Overview of refolding methods on misfolded recombinant proteins from Escherichia coli inclusion bodies
Ahmad Nabiel, Yosua Yosua, Sriwidodo Sriwidodo, Iman Permana Maksum
Abstract
Among bacterial expression system, 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 often found as inclusion bodies. While formation of inclusion bodies is beneficial in protein isolation from other cellular components, most of recombinant proteins from inclusion bodies are misfolded which have lost their biological activity. Protein refolding allows misfolded protein to rearrange into their native conformation which exhibit its biological activity, thus protein refolding become a pivotal step to recover active protein. However, protein refolding was affected by various factors; hence, screening of refolding condition was required to meet the optimal result. As a consequence, rapid and efficient characterization method is required to monitor the refolding performance. In this review, we will briefly give an overview about protein refolding method, chemical additives in protein refolding, and also provide insight in structural characterization to evaluate refolding performance.