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Methods Mol Biol. 2019;1923:343-350. doi: 10.1007/978-1-4939-9024-5_17.

Purification of Recombinant Glycoproteins from Pichia pastoris Culture Supernatants.

Author information

1
Institute of Chemical, Environmental and Bioscience Engineering, Research Division Biochemical Engineering, Vienna University of Technology (TU Wien), Vienna, Austria.
2
Institute of Chemical, Environmental and Bioscience Engineering, Research Division Biochemical Engineering, Vienna University of Technology (TU Wien), Vienna, Austria. oliver.spadiut@tuwien.ac.at.

Abstract

Pichia pastoris is a common host organism for the production of recombinant proteins. While unglycosylated recombinant proteins derived from this yeast can be purified efficiently by only a few conventional chromatography steps, the purification of glycosylated recombinant proteins is a very challenging process due to the intrinsic feature of the yeast of hypermannosylation. The resulting vast glycosylation pattern on the recombinant target protein masks its physicochemical properties hampering a conventional downstream process. Here, we describe a fast and efficient two-step chromatography strategy, where both steps are operated in flow-through mode, to purify recombinant glycoproteins from P. pastoris culture supernatants.

KEYWORDS:

Downstream process; Flow-through chromatography; Glycosylation; Pichia pastoris; Recombinant protein production

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