Protein secretion in Pichia pastoris and advances in protein production. Applied Microbiology Biotechnology

dc.creatorDamasceno, L. M.
dc.creatorHuang, C. J.
dc.creatorBatt, C. A.
dc.date2014-03-19T18:13:59Z
dc.date2014-03-19T18:13:59Z
dc.date2012
dc.date.accessioned2023-09-26T20:23:31Z
dc.date.available2023-09-26T20:23:31Z
dc.identifierDAMASCENO, LM; HUANG, CJ; BATT, CA. Protein secretion in Pichia pastoris and advances in protein production. Applied Microbiology Biotechnology. 2012, vol.93, n.1, pp. 31-39.
dc.identifier0175-7598
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/7427
dc.identifier10.1007/s00253-011-3654-z
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8855858
dc.descriptionYeast 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.
dc.formatapplication/pdf
dc.languageeng
dc.publisherSpringer Link
dc.rightsopen access
dc.subjectPichia pastoris
dc.subjectRecombinant protein secretion
dc.subjectUnfolded protein response
dc.subjectProtein folding
dc.titleProtein secretion in Pichia pastoris and advances in protein production. Applied Microbiology Biotechnology
dc.typeArticle


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