Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli.

ABSTRACT: Disulfide bonds occurred in majority of secreted protein. Formation of correct disulfide bonds are must for achieving native conformation, solubility and activity. Production of recombinant proteins containing disulfide bond for therapeutic, diagnostic and various other purposes is a challenging task of research. Production of such proteins in the reducing cytosolic compartment of E. coli usually ends up in inclusion bodies formation. Refolding of inclusion bodies can be difficult, time and labor consuming and uneconomical. Translocation of these proteins into the oxidative periplasmic compartment provides correct environment to undergo proper disulfide bonds formation and thus achieving native conformation. However, not all proteins can be efficiently translocated to the periplasm with th

SUBMITTER: Malik A 

PROVIDER: S-EPMC4742420 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature