Escherichia coli as a versatile cell factory: Advances and challenges in recombinant protein production

被引:12
|
作者
Incir, Ibrahim [1 ]
Kaplan, Ozlem [2 ]
机构
[1] Karamanoglu Mehmetbey Univ, Kazim Karabekir Vocat Sch, Dept Med Serv & Tech, Environm Hlth Program, Karaman, Turkiye
[2] Alanya Alaaddin Keykubat Univ, Rafet Kayis Fac Engn, Dept Genet & Bioengn, Antalya, Turkiye
关键词
E; coli; Recombinant protein; Optimized protein production; Solubility of protein; RNA SECONDARY-STRUCTURE; MOLECULAR CHAPERONES; FUNCTIONAL EXPRESSION; CODON USAGE; GENES; OPTIMIZATION; TRANSLATION; AGGREGATION; STRATEGIES; OVEREXPRESSION;
D O I
10.1016/j.pep.2024.106463
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
E. coli plays a substantial role in recombinant protein production. Its importance increased with the discovery of recombinant DNA technology and the subsequent production of the first recombinant insulin in E. coli. E. coli is a widely used and cost-effective host to produce recombinant proteins. It is also noteworthy that a significant portion of the approved therapeutic proteins have been produced in this organism. Despite these advantages, it has some disadvantages, such as toxicity and lack of eukaryotic post-translational modifications that can lead to the production of misfolded, insoluble, or dysfunctional proteins. This study focused on the challenges and engineering approaches for improved expression and solubility in recombinant protein production in E. coli. In this context, solution strategies such as strain and vector selection, codon usage, mRNA stability, expression conditions, translocation to the periplasmic region and addition of fusion tags in E. coli were discussed.
引用
收藏
页数:8
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