Indian Journal of Animal Research

SCOPUSWeb of Science
  • Year: 2020
  • Volume: 54
  • Issue: 6

Recombinant protein expression optimization in Escherichia coli: A review

  • Author:
  • N. Hemamalini, S. Ezhilmathi1,, A. Angela Mercy2
  • Total Page Count: 8
  • Page Number: 653 to 660

1Department of Aquaculture, Dr. M.G.R Fisheries College and Research Institute, Ponneri-601 204, Tamil Nadu, India

2Department of Fisheries Biotechnology, Institute of Fisheries Post Graduate Studies, Chennai-603 103, Tamil Nadu, India

*Corresponding Author: S. Ezhilmathi, Department of Aquaculture, Dr. M.G.R. Fisheries College and Research Institute, Ponneri-601 204, Tamil Nadu, India, Email: s.ezhilmathi.mfsc@gmail.com

Online published on 20 July, 2020.

Abstract

Escherichia coli is the most extensively used organism in recombinant protein production. It has several advantages including a very short life cycle, ease of genetic manipulation and the well-known cell biology etc. which makes E. coli as the perfect host for recombinant protein expression. Despite many advantages, E. coli also have few disadvantages such as coupled transcription and translation and lack of eukaryotic post-translational modifications. These challenges can be overcome by adopting several strategies such as, using different E. coli expression vectors, changing the gene sequence without altering the functional domain, modified E. coli strain usage, changing the culture parameters and co-expression with a molecular chaperone. In this review, we present the level of strategies used to enhance the recombinant protein expression and its stability in E. coli.

Keywords

E. coli, Fusion tags, Heterologous protein, Promoter, Recombinant protein expression