摘要
以大肠杆菌为代表的原核表达蛋白系统具有操作简单、周期短、成本低、表达量高等优点而成为获得外源表达蛋白的首选方案。但外源蛋白在原核宿主中往往以无生物活性的包涵体形式存在,这限制了原核表达系统的广泛应用。随着对蛋白折叠动力学、参与蛋白折叠的酶和分子伴侣等认识的不断深入,科学家们通过诱导条件优化、宿主细胞改造以及使用融合标签等手段,在促进原核表达蛋白可溶性方面取得了较大的进展。就这些研究进展进行综述,旨在为设计和获得原核可溶表达蛋白的实验方案提供参考。
The prokaryotic expression protein system,especially Escherichia coli expression system,is a preferred method for obtaining exogenous proteins because of its advantages of simple operation,short cycle,high expression level and relatively low cost.However,one of the major factors to limit the extensive application of E.coli expression protein system is that the exogenous proteins,when expressed in a high amount,are often present in an insoluble form.With the understanding of protein folding dynamics,enzymes and molecular chaperones involved in protein folding,scientists have made great progress in promoting solubility of heterologous proteins by changing expression conditions,modifying host cells or using fusion tags.Here,we review the related progress in order to provide reference for related research.
作者
张磊
唐永凯
李红霞
李建林
徐逾鑫
李迎宾
俞菊华
ZHANG Lei;TANG Yong-kai;LI Hong-xia;LI Jian-lin;XU Yu-xin;LI Ying-bin;YU Ju-hua(Wuxi Fisheries College,Nanjing Agricultural University,Wuxi,Jiangsu 214128,China;Freshwater Fisheries Research Center,Chinese Academy of Fishery Sciences,Wuxi,Jiangsu 214128,China)
出处
《中国生物工程杂志》
CAS
CSCD
北大核心
2021年第2期138-149,共12页
China Biotechnology
基金
中国水产科学研究院基本科研业务费(2020TD37)资助项目。
关键词
原核表达
可溶性
蛋白折叠酶
分子伴侣
融合标签
Prokaryotic expression
Solubility
Folding enzyme
Molecular chaperone
Fusion tags
