Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 99, Issue 7, Pages 2925-2938Publisher
SPRINGER
DOI: 10.1007/s00253-015-6470-z
Keywords
Yeast; Pichia pastoris; Recombinant protein; Folding; Secretion; Glycosylation
Categories
Funding
- Austrian Science Fund (FWF)
- Austrian Research Promotion Agency
- Federal Ministry of Science, Research and Economy (BMWFW)
- Federal Ministry of Traffic, Innovation and Technology (bmvit)
- Styrian Business Promotion Agency SFG
- Standortagentur Tirol
- ZIT-Technology Agency of the City of Vienna through the COMET-Funding Program
- Polymun Scientific GmbH
- Biomin Research Center
- Boehringer-Ingelheim RCV
- Lonza AG
- Biocrates Life Sciences AG
- VTU Technology GmbH
- Sandoz GmbH
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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.
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