Among bacterial expression systems, Escherichia coli was the popular and widely used expression host due to its high-rate expression trait. However, overexpression of recombinant protein in E. coli is often found as inclusion bodies. While the formation of inclusion bodies is beneficial in protein isolation from other cellular components, most of the recombinant proteins from inclusion bodies are misfolded and have lost their biological activity. Protein refolding allows the misfolded protein to rearrange into its native conformation which exhibits its biological activity, thus protein refolding become a pivotal step in recovering the active protein. However, protein refolding was affected by various factors; hence, screening of refolding conditions was required to meet the optimal result. As a consequence, a rapid and efficient characterization method is required to monitor the refolding performance. In this review, we will briefly give an overview of the protein refolding method, and chemical additives in protein refolding, and also provide insight into structural characterization to evaluate refolding performance.
Key words: Protein refolding, Recombinant proteins, Chemical additives, Inclusion body
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