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Production of a recombinant peroxidase in different glyco-engineered Pichia pastoris strains: a morphological and physiological comparison.

Microb. Cell Fact.. 2018;

PekarskyAlexander，VeiterLukas，RajamanickamVignesh，HerwigChristoph，Grünwald-GruberClemens，AltmannFriedrich，SpadiutOl

Products/Services Used	Details	Operation
Codon Optimization	For this study, a HRP C1A gene, codon-optimized for P. pastoris, was ordered from GenScript (Nanjing, China) and cloned into a pPICZαC vector, providing a Zeocin™ (Zeo) resistance gene as well as an α-prepro mating signal sequence from Saccharomyces cerevisiae for product secretion, using standard methods. Correct integration was verified by sequencing.	Get A Quote

摘要

The methylotrophic yeast Pichia pastoris is a common host for the production of recombinant proteins. However， hypermannosylation hinders the use of recombinant proteins from yeast in most biopharmaceutical applications. Glyco-engineered yeast strains produce more homogeneously glycosylated proteins， but can be physiologically impaired and show tendencies for cellular agglomeration， hence are hard to cultivate. Further， comprehensive data regarding growth， physiology and recombinant protein production in the controlled environment of a bioreactor are scarce.