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

IF 1.4 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS

Protein expression and purification Pub Date : 2024-03-12 DOI:10.1016/j.pep.2024.106463

İbrahim İncir , Özlem Kaplan

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引用次数: 0

Abstract

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.

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作为多功能细胞工厂的大肠杆菌：重组蛋白质生产的进步与挑战。

大肠杆菌在重组蛋白质生产中发挥着重要作用。随着 DNA 重组技术的发现以及随后在大肠杆菌中生产出首个重组胰岛素，大肠杆菌的重要性也随之增加。大肠杆菌是生产重组蛋白质的一种广泛使用且具有成本效益的宿主。值得注意的是，相当一部分已获批准的治疗用蛋白质也是在这种生物体内生产的。尽管有这些优点，但它也有一些缺点，如毒性和缺乏真核翻译后修饰，这可能导致产生折叠错误、不溶解或功能障碍的蛋白质。本研究的重点是大肠杆菌重组蛋白生产中改善表达和溶解性的挑战和工程方法。在此背景下，讨论了解决策略，如菌株和载体的选择、密码子的使用、mRNA 的稳定性、表达条件、转位到大肠杆菌的外质区和添加融合标签。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Protein expression and purification 生物-生化研究方法

CiteScore

3.70

自引率

6.20%

发文量

120

审稿时长

32 days

期刊介绍： Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.