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.
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