Protein disaggregation and refolding using high hydrostatic pressure

Production of recombinant proteins often leads to aggregate formation. These aggregates may make it impossible to solubilize the protein for downstream applications such as assay development or structural studies by X‐ray crystallography or nuclear magnetic resonance spectroscopy. High hydrostatic pressure technology has been developed which offers significant advantages over traditional methods of protein disaggregation and refolding. Pressure induced disruption of protein aggregates and subsequent refolding can take place at high concentrations in a single process step, without the need for high concentrations of chaotropic agents. Copyright © 2007 Society of Chemical Industry