Characterization of Escherichia coli as a Recombinant Protein Expression Host and its Optimization

Authors

  • Kang Yu
  • Congjing Cao
  • Luwen Huang
  • Enxu Wang

DOI:

https://doi.org/10.54097/qsa77p06

Keywords:

Escherichia Coli; Recombinant Protein; Expression Host; Optimization Strategy.

Abstract

Engineered Escherichia coli serves as an efficient platform for the production of a diverse array of recombinant proteins, thereby addressing the pharmaceutical industry's demand for high-quality biological agents. Nevertheless, challenges related to protein folding and the complexities involved in product purification must be acknowledged. This review delineates the advantages and disadvantages of utilizing E. coli as an expression host and further investigates various strategies aimed at optimizing and enhancing the E. coli expression system to elevate the yield, purity, and biological activity of recombinant proteins, ultimately supporting advancements in biopharmaceuticals and other relevant fields.

Downloads

Download data is not yet available.

References

[1] Hayat SMG, Farahani N, Golichenari B, Sahebkar A. Recombinant Protein Expression in Escherichia coli (E. coli): What We Need to Know. Curr Pharm Des. 2018;24(6):718-725.

[2] Ahmad I, Nawaz N, Darwesh NM, Ur Rahman S, Mustafa MZ, Khan SB, Patching SG. Overcoming challenges for amplified expression of recombinant proteins using Escherichia coli. Protein Expr Purif. 2018 Apr; 144:12-18.

[3] Gopal GJ, Kumar A. Strategies for the production of recombinant protein in Escherichia coli. Protein J. 2013 Aug; 32 (6): 419-425.

[4] Saroha P, Patil RS, Rathore AS. Recent advancements in soluble expression of recombinant antibody fragments in microbial host systems. Prep Biochem Biotechnol. 2024 Aug 28:1-10.

[5] Rosano GL, Ceccarelli EA. Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol. 2014 Apr 17; 5:172.

[6] Zhang ZX, Nong FT, Wang YZ, Yan CX, Gu Y, Song P, Sun XM. Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity. Microb Cell Fact. 2022 Sep 15;21(1):191.

[7] Huang CJ, Lin H, Yang X. Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements. J Ind Microbiol Biotechnol. 2012 Mar;39 (3): 383-399.

[8] Gupta V, Sengupta M, Prakash J, Tripathy BC. Production of Recombinant Pharmaceutical Proteins. Basic and Applied Aspects of Biotechnology. 2016 Oct 23:77–101.

[9] Rosano GL, Morales ES, Ceccarelli EA. New tools for recombinant protein production in Escherichia coli: A 5-year update. Protein Sci. 2019 Aug;28(8):1412-1422.

[10] İncir İ, Kaplan Ö. Escherichia coli as a versatile cell factory: Advances and challenges in recombinant protein production. Protein Expr Purif. 2024 Jul; 219:106463.

[11] Singh A, Upadhyay V, Upadhyay AK, Singh SM, Panda AK. Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process. Microb Cell Fact. 2015 Mar 25; 14:41.

[12] Baneyx F. Recombinant protein expression in Escherichia coli. Curr Opin Biotechnol. 1999 Oct;10(5):411-421.

[13] Georgiou G, Valax P. Expression of correctly folded proteins in Escherichia coli. Curr Opin Biotechnol. 1996 Apr;7(2):190-197.

[14] Falak S, Sajed M, Rashid N. Strategies to enhance soluble production of heterologous proteins in Escherichia coli. Biologia (2022) 77:893–905.

[15] Schramm FD, Schroeder K, Jonas K. Protein aggregation in bacteria. FEMS Microbiol Rev. 2020 Jan 1;44(1):54-72.

[16] de Marco A, Vigh L, Diamant S, Goloubinoff P. Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones. Cell Stress Chaperones. 2005 Winter;10 (4): 329-339.

[17] Maldonado LM, Hernández VE, Rivero EM, Barba de la Rosa AP, Flores JL, Acevedo LG, De León Rodríguez A. Optimization of culture conditions for a synthetic gene expression in Escherichia coli using response surface methodology: the case of human interferon beta. Biomol Eng. 2007 Jun;24(2):217-222.

[18] Valente CA, Prazeres DM, Cabral JM, Monteiro GA. Translational features of human alpha 2b interferon production in Escherichia coli. Appl Environ Microbiol. 2004 Aug;70 (8): 5033-5036.

[19] Kaur J, Kumar A, Kaur J. Strategies for optimization of heterologous protein expression in E. coli: Roadblocks and reinforcements. Int J Biol Macromol. 2018 Jan; 106:803-822.

[20] Ge J, Wang X, Bai Y, Wang Y, Wang Y, Tu T, Qin X, Su X, Luo H, Yao B, Huang H, Zhang J. Engineering Escherichia coli for efficient assembly of heme proteins. Microb Cell Fact. 2023 Mar 28;22(1):59.

[21] Mühlmann M, Forsten E, Noack S, Büchs J. Optimizing recombinant protein expression via automated induction profiling in microtiter plates at different temperatures. Microb Cell Fact. 2017 Nov 28;16(1):220.

[22] Rigi G, Rostami A, Ghomi H, Ahmadian G, Mirbagheri VS, Jeiranikhameneh M, Vahed M, Rahimi S. Optimization of expression, purification and secretion of functional recombinant human growth hormone in Escherichia coli using modified staphylococcal protein a signal peptide. BMC Biotechnol. 2021 Aug 16;21(1):51.

[23] Vincentelli R, Romier C. Expression in Escherichia coli: becoming faster and more complex. Curr Opin Struct Biol. 2013 Jun;23(3):326-334.

[24] Bahreini E, Aghaiypour K, Abbasalipourkabir R, Goodarzi MT, Saidijam M, Safavieh SS. An optimized protocol for overproduction of recombinant protein expression in Escherichia coli. Prep Biochem Biotechnol. 2014;44(5):510-528.

[25] Zhou Y, Lu Z, Wang X, Selvaraj JN, Zhang G. Genetic engineering modification and fermentation optimization for extracellular production of recombinant proteins using Escherichia coli. Appl Microbiol Biotechnol. 2018 Feb;102(4): 1545-1556.

Downloads

Published

14-09-2024

Issue

Section

Articles

How to Cite

Yu, K., Cao, C., Huang, L., & Wang, E. (2024). Characterization of Escherichia coli as a Recombinant Protein Expression Host and its Optimization. Academic Journal of Science and Technology, 12(2), 223-225. https://doi.org/10.54097/qsa77p06