The Study of Different Signal Peptides in Improvement of Recombinant Proteins Solubility in E. coli: A Mini-Review Article

被引:0
作者
Rahmatabadi, Seyyed Soheil [1 ,2 ]
Askari, Soudabeh [3 ]
Khademi, Fatemeh [2 ]
Soleymani, Bijan [2 ]
机构
[1] Kermanshah Univ Med Sci, Hlth Technol Inst, Nano Drug Delivery Res Ctr, Kermanshah, Iran
[2] Kermanshah Univ Med Sci, Hlth Technol Inst, Med Biol Res Ctr, Kermanshah, Iran
[3] Appl Razi Biotechnol, Kermanshah, Iran
关键词
Inclusion bodies; solubility; signal peptide; recombinant protein; expression; E; coli; ESCHERICHIA-COLI; BACILLUS-SUBTILIS; EXTRACELLULAR PRODUCTION; HETEROLOGOUS PROTEINS; SECRETORY EXPRESSION; POSITIVE CHARGE; DISULFIDE BONDS; TAC PROMOTER; MEMBRANE; OPTIMIZATION;
D O I
10.2174/0115701646305738240730113619
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
In E. coli, the production of proteins as inclusion bodies (IBs) caused a decrease in the solubility and activity of these products. Diverse approaches and methods have been used by investigators to overcome this problem. The secretion of recombinant proteins into the periplasmic space by means of suitable signal peptides is a way to resolve these limitations for the production of recombinant proteins in a native form. Secretory production of recombinant proteins in bacterial hosts has many advantages and thus, it is a topic of interest. However, it is hard to achieve due to the difficulty of the process and the need for the choice of appropriate signal peptide for each host and protein. Based on the literature, different signal peptides have experimentally been applied to enhance the solubility of various recombinant proteins. It has been shown that the secretion efficiency of a given protein differs dramatically based on the type of the signal peptide that is attached to the protein. Therefore, the choice and alteration of signal peptides are the two crucial approaches for the improvement of a recombinant protein secretion that have been discussed in this review. Also, different factors affecting the expression and solubility of recombinant proteins have been discussed.
引用
收藏
页码:129 / 139
页数:11
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