scholarly journals Process Technology for Production and Recovery of Heterologous Proteins with Pichia Pastoris

2007 ◽  
Vol 23 (2) ◽  
pp. 516-516
Author(s):  
M. Jahic ◽  
A. Veide ◽  
T. Charoenrat ◽  
T. Teeri ◽  
S.-O. Enfors
Keyword(s):  
Pichia Pastoris ◽  
Heterologous Proteins ◽  
Process Technology

Process Technology for Production and Recovery of Heterologous Proteins with Pichia pastoris

2006 ◽  
Vol 22 (6) ◽  
pp. 1465-1473 ◽  
Author(s):  
M. Jahic ◽  
A. Veide ◽  
T. Charoenrat ◽  
T. Teeri ◽  
S.-O. Enfors
Keyword(s):  
Pichia Pastoris ◽  
Heterologous Proteins ◽  
Process Technology

Production of foreign proteins in the yeast Pichia pastoris

1995 ◽  
Vol 73 (S1) ◽  
pp. 891-897 ◽  
Author(s):  
James M. Cregg ◽  
David R. Higgins
Keyword(s):  
Gene Expression ◽  
Pichia Pastoris ◽  
Heterologous Gene Expression ◽  
Expression System ◽  
Methylotrophic Yeast ◽  
Culture Broth ◽  
Heterologous Gene ◽  
Foreign Gene ◽  
Heterologous Proteins ◽  
Yeast Pichia Pastoris

The methanol-utilizing yeast Pichia pastoris has been developed as a host system for the production of heterologous proteins of commercial interest. An industrial yeast selected for efficient growth on methanol for biomass generation, P. pastoris is readily grown on defined medium in continuous culture at high volume and density. A unique feature of the expression system is the promoter employed to drive heterologous gene expression, which is derived from the methanol-regulated alcohol oxidase I gene (AOX1) of P. pastoris, one of the most efficient and tightly regulated promoters known. The strength of the AOX1 promoter results in high expression levels in strains harboring only a single integrated copy of a foreign-gene expression cassette. Levels may often be further enhanced through the integration of multiple cassette copies into the P. pastoris genome and strategies to construct and select multicopy cassette strains have been devised. The system is particularly attractive for the secretion of foreign-gene products. Because P. pastoris endogenous protein secretion levels are low, foreign secreted proteins often appear to be virtually the only proteins in the culture broth, a major advantage in processing and purification. Key words: heterologous gene expression, methylotrophic yeast, Pichia pastoris, secretion, glycosylation.

Process Technology for Production and Recovery of Heterologous Proteins withPichia pastoris

2006 ◽  
Vol 22 (6) ◽  
pp. 1465-1473 ◽  
Author(s):  
Mehmedalija Jahic ◽  
Andres Veide ◽  
Theppanya Charoenrat ◽  
Tuula Teeri ◽  
Sven-Olof Enfors
Keyword(s):  
Heterologous Proteins ◽  
Process Technology

Construction of a novel system for cell surface display of heterologous proteins on Pichia pastoris

2007 ◽  
Vol 29 (10) ◽  
pp. 1561-1566 ◽  
Author(s):  
Qingjie Wang ◽  
Lei Li ◽  
Min Chen ◽  
Qingsheng Qi ◽  
Peng George Wang
Keyword(s):  
Pichia Pastoris ◽  
Cell Surface ◽  
Surface Display ◽  
Cell Surface Display ◽  
Heterologous Proteins

scholarly journals Reduced Proteolysis of Secreted Gelatin and Yps1-Mediated α-Factor Leader Processing in a Pichia pastoris kex2 Disruptant

2005 ◽  
Vol 71 (5) ◽  
pp. 2310-2317 ◽  
Author(s):  
Marc W. T. Werten ◽  
Frits A. de Wolf
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Pichia Pastoris ◽  
Single Gene ◽  
Foreign Protein ◽  
Heterologous Proteins ◽  
Basic Residue ◽  
Substrate Specificities ◽  
Basic Amino Acids ◽  
High Level

ABSTRACT Heterologous proteins secreted by yeast and fungal expression hosts are occasionally degraded at basic amino acids. We cloned Pichia pastoris homologs of the Saccharomyces cerevisiae basic residue-specific endoproteases Kex2 and Yps1 to evaluate their involvement in the degradation of a secreted mammalian gelatin. Disruption of the P. pastoris KEX2 gene prevented proteolysis of the foreign protein at specific monoarginylic sites. The S. cerevisiae α-factor preproleader used to direct high-level gelatin secretion was correctly processed at its dibasic site in the absence of the prototypical proprotein convertase Kex2. Disruption of the YPS1 gene had no effect on gelatin degradation or processing of the α-factor propeptide. When both the KEX2 and YPS1 genes were disrupted, correct precursor maturation no longer occurred. The different substrate specificities of both proteases and their mutual redundancy for propeptide processing indicate that P. pastoris kex2 and yps1 single-gene disruptants can be used for the α-factor leader-directed secretion of heterologous proteins otherwise degraded at basic residues.

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