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

Kang Yu; Congjing Cao; Luwen Huang; Enxu Wang

doi:10.54097/qsa77p06

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.

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