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PROTEIN SECRETION IN PICHIA PASTORIS AND ADVANCES IN PROTEIN PRODUCTION. APPLIED MICROBIOLOGY BIOTECHNOLOGY
Recombinant protein secretion
Unfolded protein response
Protein folding
Afiliación
Fundação Oswaldo Cruz. Centro de Pesquisas René Rachou. Belo Horizonte, MG, Brazil
Cornell University. Department of Microbiolog. Ithaca, NY, USA
Cornell University. Department of Microbiolog. Ithaca, NY, USA
Cornell University. Department of Microbiolog. Ithaca, NY, USA
Cornell University. Department of Microbiolog. Ithaca, NY, USA
Resumen en ingles
Yeast expression systems have been successfully used for over 20 years for the production of recombinant proteins. With the growing interest in recombinant protein expression for various uses, yeast expression systems, such as the popular Pichia pastoris, are becoming increasingly important. Although P. pastoris has been successfully used in the production of many secreted and intracellular recombinant proteins, there is still room for improvement of this expression system. In particular, secretion of recombinant proteins is still one of the main reasons for using P. pastoris. Therefore, endoplasmic reticulum protein folding, correct glycosylation, vesicular transport to the plasma membrane, gene dosage, secretion signal sequences, and secretome studies are important considerations for improved recombinant protein production.
Palabras clave en ingles
Pichia pastorisRecombinant protein secretion
Unfolded protein response
Protein folding
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