Strategies to enhance soluble production of heterologous proteins in Escherichia coli

被引：19
|
作者：
Falak, Samia [1 ]
Sajed, Muhammad [1 ]
Rashid, Naeem [1 ]
机构：
[1] Univ Punjab, Sch Biol Sci, Quaid E Azam Campus, Lahore 54590, Pakistan
来源：
BIOLOGIA | 2022年 / 77卷 / 03期
关键词：
Escherichia coli; Heterologous expression; Soluble production; Fusion tags; Chaperones; DISULFIDE BOND FORMATION; HIGH-LEVEL EXPRESSION; RECOMBINANT PROTEINS; MOLECULAR CHAPERONES; LOW-TEMPERATURE; MESSENGER-RNA; IN-VITRO; CHEMICAL CHAPERONES; HEAT-SHOCK; LIPASE-B;
D O I：
10.1007/s11756-021-00994-5
中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Escherichia coli is the first choice host for heterologous production of recombinant proteins with high yield due to its robust and economical growth. However, occasionally recombinant proteins are either not produced or produced in misfolded, insoluble and inactive form. In this review we focus on various strategies to enhance the soluble yield of active recombinant proteins by exploring the choice of vector, host strain, culturing conditions, use of various fusion tags and chemical or biological chaperones for soluble production of heterologous proteins.
引用
收藏
页码：893 / 905
页数：13
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