1. ZHAW digitalcollection
  2. Life Sciences und Facility Management
  3. Publikationen
  4. Publikationen Life Sciences und Facility Management
Full metadata record
DC FieldValueLanguage
dc.contributor.authorKovar, Karin-
dc.contributor.authorLooser, Verena-
dc.contributor.authorHyka, Petr-
dc.contributor.authorMerseburger, Tobias-
dc.contributor.authorMeier, Christian-
dc.date.accessioned2018-10-08T11:32:01Z-
dc.date.available2018-10-08T11:32:01Z-
dc.date.issued2010-11-01-
dc.identifier.issn0009-4293de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/11465-
dc.description.abstractHealth and safety concerns, enhanced quality criteria, and environmental sustainability, have prompted investigations into production using recombinant yeasts as a feasible alternative for isolation of proteins from natural animal or plant sources, as well as for processes utilising either mammalian cell cultures or bacterial systems. An overview of recent research papers and review articles provides readers with a comprehensive insight into the field of next-generation yeast expression systems. Major breakthroughs in recombinant yeast technology linked to Pichia pastoris are (i) the public availability of tools to generate proteins with tailored and highly homogenous N-glycan structures, similar to the forms assembled in humans, (ii) the recent accomplishment of the annotation of its genome sequence, and finally, (iii) the presence of the first few (non-glycosylated) therapeutic proteins in Pichia on the market. The P. pastoris expression platform is now well developed, as proven by multiple products used in human and veterinary medicine and in industry (e.g. enzymes for chemical synthesis and for the modification/synthesis of pharmaceuticals, drug target proteins used for structural analysis or for high throughput screening, proteins for diagnostics, proteinous biomaterials, vaccines, and therapeutic proteins). Nevertheless, the complexity of protein analysis (monitoring) continues to restrict process development for recombinant products. Drawing on combined expertise in molecular biology and process technology, the Institute of Biotechnology (IBT) at the Zurich University of Applied Science (ZHAW) and its international partners have developed solutions which (i) fully eliminate (or partially reduce) the use of methanol, which is undesirable in high-cell-density and high-productivity processes, (ii) match both strain construction and process design with the target protein characteristics to the benefit of the cells’ physiological shape, and (iii) allow multi-gene expressions to be balanced to achieve custom tailored and reproducible protein quality at the level of (engineered) posttranslational modifications. In addition to enabling superior product quality specifications to be achieved with reduced development time, these innovations have helped the industries involved to minimise financial risks and the risk of failure, as well as create an opportunity for (new) drugs with improved functionality at low cost.de_CH
dc.language.isoende_CH
dc.publisherSchweizerische Chemische Gesellschaftde_CH
dc.relation.ispartofChimiade_CH
dc.rightsLicence according to publishing contractde_CH
dc.subjectTailored and engineered glycosylationde_CH
dc.subjectPichia pastoris expression platformde_CH
dc.subjectRecombinant enzymesde_CH
dc.subjectGreen chemistryde_CH
dc.subject.ddc540: Chemiede_CH
dc.titleRecombinant yeast technology at the cutting edge : robust tools for both designed catalysts and new biologicalsde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
zhaw.organisationalunitInstitut für Chemie und Biotechnologie (ICBT)de_CH
dc.identifier.doi10.2533/chimia.2010.813de_CH
zhaw.funding.euNode_CH
zhaw.issue11de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.end818de_CH
zhaw.pages.start813de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume64de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
zhaw.webfeedBiokatalysede_CH
Appears in collections:Publikationen Life Sciences und Facility Management

Files in This Item:
There are no files associated with this item.
Show simple item record
Kovar, K., Looser, V., Hyka, P., Merseburger, T., & Meier, C. (2010). Recombinant yeast technology at the cutting edge : robust tools for both designed catalysts and new biologicals. Chimia, 64(11), 813–818. https://doi.org/10.2533/chimia.2010.813
Kovar, K. et al. (2010) ‘Recombinant yeast technology at the cutting edge : robust tools for both designed catalysts and new biologicals’, Chimia, 64(11), pp. 813–818. Available at: https://doi.org/10.2533/chimia.2010.813.
K. Kovar, V. Looser, P. Hyka, T. Merseburger, and C. Meier, “Recombinant yeast technology at the cutting edge : robust tools for both designed catalysts and new biologicals,” Chimia, vol. 64, no. 11, pp. 813–818, Nov. 2010, doi: 10.2533/chimia.2010.813.
KOVAR, Karin, Verena LOOSER, Petr HYKA, Tobias MERSEBURGER und Christian MEIER, 2010. Recombinant yeast technology at the cutting edge : robust tools for both designed catalysts and new biologicals. Chimia. 1 November 2010. Bd. 64, Nr. 11, S. 813–818. DOI 10.2533/chimia.2010.813
Kovar, Karin, Verena Looser, Petr Hyka, Tobias Merseburger, and Christian Meier. 2010. “Recombinant Yeast Technology at the Cutting Edge : Robust Tools for Both Designed Catalysts and New Biologicals.” Chimia 64 (11): 813–18. https://doi.org/10.2533/chimia.2010.813.
Kovar, Karin, et al. “Recombinant Yeast Technology at the Cutting Edge : Robust Tools for Both Designed Catalysts and New Biologicals.” Chimia, vol. 64, no. 11, Nov. 2010, pp. 813–18, https://doi.org/10.2533/chimia.2010.813.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.