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 Chemistry, FH 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
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Synthetic activation of yeast stress response improves secretion of recombinant proteins
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BOKU Töchtertag 2022
Workshop: Lebende Proteinfabriken: von der Zelle zum Produkt
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Two homologs of the Cat8 transcription factor are involved in the regulation of ethanol utilization in Komagataella phaffii
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Pushing and pulling proteins into the yeast secretory pathway enhances recombinant protein secretion
FEMS Yeast Research Best Article Award 2021
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What makes Komagataella phaffii non-conventional?
BOKU Erfinderin 2019
Brigitte Gasser wurde 2019 als eine der BOKU Erfinderinnen 2019 gewürdigt.
In diesem Video stellt sie sich selbst und ihre Forschungsarbeit vor.
BOKU Invention Awards 2019 for Brigitte Gasser, Diethard Mattanovich, Michael Sauer and Thomas Gaßler
![D. Mattanovich, Ch. Obinger, B. Gasser, T. Gaßler](/fileadmin/_processed_/8/0/csm_csm_IFA-Tulln_25-Jahr-Feier-228_e3118e5bff_296faf823e.jpg)
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Going beyond the limit: Increasing global translation activity leads to increased productivity of recombinant secreted proteins in Pichia pastoris.
Established tools and emerging trends for the production of recombinant proteins and metabolites in Pichia pastoris.
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Treatment with surfactants enables quantification of translational activity by O-propargyl-puromycin labelling in yeast.
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Beyond alcohol oxidase: the methylotrophic yeast Komagataella phaffii utilizes methanol also with its native alcohol dehydrogenase Adh2
Brigitte Gasser, Assoc. Prof. Priv.-Doz. Dipl.-Ing. Dr.nat.techn.
- Stellvertreterin
- H79200 Institut für Mikrobiologie und Mikrobielle Biotechnologie
- brigitte.gasser@boku.ac.at
- Telefon
- +43 1 47654-79033
- Fax
- +43 1 47654-79009
- Postadresse
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Institut für Mikrobiologie und Mikrobielle Biotechnologie
Muthgasse 18/V
1190 Wien - Büro
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MUG1-04/03
Muthgasse 18/IV
1190 Wien