Quo vadis? The challenges of recombinant protein folding and secretion in Pichia pastoris

被引：0
|
作者：
Verena Puxbaum
Diethard Mattanovich
Brigitte Gasser
机构：
[1] Austrian Centre of Industrial Biotechnology,Department of Biotechnology
[2] University of Natural Resources and Life Sciences,undefined
[3] Vienna,undefined
来源：
Applied Microbiology and Biotechnology | 2015年 / 99卷
关键词：
Yeast; Recombinant protein; Folding; Secretion; Glycosylation;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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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页码：2925 / 2938
页数：13
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