Acting on Folding Effectors to Improve Recombinant Protein Yields and Functional Quality

  • Ario de Marco
Part of the Methods in Molecular Biology book series (MIMB, volume 1586)


Molecular and chemical chaperones/foldases can strongly contribute to improve the amounts and the structural quality of recombinant proteins. Several methodologies have been proposed to optimize their beneficial effects. This chapter presents a condensed summary of the biotechnological opportunities offered by this approach followed by a protocol describing the method we use for expressing disulfide bond-dependent recombinant antibodies in the cytoplasm of bacteria engineered to overexpress sulfhydryl oxidase and DsbC isomerase. The system is based on the possibility to trigger the foldase expression independently and before the induction of the target protein. As a consequence, the recombinant antibody synthesis starts only after enough foldases have accumulated to promote correct folding of the antibody.

Key words

Molecular chaperones Disulfide isomerases Sulfhydryl oxidase Osmolytes Protein soluble aggregates Protein quality assessment Secretion efficiency 


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Copyright information

© Springer Science+Business Media LLC 2017

Authors and Affiliations

  1. 1.Department of Biomedical Sciences and EngineeringUniversity of Nova GoricaVipavaSlovenia

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