Strategies to improve the folding and modification of recombinant proteins: a review.

Author: Jiadong LI ¹ ; Hong WANG ¹
Author Information

1. National-Local Joint Engineering Research Center for Processing and Safety Control of Livestock and Poultry Products (Guangdong), Guangdong Provincial Key Laboratory of Food Quality and Safety, College of Food Science, South China Agricultural University, Guangzhou 510642, Guangdong, China.
Publication Type:Journal Article
Keywords: expression systems; folding; posttranslational modification; recombinant proteins
From: Chinese Journal of Biotechnology 2017;33(4):591-600
CountryChina
Language:Chinese
Abstract: Gene expression technology has made great progress with the continuous developments and researches of molecular biology. Though many systems to produce recombinant proteins have been studied, none of them is available so far to satisfy the needs completely. With the increasing demands of bioactive peptides and protein drugs, expression quantity and correct posttranslational folding and modifications are also needed under the circumstance which can make proteins more close to native conformation and higher activity and stability. Based on our previous work, we summarized the factors affecting the folding and modifications of recombinant proteins correctly from five aspects, including expression system and hosts, secretory expression, coexpression, fusion expression, and the culture conditions, as well as improvement strategies.