PMID:10933845

Citation	Kohler, RJ, Preuss, M and Miller, AD Design of a molecular chaperone-assisted protein folding bioreactor. Biotechnol. Prog. 16:671-5
Abstract	Escherichia coli molecular chaperone GroEL and co-chaperone GroES are well known to assist the folding/refolding of a diverse range of substrate proteins. Despite this, there have been relatively few reports of the GroEL/GroES molecular chaperone system being used as a biotechnology tool for protein folding/refolding. In this paper, a solution-phase protein folding bioreactor is described that involves the complete GroEL/GroES system. The main features of this bioreactor are the use of a stirred-cell concentrator fitted with a 100 kDa molecular weight cutoff membrane and an attached buffer reservoir. This bioreactor system was used successfully for assisted-batch refolding of guanidinium chloride (Gu-HCl) unfolded mitochondrial malate dehydrogenase (mMDH). We believe that protein folding bioreactor systems of this type could have wide potential utility for the folding/refolding of unfolded protein substrates.
Links	PubMed Online version:10.1021/bp0000609
Keywords	Animals; Bioreactors; Chaperonin 10/metabolism; Chaperonin 60/metabolism; Malate Dehydrogenase/metabolism; Mitochondria, Heart/enzymology; Molecular Chaperones/metabolism; Protein Folding; Swine
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