Glycosylation of <i>Pichia pastoris</i> ‐derived proteins

Abstract

The Pichia pastoris system for expression of heterologous recombinant proteins is being used increasingly because of the large yields of properly folded proteins that result and the ease of scaling preparations into large-biomass fermentors. Another advantage of this system centres on the type of glycosylation that results, generally yielding protein-bound oligosaccharides that are of much shorter chain length than found in Saccharomyces cerevisiae. This review is a summary of the current state of knowledge of glycosylation of proteins in this methylotrophic yeast.