, M. J., & Walker, J. E. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02054-8 · Cited by 161 · see citing works
Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein
Wigley, W. C., Stidham, R. D., Smith, N. M., Hunt, J. F., & Thomas, P. (2001) · Nature Biotechnology · doi:10.1038/84389 · Cited by 160 · see citing works
Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology
Schlieker, C. D., Bukau, B., & Mogk, A. (2002) · Journal of Biotechnology · doi:10.1016/s0168-1656(02)00033-0 · Cited by 159 · see citing works
Optimization of heterologous protein production in Escherichia coli
Weickert, M. J., Doherty, D. H., Best, E. A., & Olins, P. O. (1996) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(96)80051-6 · Cited by 157 · see citing works
A simple in vivo assay for increased protein solubility
Maxwell, K. L., Mittermaier, A., Forman-Kay, J. D., & Davidson, A. R. (1999) · Protein Science · doi:10.1110/ps.8.9.1908 · Cited by 154 · see citing works
Single amino acid substitutions on the surface ofEscherichia colimaltose‐binding protein can have a profound impact on the solubility of fusion proteins
Fox, J. D., Kapust, R. B., & Waugh, D. S. (2001) · Protein Science · doi:10.1110/ps.45201 · Cited by 142 · see citing works
Genetic screens and directed evolution for protein solubility
Waldo, G. S. (2003) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00017-0 · Cited by 138 · see citing works
Protein aggregation during overexpression limited by peptide extensions with large net negative charge
Zhang, Y., Howitt, J. A., McCorkle, S., Lawrence, P., Springer, K., & Freimuth, P. (2004) · Protein Expression and Purification · doi:10.1016/j.pep.2004.04.020 · Cited by 130 · see citing works
Maltodextrin‐binding proteins from diverse bacteria and archaea are potent solubility enhancers
Fox, J. D., Routzahn, K. M., Bucher, M. H., & Waugh, D. S. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00070-x · Cited by 124 · see citing works
Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants
Kitagawa, M., 宮川, 瑞., Matsumura, Y., & Tsuchido, T. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02958.x · Cited by 119 · see citing works
The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock
Kuczyńska‐Wiśnik, D., Kędzierska‐Mieszkowska, S., Matuszewska, E., Lund, P. A., Taylor, A., Lipińska, B., & Laskowska, E. (2002) · Microbiology · doi:10.1099/00221287-148-6-1757 · Cited by 113 · see citing works
Gene expression response to misfolded protein as a screen for soluble recombinant protein
Lesley, S. A., Graziano, J., Cho, C. Y., Knuth, M. W., & Klock, H. E. (2002) · Protein Engineering Design and Selection · doi:10.1093/protein/15.2.153 · Cited by 113 · see citing works
Expression of Eukaryotic Proteins in Soluble Form inEscherichia coli
Zhang, Y., Olsen, D. R., Nguyen, K. B., Olson, P. S., Rhodes, E. T., & Mascarenhas, D. D. (1998) · Protein Expression and Purification · doi:10.1006/prep.1997.0834 · Cited by 105 · see citing works
A strategy for optimizing the monodispersity of fusion proteins: application to purification of recombinant HPV E6 oncoprotein
Nominé, Y., Ristriani, T., Laurent, C., Lefèvre, J., Weiss, É., & Travé, G. (2001) · Protein Engineering Design and Selection · doi:10.1093/protein/14.4.297 · Cited by 104 · see citing works
Mechanisms of Protein Folding: Molecular Chaperones and Their Application in Biotechnology
Mogk, A., Mayer, M. P., & Deuerling, E. (2002) · ChemBioChem · doi:10.1002/1439-7633(20020902)3:9 · Cited by 92 · see citing works
Expression of a Temperature-Sensitive Esterase in a Novel Chaperone-Based Escherichia coli Strain
Ferrer, M., Chernikova, T. N., Timmis, K. N., & Golyshin, P. N. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.8.4499-4504.2004 · Cited by 87 · see citing works
Improving protein solubility through rationally designed amino acid replacements: solubilization of the trimethoprim-resistant type S1 dihydrofolate reductase
Dale, G. E., Broger, C., Langen, H., Arcy, A. D., & Stüber, D. (1994) · Protein Engineering Design and Selection · doi:10.1093/protein/7.7.933 · Cited by 78 · see citing works
Identification of C-terminal extensions that protect proteins from intracellular proteolysis
Bowie, J. U., & Sauer, R. T. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83276-8 · Cited by 78 · see citing works
Recombinant protein expression at low temperatures under the transcriptional control of the major Escherichia coli cold shock promoter cspA
Vasina, J. A., & Baneyx, F. (1996) · Applied and Environmental Microbiology · doi:10.1128/aem.62.4.1444-1447.1996 · Cited by 76 · see citing works
Low temperatures stabilize interferon ?-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli
Chesshyre, J. A., & Hipkiss, A. R. (1989) · Applied Microbiology and Biotechnology · doi:10.1007/bf00262455 · Cited by 72 · see citing works
Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins
Routzahn, K. M., & Waugh, D. S. (2002) · Journal of Structural and Functional Genomics · doi:10.1023/a:1020424023207 · Cited by 71 · see citing works
Synthesis of Macromolecules by Escherichia coli near the Minimal Temperature for Growth
Shaw, M. K., & Ingraham, J. L. (1967) · Journal of Bacteriology · doi:10.1128/jb.94.1.157-164.1967 · Cited by 68 · see citing works
A favorable solubility partner for the recombinant expression of streptavidin
Sørensen, H. P., Sperling‐Petersen, H. U., & Mortensen, K. K. (2003) · Protein Expression and Purification · doi:10.1016/j.pep.2003.07.001 · Cited by 67 · see citing works
Self-citation
High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2
Lehmann, K., Hoffmann, S., Neudecker, P., Suhr, M., Becker, W., & ROSCH, P. J. (2003) · Protein Expression and Purification · doi:10.1016/s1046-5928(03)00190-6 · Cited by 62 · see citing works
Cold-inducible cloning vectors for low-temperature protein expression in Escherichia coli: application to the production of a toxic and proteolytically sensitive fusion protein
Mujacic, M., Cooper, K. W., & Baneyx, F. (1999) · Gene · doi:10.1016/s0378-1119(99)00328-5 · Cited by 57 · see citing works
Production of recombinant thermostable proteins expressed in Escherichia coli: completion of protein synthesis is the bottleneck
Sørensen, H. P., Sperling‐Petersen, H. U., & Mortensen, K. K. (2003) · Journal of Chromatography B · doi:10.1016/s1570-0232(02)00689-x · Cited by 55 · see citing works
Self-citation
Highly efficient over-production in E. coli of YvcC, a multidrug-like ATP-binding cassette transporter from Bacillus subtilis
Steinfels, E., Orelle, C., Dalmas, O., Pénin, F., Miroux, B., Pietro, A. D., & Jault, J. (2002) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(02)00515-1 · Cited by 52 · see citing works
A system for purification of recombinant proteins in Escherichia coli via artificial oil bodies constituted with their oleosin-fused polypeptides
Peng, C., Chen, J. C. F., Shyu, D. J. H., Chen, M.-J., & Tzen, J. T. C. (2004) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2004.03.013 · Cited by 49 · see citing works
A Mutation That Improves Soluble Recombinant Hemoglobin Accumulation in Escherichia coli in Heme Excess
Weickert, M. J., Pagratis, M., Glascock, C. B., & Blackmore, R. S. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.2.640-647.1999 · Cited by 48 · see citing works
The application of multi-parameter flow cytometry to the study of recombinant Escherichia coli batch fermentation processes
Lewis, G., Taylor, I. W., Nienow, A. W., & Hewitt, C. J. (2004) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-004-0151-8 · Cited by 47 · see citing works
Expression of a Recombinant Toxoplasma gondii ROP2 Fragment as a Fusion Protein in Bacteria Circumvents Insolubility and Proteolytic Degradation
Jacquet, A., Daminet, V., Haumont, M., Garcia, L., Chaudoir, S., Bollen, A., & Biemans, R. (1999) · Protein Expression and Purification · doi:10.1006/prep.1999.1150 · Cited by 46 · see citing works
Production of a Functional Catalytic Antibody ScFv-NusA Fusion Protein in Bacterial Cytoplasm
Zheng, L. (2003) · The Journal of Biochemistry · doi:10.1093/jb/mvg074 · Cited by 43 · see citing works
An unusual halotolerant α-type carbonic anhydrase from the alga Dunaliella salina functionally expressed in Escherichia coli
Premkumar, L., Bageshwar, U. K., Gokhman, I., Zamir, A., & Sussman, J. L. (2003) · Protein Expression and Purification · doi:10.1016/s1046-5928(02)00683-6 · Cited by 39 · see citing works
CO-OVEREXPRESSION OF FOLDING MODULATORS IMPROVES THE SOLUBILITY OF THE RECOMBINANT GUINEA PIG LIVER TRANSGLUTAMINASE EXPRESSED INESCHERICHIA COLI
Ikura, K., Kokubu, T., Natsuka, S., Ichikawa, A., Adachi, M., Nishihara, K., Yanagi, H., & Utsumi, S. (2002) · Preparative Biochemistry & Biotechnology · doi:10.1081/pb-120004130 · Cited by 38 · see citing works
Over‐expression of Escherichia coli F1Fo–ATPase subunit a is inhibited by instability of the uncB gene transcript
Aréchaga, I., Miroux, B., Runswick, M. J., & Walker, J. E. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00677-x · Cited by 37 · see citing works
Visualization of coupled protein folding and binding in bacteria and purification of the heterodimeric complex
Wang, H., & Chong, S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0236088100 · Cited by 37 · see citing works
Extra terminal residues have a profound effect on the folding and solubility of a Plasmodium falciparum sexual stage‐specific protein over‐expressed in Escherichia coli
Sati, S. P., Singh, S. K., Kumar, N., & Sharma, A. K. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03237.x · Cited by 35 · see citing works
Optimal Induction of Protein Synthesis in Recombinant Bacterial Culturesa
Bentley, W. E., & Kompala, D. S. (1990) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1990.tb24239.x · Cited by 35 · see citing works
The effect of molecular chaperones on in vivo and in vitro folding processes.
Schwarz, E., Lilie, H., & Rudolph, R. (1997) · PubMed · Cited by 35 · see citing works
High-level expression of a soluble snake venom enzyme, gloshedobin, in E. coli in the presence of metal ions
Yang, Q. K., Xu, J., Li, M., Lei, X., & An, L. (2003) · Biotechnology Letters · doi:10.1023/a:1023067626846 · Cited by 31 · see citing works
Fusion of the antiferritin antibody VL domain to barnase results in enhanced solubility and altered pH stability
Martsev, S. P., Tsybovsky, Y., Stremovskiy, O. A., Odintsov, S. G., Balandin, T. G., Arosio, P., Kravchuk, Z. I., & Deyev, S. M. (2004) · Protein Engineering Design and Selection · doi:10.1093/protein/gzh011 · Cited by 31 · see citing works
Expression of foreign proteins in Escherichia coli by fusing with an archaeal FK506 binding protein
Ideno, A., Furutani, M., Iwabuchi, T., Iida, T., Iba, Y., Kurosawa, Y., Sakuraba, H., Ohshima, T., Kawarabayashi, Y., & Maruyama, T. (2004) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-003-1459-4 · Cited by 30 · see citing works
Soluble expression of aggregating proteins by covalent coupling to the ribosome
Sørensen, H. P., Kristensen, J. E., Petersen, H. U., & Mortensen, K. K. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.081 · Cited by 26 · see citing works
Self-citation
Soluble expression of a functionally active Plasmodium falciparum falcipain-2 fused to maltose-binding protein in Escherichia coli
Goh, L. L., Loke, P., Singh, M., & Sim, T. S. (2003) · Protein Expression and Purification · doi:10.1016/s1046-5928(03)00225-0 · Cited by 22 · see citing works
Expression, purification, and initial characterization of a recombinant form of plant PEP-carboxylase kinase from CAM-induced Mesembryanthemum crystallinum with enhanced solubility in Escherichia coli
Ermolova, N. V., Cushman, M. A., Taybi, T., Condon, S. A., Cushman, J. C., & Chollet, R. (2003) · Protein Expression and Purification · doi:10.1016/s1046-5928(03)00014-7 · Cited by 21 · see citing works
Purification and folding of recombinant bovine oxoglutarate/malate carrier by immobilized metal-ion affinity chromatography
Smith, V. R. P., & Walker, J. E. (2003) · Protein Expression and Purification · doi:10.1016/s1046-5928(03)00064-0 · Cited by 19 · see citing works
A system using convertible vectors for screening soluble recombinant proteins produced in Escherichia coli from randomly fragmented cDNAs
Nakayama, M., & Ohara, O. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.10.193 · Cited by 19 · see citing works
High-yield expression and purification of p18 form of Bax as an MBP-fusion protein
Eliseev, R. A., Alexandrov, A., & Gunter, T. E. (2004) · Protein Expression and Purification · doi:10.1016/j.pep.2004.01.015 · Cited by 13 · see citing works
Novel approach to obtain biologically active recombinant heterodimeric proteins in Escherichia coli
Austin, C. A. (2003) · Journal of Chromatography B · doi:10.1016/s1570-0232(02)00720-1 · Cited by 12 · see citing works
Flow cytometry studies of recombinant Escherichia coli in batch and continuous cultures: DNA and RNA contents; light-scatter parameters
Fouchet, P., Manin, C., Richard, H. B., Frelat, G., & Barbotin, J. N. (1994) · Applied Microbiology and Biotechnology · doi:10.1007/bf00178494 · Cited by 12 · see citing works
Co-expression of gene 31 and 23 products of bacteriophage T4.
Kurochkina, L. P., & Mesyanzhinov, V. V. (1999) · PubMed · Cited by 2 · see citing works
Untitled work
Davis (1999) · doi:10.1002/(sici)1097-0290(19991120)65:4

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2 of the 83 references couldn’t be matched to a known paper.

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The CamSol method of rational design of protein mutants with enhanced solubility
Sormanni, P., Aprile, F. A., & Vendruscolo, M. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.09.026 · Cited by 494 · see citing works
“Effective experimental approaches to improve protein solubility during recombinant expression include the use of weak promoters, modified growth media, low temperatures, and solubility-enhancing tags [23–25] or large-scale screening and random mutagenesis [26,27].”
Microbial factories for recombinant pharmaceuticals
Ferrer‐Miralles, N., Domingo‐Espín, J., Corchero, J. L., Vázquez, E., & Villaverde, A. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-17 · Cited by 465 · see citing works
“By adjusting media composition, growth temperature, inducer concentration, promoter strength and plasmid copy number, variable amounts of the target protein can be forced to appear in the soluble form [26,27], although unfortunately, many eukaryotic proteins are exclusively found trapped in IBs and seem to be resistan…”
Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system
Costa, S. M., ALMEIDA, A. A., CASTRO, A. O., & Domingues, L. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00063 · Cited by 455 · see citing works
“…also boosted the biopharmaceutical industry: 30% of the recombinant biopharmaceuticals licensed up to 2011 by the U.S. Food and Drug Administration (FDA) and European Medicines Agency (EMEA) were obtained using this host cell (Ferrer-Miralles et al., 2009; Walsh, 2010; Berlec and Strukelj, 2013).”
Bacteriocins Produced by Lactic Acid Bacteria a Review Article
Zacharof, M., & Lovitt, R. W. (2012) · APCBEE Procedia · doi:10.1016/j.apcbee.2012.06.010 · Cited by 431 · see citing works
Strategies for optimization of heterologous protein expression in E. coli: Roadblocks and reinforcements
Kaur, J., Kumar, A., & Kaur, J. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.08.080 · Cited by 412 · see citing works
Catalase and ascorbate peroxidase—representative H2O2-detoxifying heme enzymes in plants
Anjum, N. A., Sharma, P., Gill, S. S., Hasanuzzaman, M., Khan, E. A., Kachhap, K., Mohamed, A. A., Thangavel, P., Devi, G. D., Vasudhevan, P., et al. (2016) · Environmental Science and Pollution Research · doi:10.1007/s11356-016-7309-6 · Cited by 403 · see citing works
Protein quality in bacterial inclusion bodies
Ventura, S., & Villaverde, A. (2006) · Trends in biotechnology · doi:10.1016/j.tibtech.2006.02.007 · Cited by 382 · see citing works
Renewable energy from Cyanobacteria: energy production optimization by metabolic pathway engineering
Quintana, N., Van der Kooy, F., Van de Rhee, M. D., Voshol, G. P., & Verpoorte, R. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3394-0 · Cited by 338 · see citing works
Production of Biopharmaceuticals in E. coli: Current Scenario and Future Perspectives
Baeshen, M. N., Al-Hejin, A. M., Bora, R. S., Ahmed, M. M. M., Ramadan, H. A. I., Saini, K. S., Baeshen, N. A., & Redwan, E. M. (2015) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.1412.12079 · Cited by 330 · see citing works
Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview
Gasser, B., Saloheimo, M., Rinas, U., Dragosits, M., Rodríguez‐Carmona, E., Baumann, K., Giuliani, M., Parrilli, E., Branduardi, P., Lang, C., et al. (2008) · Microbial Cell Factories · doi:10.1186/1475-2859-7-11 · Cited by 327 · see citing works
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins
García‐Fruitós, E., González‐Montalbán, N., Morell, M., Vera, A., Ferraz, R. M., Arı́s, A., Ventura, S., & Villaverde, A. (2005) · Microbial Cell Factories · doi:10.1186/1475-2859-4-27 · Cited by 320 · see citing works
“In this context, soluble micro-aggregates have been described [11] and recently characterized in detail [12].”
Recombinant production of antimicrobial peptides in Escherichia coli: A review
Li, Y. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.08.001 · Cited by 307 · see citing works
BacArena: Individual-based metabolic modeling of heterogeneous microbes in complex communities
Bauer, E., Zimmermann, J., Baldini, F., Thiele, I., & Kaleta, C. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005544 · Cited by 308 · see citing works
High-throughput recombinant protein expression in Escherichia coli : current status and future perspectives
Jia, B., & Jeon, C. O. (2016) · Open Biology · doi:10.1098/rsob.160196 · Cited by 295 · see citing works
“The addition of the cofactors or binding partners required for protein folding to the cultivation media will enhance protein solubility and prevent inclusion body formation [151,152].”
The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures
Vera, A., González‐Montalbán, N., Arı́s, A., & Villaverde, A. (2006) · Biotechnology and Bioengineering · doi:10.1002/bit.21218 · Cited by 258 · see citing works
Antifungal Plant Defensins: Mechanisms of Action and Production
Vriens, K., Cammue, B. P. A., & Thevissen, K. (2014) · Molecules · doi:10.3390/molecules190812280 · Cited by 229 · see citing works
Recombinant protein production in bacterial hosts
Overton, T. W. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.11.008 · Cited by 221 · see citing works
Regulation Systems of Bacteria such as Escherichia coli in Response to Nutrient Limitation and Environmental Stresses
Shimizu, K. (2013) · Metabolites · doi:10.3390/metabo4010001 · Cited by 204 · see citing works
“Small heat shock proteins such as IbpA and IbpB protect heat-denatured proteins from irreversible changes in association with inclusion bodies [169,170].”
Expression systems for heterologous production of antimicrobial peptides
Parachin, N. S., Mulder, K. C. L., Viana, A. A. B., Dias, S. C., & Franco, O. L. (2012) · Peptides · doi:10.1016/j.peptides.2012.09.020 · Cited by 197 · see citing works
Advanced microalgae-based renewable biohydrogen production systems: A review
Goswami, R. K., Mehariya, S., Obulisamy, P. K., & Verma, P. (2021) · Bioresource Technology · doi:10.1016/j.biortech.2020.124301 · Cited by 189 · see citing works
Metabolic engineering of Escherichia coli for high-level astaxanthin production with high productivity
Park, S. Y., Binkley, R. M., Kim, W. J., Lee, M. H., & Lee, S. Y. (2018) · Metabolic Engineering · doi:10.1016/j.ymben.2018.08.002 · Cited by 182 · see citing works
Overcoming genetic heterogeneity in industrial fermentations
Rugbjerg, P., & Sommer, M. O. A. (2019) · Nature Biotechnology · doi:10.1038/s41587-019-0171-6 · Cited by 183 · see citing works
Production of glycoprotein vaccines in Escherichia coli
Ihssen, J., Kowarik, M., Dilettoso, S., Tanner, C., Wacker, M., & Thöny‐Meyer, L. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-61 · Cited by 180 · see citing works
Fusion tags to enhance heterologous protein expression
Ki, M., & Pack, S. P. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10402-8 · Cited by 180 · see citing works
Sustainability and cyanobacteria (blue-green algae): facts and challenges
Sharma, N. K., Tiwari, S. P., Tripathi, K., & Rai, A. K. (2010) · Journal of Applied Phycology · doi:10.1007/s10811-010-9626-3 · Cited by 178 · see citing works
Effect of temperature on protein quality in bacterial inclusion bodies
de Groot, N. S., & Ventura, S. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.071 · Cited by 178 · see citing works
“A widespread strategy to reduce the in vivo aggregation of recombinant polypeptides consists of cultivation at reduced temperatures [9].”
Bacterial Inclusion Bodies: Discovering Their Better Half
Rinas, U., García‐Fruitós, E., Corchero, J. L., Vázquez, E., Seras‐Franzoso, J., & Villaverde, A. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.01.005 · Cited by 175 · see citing works
Engineering inclusion bodies for non denaturing extraction of functional proteins
Peternel, Š., Grdadolnik, J., Gaberc‐Porekar, V., & Komel, R. (2008) · Microbial Cell Factories · doi:10.1186/1475-2859-7-34 · Cited by 166 · see citing works
“To avoid time consuming and often unfavorable renaturation procedures, a lot of effort has been made to produce soluble proteins in bacteria either by altering the production process [1, 2 ], by co-expression of chaperones [3,4] or by altering the target protein (point mutations, fusion proteins) [5,6].”
Statistical approaches to maximize recombinant protein expression in Escherichia coli: A general review
Papaneophytou, C. P., & Kontopidis, G. A. (2013) · Protein Expression and Purification · doi:10.1016/j.pep.2013.10.016 · Cited by 165 · see citing works
Engineering cell physiology to enhance recombinant protein production in Escherichia coli
Chou, C.-H. P. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-1039-0 · Cited by 161 · see citing works
Computational Design of Stable and Soluble Biocatalysts
Musil, M., Konegger, H., Hon, J., Bednář, D., & Damborský, J. (2018) · ACS Catalysis · doi:10.1021/acscatal.8b03613 · Cited by 155 · see citing works
Vanillin production using metabolically engineered Escherichia coli under non-growing conditions
Barghini, P., Gioia, D. D., Fava, F., & Ruzzi, M. (2007) · Microbial Cell Factories · doi:10.1186/1475-2859-6-13 · Cited by 156 · see citing works
“A decrease in cultivation temperature affects replication, transcription and translation resulting in a decrease of the bacterial growth and in a reduction of cellular protein concentration, but, at the same time, reduces the harmful effects of the production of toxic stress proteins [ 28 ].”
Strategies for efficient and economical 2,3-butanediol production: new trends in this field
Białkowska, A. M. (2016) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-016-2161-x · Cited by 155 · see citing works
Screening of fusion partners for high yield expression and purification of bioactive viscotoxins
Bogomolovas, J., Simon, B., Sattler, M., & Stier, G. (2008) · Protein Expression and Purification · doi:10.1016/j.pep.2008.10.003 · Cited by 145 · see citing works
Effects of flocculants on lipid extraction and fatty acid composition of the microalgae Nannochloropsis oculata and Thalassiosira weissflogii
Borges, L. D. V., Morón-Villarreyes, J. A., D’Oca, M. G. M., & Abreu, P. C. (2011) · Biomass and Bioenergy · doi:10.1016/j.biombioe.2011.09.003 · Cited by 139 · see citing works
Engineering NADH/NAD+ ratio in Halomonas bluephagenesis for enhanced production of polyhydroxyalkanoates (PHA)
Chen, L., Qiao, G., Shuai, B., Olavarría, K., Yin, J., Xiang, R., Song, K., Shen, Y.-H., Guo, Y., & Chen, G. (2018) · Metabolic Engineering · doi:10.1016/j.ymben.2018.09.007 · Cited by 138 · see citing works
Cloning, sequencing and expression of a novel glutamate decarboxylase gene from a newly isolated lactic acid bacterium, Lactobacillus brevis OPK-3
Park, K.-B., & Oh, S. (2006) · Bioresource Technology · doi:10.1016/j.biortech.2006.01.004 · Cited by 134 · see citing works
Unconventional microbial systems for the cost-efficient production of high-quality protein therapeutics
Corchero, J. L., Gasser, B., Resina, D., Smith, W., Parrilli, E., Vázquez, F., Abasolo, I., Giuliani, M., Jäntti, J., Ferrer, P., et al. (2013) · Biotechnology Advances · doi:10.1016/j.biotechadv.2012.09.001 · Cited by 133 · see citing works
Effect of osmotic stress and heat shock in recombinant protein overexpression and crystallization
Oganesyan, N., Ankoudinova, I., Kim, S., & Kim, R. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2006.09.015 · Cited by 132 · see citing works
A review on mechanism and future perspectives of cadmium-resistant bacteria
Abbas, S. Z., Rafatullah, M., Hossain, K., Ismail, N., Tajarudin, H. A., & Khalil, H. P. S. A. (2017) · International Journal of Environmental Science and Technology · doi:10.1007/s13762-017-1400-5 · Cited by 132 · see citing works
Impact of the Expression System on Recombinant Protein Production in Escherichia coli BL21
Terol, G. L., Gallego‐Jara, J., Martínez, R. A. S., Vivancos, A. M., Díaz, M. C., & Puente, T. D. D. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.682001 · Cited by 130 · see citing works
Preparation of NIR-responsive, ROS-generating and antibacterial black phosphorus quantum dots for promoting the MRSA-infected wound healing in diabetic rats
Huang, S., Xu, S., Hu, Y., Zhao, X., Chang, L., Chen, Z., & Mei, X. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.10.008 · Cited by 130 · see citing works
Recombinant protein solubility—does more mean better?
González‐Montalbán, N., García‐Fruitós, E., & Villaverde, A. (2007) · Nature Biotechnology · doi:10.1038/nbt0707-718 · Cited by 130 · see citing works
Side effects of chaperone gene co-expression in recombinant protein production
Martínez‐Alonso, M., García‐Fruitós, E., Ferrer‐Miralles, N., Rinas, U., & Villaverde, A. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-64 · Cited by 123 · see citing works
Sequence determinants of protein aggregation: tools to increase protein solubility
Ventura, S. (2005) · Microbial Cell Factories · doi:10.1186/1475-2859-4-11 · Cited by 119 · see citing works
Metabolic Regulation of a Bacterial Cell System with Emphasis onEscherichia coliMetabolism
Shimizu, K. (2013) · ISRN Biochemistry · doi:10.1155/2013/645983 · Cited by 117 · see citing works
Non-invasive microelectrode ion flux measurements to study adaptive responses of microorganisms to the environment
Shabala, L., Ross, T., McMeekin, T. A., & Shabala, S. N. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00019.x · Cited by 114 · see citing works
Bacterial inclusion bodies are industrially exploitable amyloids
de Marco, A., Ferrer‐Miralles, N., García‐Fruitós, E., Mitraki, A., Peternel, Š., Rinas, U., Trujillo‐Roldán, M. A., Valdez‐Cruz, N. A., Vázquez, E., & Villaverde, A. (2018) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuy038 · Cited by 109 · see citing works
Enzyme Engineering for In Situ Immobilization
Rehm, F. B. H., Chen, S., & Rehm, B. H. A. (2016) · Molecules · doi:10.3390/molecules21101370 · Cited by 108 · see citing works
Production of soluble recombinant proteins in Escherichia coli: Effects of process conditions and chaperone co-expression on cell growth and production of xylanase
Jhamb, K., & Sahoo, D. K. (2012) · Bioresource Technology · doi:10.1016/j.biortech.2012.07.011 · Cited by 106 · see citing works
Critical Factors Affecting the Success of Cloning, Expression, and Mass Production of Enzymes by RecombinantE. coli
Fakruddin, M., Mazumdar, R. M., Mannan, K. S. B., Chowdhury, A., & Hossain, M. N. (2012) · ISRN Biotechnology · doi:10.5402/2013/590587 · Cited by 105 · see citing works
Bioinformatics in microbial biotechnology – a mini review
Bansal, A. K. (2005) · Microbial Cell Factories · doi:10.1186/1475-2859-4-19 · Cited by 105 · see citing works
Genome engineering for improved recombinant protein expression in Escherichia coli
Mahalik, S., Sharma, A. K., & Mukherjee, K. J. (2014) · Microbial Cell Factories · doi:10.1186/s12934-014-0177-1 · Cited by 103 · see citing works
Assessment of Environmental Stresses for Enhanced Microalgal Biofuel Production â€“ An Overview
Cheng, D., & He, Q. (2014) · Frontiers in Energy Research · doi:10.3389/fenrg.2014.00026 · Cited by 106 · see citing works
Recombinant production of eukaryotic cytochrome P450s in microbial cell factories
Hausjell, J., Halbwirth, H., & Oliver Spadiut, A. (2018) · Bioscience Reports · doi:10.1042/bsr20171290 · Cited by 99 · see citing works
Molecular cloning and characterization of a novel metagenome-derived multicopper oxidase with alkaline laccase activity and highly soluble expression
Ye, M., Li, G., Liang, W. Q., & Liu, Y. H. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2507-5 · Cited by 98 · see citing works
Surface Display Technology for Biosensor Applications: A Review
Park, M. (2020) · Sensors · doi:10.3390/s20102775 · Cited by 96 · see citing works
Functional characterization and synergic action of fungal xylanase and arabinofuranosidase for production of xylooligosaccharides
Gonçalves, T. A., Damásio, A., Segato, F., Alvarez, T. M., Bragatto, J. M., Brenelli, L. B., Citadini, A. P., Murakami, M. T., Ruller, R., Leme, A. F. P., et al. (2012) · Bioresource Technology · doi:10.1016/j.biortech.2012.05.062 · Cited by 94 · see citing works
Comparative genomics in acid mine drainage biofilm communities reveals metabolic and structural differentiation of co-occurring archaea
Yelton, A. P., Comolli, L. R., Justice, N. B., Castelle, C. J., Denef, V. J., Thomas, B. C., & Banfield, J. F. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-485 · Cited by 94 · see citing works
An insight into fusion technology aiding efficient recombinant protein production for functional proteomics
Yadav, D. K., Yadav, N., Yadav, S., Haque, S., & Tuteja, N. K. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.10.012 · Cited by 94 · see citing works
Engineered yeast with a CO2-fixation pathway to improve the bio-ethanol production from xylose-mixed sugars
Li, Y., Wang, M., Chen, Y., Wang, M., Fan, L., & Tan, T. (2017) · Scientific Reports · doi:10.1038/srep43875 · Cited by 95 · see citing works
Novel, Versatile, and Tightly Regulated Expression System for E scherichia coli Strains
Choi, Y. J., Morel, L., Le François, T., Bourque, D., Bourget, L., Groleau, D., Massie, B., & Míguez, C. B. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00413-10 · Cited by 94 · see citing works
A strategy for high-level expression of soluble and functional human interferon α as a GST-fusion protein in E.coli
Rabhi, I., Sadok, A., Khalaf, N. B., & Fathallah, D. M. (2007) · Protein Engineering Design and Selection · doi:10.1093/protein/gzm012 · Cited by 93 · see citing works
Divergent Genetic Control of Protein Solubility and Conformational Quality in Escherichia coli
García‐Fruitós, E., Martínez‐Alonso, M., González‐Montalbán, N., Valli, M., Mattanovich, D., & Villaverde, A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.09.004 · Cited by 92 · see citing works
The novel Fh8 and H fusion partners for soluble protein expression in Escherichia coli: a comparison with the traditional gene fusion technology
Costa, S. J., ALMEIDA, A. A., CASTRO, A. O., Domingues, L., & Besir, H. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4559-1 · Cited by 90 · see citing works
“Several efforts have been exploited to prevent recombinant protein aggregation and to improve its soluble production by the use of different promoters, expression strains and induction conditions, co-expression of chaperones, and soluble fusion partners (Berrow et al. 2006; Makino et al. 2011; Pacheco et al. 2012; Sor…”
The heterologous expression strategies of antimicrobial peptides in microbial systems
Deng, T., Ge, H., He, H., Liu, Y., Zhai, C., Feng, L., & Li, Y. (2017) · Protein Expression and Purification · doi:10.1016/j.pep.2017.08.003 · Cited by 89 · see citing works
Technical methods to improve yield, activity and stability in the development of microbial lipases
Shu, Z., Jiang, H., Lin, R., Jiang, Y., Lin, L., & Huang, J. (2009) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2009.09.003 · Cited by 88 · see citing works
Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusion bodies
Doglia, S. M., Ami, D., Natalello, A., Gatti‐Lafranconi, P., & Lotti, M. (2008) · Biotechnology Journal · doi:10.1002/biot.200700238 · Cited by 84 · see citing works
Expression of Candida antarctica lipase B in Pichia pastoris and various Escherichia coli systems
Larsen, M. W., Bornscheuer, U. T., & Hult, K. (2008) · Protein Expression and Purification · doi:10.1016/j.pep.2008.07.012 · Cited by 84 · see citing works
High-yield production of functional soluble single-domain antibodies in the cytoplasm of Escherichia coli
Zarschler, K., Witecy, S., Kapplusch, F., Foerster, C., & Stephan, H. (2013) · Microbial Cell Factories · doi:10.1186/1475-2859-12-97 · Cited by 84 · see citing works
Yeast as an expression system for producing virus-like particles: what factors do we need to consider?
Kim, H. J., & Kim, H.-J. (2016) · Letters in Applied Microbiology · doi:10.1111/lam.12695 · Cited by 83 · see citing works
Classification of lipolytic enzymes and their biotechnological applications in the pulping industry
Ramnath, L., Sithole, B. B., & Govinden, R. (2016) · Canadian Journal of Microbiology · doi:10.1139/cjm-2016-0447 · Cited by 81 · see citing works
Learning about protein solubility from bacterial inclusion bodies
Martínez‐Alonso, M., González‐Montalbán, N., García‐Fruitós, E., & Villaverde, A. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-4 · Cited by 80 · see citing works
“Eventually, recombinant protein solubility could be merely dependent on the intracellular concentration of the recombinant protein itself, what would ultimately fit with the enhanced solubility observed at low growth rates, low temperatures and weak doses of gene expression inductor [36,41].”
Expression and functional characterization of the plant antimicrobial snakin-1 and defensin recombinant proteins
Kovalskaya, N. Y., & Hammond, R. W. (2008) · Protein Expression and Purification · doi:10.1016/j.pep.2008.08.013 · Cited by 80 · see citing works
Advances in Applied Biotechnology
Juodeikienė, G., Bartkienė, E., Viškelis, P., Urbonavičienė, D., Eidukonytė, D., & Bobinas, Č. (2012) · InTech eBooks · doi:10.5772/1096 · Cited by 80 · see citing works
Overexpression and simple purification of the Thermotoga maritima 6-phosphogluconate dehydrogenase in Escherichia coli and its application for NADPH regeneration
Wang, Y., & Zhang, Y. P. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-30 · Cited by 79 · see citing works
“coli rare tRNA genes [22], (ii) enhancing protein folding in a host co-expressing folding modulators, such as chaperons [17,23], (iii) decreasing formation of disulfide bond in some special host's cytoplasm [24], and (iv) repressing basal expression of a toxic protein in a host with a repressor [25].”
Efficient production of xylitol from hemicellulosic hydrolysate using engineered Escherichia coli
Su, B., Wu, M., Zhang, Z., Lin, J., & Yang, L. (2015) · Metabolic Engineering · doi:10.1016/j.ymben.2015.07.003 · Cited by 78 · see citing works
From Water and Ions to Crowded Biomacromolecules: In Vivo Structuring of a Prokaryotic Cell
Spitzer, J. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00010-11 · Cited by 77 · see citing works
Heterologous protein secretion byLactobacillus plantarumusing homologous signal peptides
Mathiesen, G., Sveen, A., Piard, J.-C., Axelsson, L. T., & Eijsink, V. G. H. (2008) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2008.03734.x · Cited by 75 · see citing works
Towards universal systems for recombinant gene expression
Sørensen, H. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-27 · Cited by 74 · see citing works
Self-citation
Chromium recovery from tannery sludge by bioleaching and its reuse in tanning process
Ma, H., Zhou, J., Li, H., Cheng, F., Zhou, L., & Qiao, X. (2016) · Journal of Cleaner Production · doi:10.1016/j.jclepro.2016.10.193 · Cited by 73 · see citing works
Solubility of recombinant Src homology 2 domains expressed in E. colican be predicted by TANGO
Andersen, T. C. B., Lindsjø, K., Hem, C. D., Koll, L., Kristiansen, P. E., Skjeldal, L., Andreotti, A. H., & Spurkland, A. (2014) · BMC Biotechnology · doi:10.1186/1472-6750-14-3 · Cited by 72 · see citing works
“recombinant proteins have previously been reported [15,21].”
Improved bio-catalytic conversion by novel immobilization process using cryogel beads to increase solvent production
Tripathi, A., Sami, H., Jain, S. R., Viloria-Cols, M., Zhuravleva, N., Nilsson, G. N., Jungvid, H., & Kumar, A. (2010) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2010.03.009 · Cited by 71 · see citing works
Supramolecular organization of protein-releasing functional amyloids solved in bacterial inclusion bodies
Cano‐Garrido, O., Rodríguez‐Carmona, E., Gil, C. D., Vázquez, E., Elizondo, E., Cubarsí, R., Seras‐Franzoso, J., Corchero, J. L., Rinas, U., Ratera, I., et al. (2012) · Acta Biomaterialia · doi:10.1016/j.actbio.2012.11.033 · Cited by 70 · see citing works
Active Protein Aggregates Produced in Escherichia coli
Peternel, Š., & Komel, R. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12118275 · Cited by 69 · see citing works
Cloning, Expression, and Structural Elucidation of a Biotechnologically Potential Alkaline Serine Protease From a Newly Isolated Haloalkaliphilic Bacillus lehensis JO-26
Bhatt, H. B., & Singh, S. P. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00941 · Cited by 68 · see citing works
Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology
Gatti‐Lafranconi, P., Natalello, A., Ami, D., Doglia, S. M., & Lotti, M. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08163.x · Cited by 67 · see citing works
Waste biomass of Nostoc linckia as adsorbent of crystal violet dye: Optimization based on statistical model
Mona, S., Kaushik, A., & Kaushik, C. P. (2011) · International Biodeterioration & Biodegradation · doi:10.1016/j.ibiod.2011.02.002 · Cited by 67 · see citing works
High-level production of bioactive human beta-defensin-4 in Escherichia coli by soluble fusion expression
Xu, Z., Zhong, Z., Huang, L., Li, P., Wang, F., & Cen, P. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-005-0287-0 · Cited by 67 · see citing works
A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins
Fatima, K., Naqvi, F., & Younas, H. (2021) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-021-00970-5 · Cited by 66 · see citing works
High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli
Nozach, H., Fruchart‐Gaillard, C., Fenaille, F., Beau, F., Ramos, O. H. P., Douzi, B., Saez, N. J., Moutiez, M., Servent, D., Gondry, M., et al. (2013) · Microbial Cell Factories · doi:10.1186/1475-2859-12-37 · Cited by 65 · see citing works
Transgenic cowpeas (Vigna unguiculata L. Walp) expressing Bacillus thuringiensis Vip3Ba protein are protected against the Maruca pod borer (Maruca vitrata)
Bett, B., Gollasch, S., Moore, A., James, W., Armstrong, J., Walsh, T., Harding, R. M., & Higgins, T. J. V. (2017) · Plant Cell Tissue and Organ Culture (PCTOC) · doi:10.1007/s11240-017-1287-3 · Cited by 64 · see citing works
Extracellular expression and biochemical characterization of α-cyclodextrin glycosyltransferase from Paenibacillus macerans
Li, Z., Li, B., Gu, Z., Du, G., Wu, J., & Chen, J. (2010) · Carbohydrate Research · doi:10.1016/j.carres.2010.02.002 · Cited by 64 · see citing works
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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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