Recombinant protein expression optimization in Escherichia coli: A review

DOI: 10.18805/ijar.B-3808    | Article Id: B-3808 | Page : 653-660
Citation :- Recombinant protein expression optimization in Escherichia coli: A review.Indian Journal Of Animal Research.2020.(54):653-660
N. Hemamalini, S. Ezhilmathi and A. Angela Mercy
Address : Department of Aquaculture, Dr. M.G.R Fisheries College and Research Institute, Thalainayeru, Nagapattinam-611 001, Tamil Nadu, India.
Submitted Date : 21-02-2019
Accepted Date : 10-04-2019


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.


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


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