Related Experiment Video
Updated: Apr 16, 2026

Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Quo vadis? The challenges of recombinant protein folding and secretion in Pichia pastoris
Verena Puxbaum1, Diethard Mattanovich, Brigitte Gasser
1Austrian Centre of Industrial Biotechnology, Muthgasse 11, 1190, Vienna, Austria.
Abstract:
The development of Pichia pastoris as a production platform for recombinant proteins has been a remarkable success story over the last three decades. Stable cheap production processes and the good protein secretion abilities were pacemakers of this development. However, limitations of protein folding, glycosylation or secretion have been identified quite early on. With the availability of genome sequences and the development of systems biology characterization in the last 5 years, remarkable success in strain improvement was achieved. Here, we focus on recent developments of characterization and improvement of P. pastoris production strains regarding protein folding, intracellular trafficking, glycosylation and proteolytic degradation.
More Related Videos
Related Concept Videos
Production of Pharmaceuticals
Upstream Processing
Molecular Chaperones and Protein Folding
The...
Bacterial Protein Maturation
Protein Folding Quality Check in the RER
Protein Folding

