• Pichia pastoris

    Pichia pastoris

    a host for recombinant protein production

Molecular Biotechnology determines and describes the underlying molecular principles of biotechnological production processes. Among these products, recombinant proteins (e.g. biotherapeutics and industrial enzymes) are of paramount importance. To accelerate the development of production strains it is crucial to understand the molecular physiology of the host, and the specific limitations that the product may exert on expression.

The yeast Pichia pastoris (syn. Komagataella spp) has emerged as an efficient host for recombinant protein production. We focus on the comprehensive understanding of protein folding and secretion, and on cell engineering for the improvement of these processes (BioTop Project 2019; BioTop Project 2015). Furthermore, we are part of the MSCA-ITN SECRETERS which designs new-generation microbial platforms for the production of disulphide-bonded and 'difficult-to-express' proteins (http://secreters-msca-itn.eu/).

In the “CD-Laboratory for growth-decoupled protein production in yeast”, the connection between cell growth and protein secretion is analyzed by looking at yeast cells cultivated at very low specific growth rates, using the yeast P. pastoris as a model system (link).

Systems biology analyses include genome, transcriptome, proteome, metabolome, and fluxome analyses, and metabolic modelling, these high throughput technologies are performed in cooperation with the Department of ChemistryFH Campus Wien Bioinformatics group, and VBCF. Computational metabolic modelling is performed in joint projects with Metabolic Modelling group. Curated genome sequences of different P. pastoris strains are available at www.pichiagenome.org.


Pichia Genome Database

This database hosts up-to-date annotation information of the genome of the methylotrophic yeast Pichia pastoris (Komagataella spp.), containing the new manually achieved annotation of K. phaffii strain CBS7435, and basic sequence and annotation information taken from the GenBank data of various Komagataella strains and species.
Additionally the sequence information of S. cerevisiae strain S288c is also available for comparison and homolog display.

Latest Publication

Komagataella phaffii Erp41 is a protein disulfide isomerase with unprecedented disulfide bond catalyzing activity when coupled to glutathione

Palma A, Rettenbacher LA, Moilanen A, Saaranen M, Gasser B, Ruddock LW. 2024 - J Biol Chem. 2024 Mar;300(3):105746. doi: 10.1016/j.jbc.2024.105746. Epub 2024 Feb 13. PMID: 38354787; PMCID: PMC10938136. (Fig.Small-scale coexpression tests of PDI-family members with Komagataella phaffii Ero1. )

Synthetic activation of yeast stress response improves secretion of recombinant proteins

(2023) Zahrl RJ, Prielhofer R, Burgard J, Mattanovich D, Gasser B. N Biotechnol. 2023 Mar 25;73:19-28. doi: 10.1016/j.nbt.2023.01.001.

BOKU Töchtertag 2022

Workshop: Lebende Proteinfabriken: von der Zelle zum Produkt
Hefen und andere Mikroorganismen werden häufig zur Herstellung von wichtigen Nahrungsmitteln und Medikamenten verwendet. Beispiele dafür sind Brot und Backwaren, Bier, Wein sowie Medikamente zur Behandlung von Diabetes (Insulin) und Impfstoffe (zB gegen Hepatitis B oder HPV). Im Workshop werden wir folgende Experimente gemeinsam durchführen: Mikroorganismen und Zellen im Mikroskop betrachten, Genetische Information (DNA) aus Lebensmitteln extrahieren und/oder Proteingehalt in Lebensmitteln bestimmen. Mit fachlicher Einleitung und Unterstützung von Brigitte Gasser wurde den interessierten Mädchen die Welt der Mikrooorganismen spannend näher gebracht!
Characterising the metabolic rewiring of extremely slow growing Komagataella phaffii.
Coltman BL, Rebnegger C, Gasser B, Zanghellini J. 2024 - Microb Biotechnol. 2024 Jan;17(1):e14386. doi: 10.1111/1751-7915.14386. Epub 2024 Jan 11. PMID: 38206275 (Fig. Accumulation profiles and derivative rates of the three retentostat cultivations after regression model adaptations.)
Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast
Palma A, Rettenbacher LA, Moilanen A, Saaranen M, Pacheco-Martinez C, Gasser B, Ruddock L. 2023 - Sci Rep. 2023 Aug 31;13(1):14298. doi: 10.1038/s41598-023-41375-z. PMID: 37652992; PMCID: PMC10471769.

Going beyond the limit: Increasing global translation activity leads to increased productivity of recombinant secreted proteins in Pichia pastoris.

(2022) Staudacher J, Rebnegger C, Dohnal T, Landes N, Mattanovich D, Gasser B. Metab Eng. 2022 Mar;70:181-195. doi: 10.1016/j.ymben.2022.01.010. Epub 2022 Jan 25. PMID: 35091068

FEMS Yeast Research Best Article Award 2021

What makes Komagataella phaffii non-conventional?

(2021) Ata Ö, Ergün BG, Fickers P, Heistinger L, Mattanovich D, Rebnegger C, Gasser B. FEMS Yeast Res. 2021 Dec 24;21(8):foab059. doi: 10.1093/femsyr/foab059. PMID: 34849756; PMCID: PMC8709784.

Established tools and emerging trends for the production of recombinant proteins and metabolites in Pichia pastoris.

(2021) De S, Mattanovich D, Ferrer P, Gasser B. Essays Biochem. 2021 Jul 26;65(2):293-307. doi: 10.1042/EBC20200138. PMID: 33956085

Brigitte Gasser, Assoc. Prof. Priv.-Doz. Dipl.-Ing. Dr.nat.techn.

Stellvertreterin
H79200 Institut für Mikrobiologie und Mikrobielle Biotechnologie

Email
brigitte.gasser@boku.ac.at
Telefon
+43 1 47654-79033
Fax
+43 1 47654-79009
Postadresse
Institut für Mikrobiologie und Mikrobielle Biotechnologie
Muthgasse 18/V
1190 Wien
Büro
MUG1-04/03
Muthgasse 18/IV
1190 Wien

Publications