Immobilized chaperones: A productive alternative to refolding of bacterial inclusion body proteins

Advances have been made in the industrial production of recombinant proteins/biomolecules by utilizing the cellular machinery of Escherichia coli. However, the potential of this organism gets limited by the fact that proteins requiring complex post-translational modifications or disulfide bond formation aggregate in the form of inclusion bodies inside the cells. The way out is to solubilize them and then refold the protein, a major challenge that leads to greatly reduced protein yields. Molecular chaperones and other folding catalysts have long been known to aid the protein-folding pathway. One popular approach explored extensively is the co-expression of the chaperones along with the protein of interest. Although positive results have been found, but the efficacies of these systems depend largely on the type of protein expressed. Manipulating these folding modulators to increase the refolding efficiencies in vitro have lately been explored and is the subject of this review. The technique of immobilization combined with the knowledge of refolding would pave the way to an optimized high-throughput refolding technology, with the advantages of reusability, easy separation from the desired protein and good protein folding yields.