提高大肠杆菌可溶性重组蛋白表达产率的研究进展

Advances in Promoting Soluble Expression of Recombinant Protein in Escherichia coli

大肠杆菌表达重组蛋白相比真核细胞具有成本低廉、大规模发酵容易、条件易于自动化控制等优点,通过大肠杆菌表达重组蛋白是一种高效、经济的途径,重组蛋白表达量可达到大肠杆菌总蛋白质量的50%。具有正常生化活性的重组蛋白通常为可溶性形式,因而对于以得到活性产物(如抗体、酶等)为目的的研究,通常采用可溶性表达途径。目前已有多种以可溶性重组蛋白为活性物质的治疗性药物经批准上市,但并非所有外源基因均能实现可溶性高表达,因此重组蛋白的可溶性高表达具有重要研究价值。在总结近年提高经大肠杆菌可溶性表达重组蛋白产率研究的基础上,从启动子的选择、SD序列的引入、信号肽的优化、宿主细胞的选择、共表达其他蛋白质,高密度发酵等方面阐释在大肠杆菌中提高可溶性重组蛋白表达产率的方法。

Recombinant protein expression in Escherichia coli（ E. coli） is sound and effective with the protein expression taking up to 50 percent of the total protein. The soluble recombinant proteins usually have biochemical activities,these proteins include antibodies and enzymes. Here are many soluble recombinant proteins have been approved as drugs, so it is crucial to research how to promote soluble expression of recombinant proteins in E. coli. Here the researches about improving yield of soluble expression of recombinant protein by E. coli have been summarized thoroughly. Variables at stages of a protein expression such as promoter system, SD sequence, signal peptide, host strains, co-expression of other proteins and high cell density cultivation to optimize soluble expression in E. coli are discussed.