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Isolation of recombinant proteins from culture broth by co-precipitation with an amino acid carrier to form stable dry powders

Moore, Barry and Deere, Joseph and Edrada-Ebel, RuAngelie and Ingram, Andrew and van der Walle, Christopher F (2010) Isolation of recombinant proteins from culture broth by co-precipitation with an amino acid carrier to form stable dry powders. Biotechnology and Bioengineering, 106 (5). pp. 764-773.

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Abstract

Protein-coated microcrystals can be generated by co-precipitation of protein and a water-soluble crystalline carrier by addition to excess water miscible organic solvent. We have investigated this novel process for its utility in the concentration and partial purification of a recombinant protein exported into the culture broth during expression by Pichia pastoris. Co-precipitation with a L-glutamine carrier selectively isolated the protein content of the culture broth, with a minimal number of steps, and simultaneously removed contaminants including a novel yeast metabolite. This pigment co-elutes during aqueous chromatography but its elucidation as a benzoylated glycosamine suggested a simple route of removal by partition during the co-precipitation process. Scale-up of the process was readily achieved through in-line mixing and subsequent reconstitution of the dried protein-coated microcrystals yielded natively folded, bioactive protein. Additional washing of the crystals with saturated L-glutamine facilitated further purification of the recombinant protein immobilized on the L-glutamine carrier. Thus, we present a novel method for the harvesting of recombinant protein from culture broth as a dry powder, which may be of general applicability to bioprocessing.