Team

Marina Ječmenica, PhD MSc

Pichia platform for difficult-to-express protein formats
The production of recombinant pharmaceutical proteins is highly important for global public health. Komagataella phaffii is a widely used host to produce such proteins and therefore represents an important target towards more sustainable, yet economically competitive bioprocesses.
The overall aim of this project is to reduce the timelines in strain development for difficult-to-express, but therapeutically promising protein formats. For this purpose, technologies that allow for rapid and efficient cell and genome engineering will be further advanced.

email: marina.jecmenica(at)boku.ac.at
phone: +43 1 47654 79032 / -79142

Rastislav Jonis, MSc

Modification of morphology of the Endoplasmic Reticulum in Komagataella phaffii
I am studying the effect of changes to the endoplasmic reticulum (ER), mainly the ratio of sheets and tubules in its composition, on the production and secretion of complex proteins, in this case antibody fragments. K. phaffii (formerly Pichia pastoris) is a promising organism for industrial biotechnology and the effect of morphological changes to the ER has so far been understudied. Aside from increasing from optimizing the protein production, I will also be studying the interactome of recombinant proteins in the newly engineered ER space.

email: rastislav.jonis(at)boku.ac.at

Vincent Elias Kaltenbach, MSc

What´s in there? - Developing rapid and high-purity organelle isolation methods for advanced subcellular metabolomics in yeast
My research project within the Cluster of Excellence (COE) Circular Bioengineering aims to establish metabolomic analysis at the subcellular level, surpassing current technical limitations. First, I will develop rapid, high-purity isolation methods of target organelles from the methylotrophic yeast Komagataella phaffii, which will subsequently be used for metabolomics and metabolic flux analysis (MFA). These methods allow for advanced resolution of valuable metabolite pools at the subcellular level which is essential for heterologous protein and metabolite production.

email: vincent.kaltenbach(at)boku.ac.at
phone: +43 1 47654-79032,79043
 

Jana Lukacova, MSc

email: jana.lukacova(at)boku.ac.at

Valentin Schachinger, Dipl.-Ing. BSc

Upcycling of pectin-rich waste streams from food and beverage industries to value-added proteins (PectiUp)

Upcycling is the process of transforming by-products or waste materials into new materials or products of greater quality. The mission of my PhD project PectiUp - funded by the Christian Doppler Research Association under the thematic call "Energy transition and Circular economy" - is to investigate the capability of yeast strains to grow on pectin-rich waste streams from food and beverage industries. I want to identify and characterize the underlying enzymes necessary to degrade pectin in yeasts and if necessary, improve the yeast’s ability to efficiently grow on these waste streams. The best performing strains will be engineered to produce value-added proteins required in food production.  It is investigated if pectin-rich waste has the potential to be a sustainable and locally available feedstock source for yeast biotechnology in a process focusing on circular bioeconomy principles.

email: valentin.schachinger(at)boku.ac.at
phone: +43 1 47654-79036,79142
 

Dorian Stadlmayer, MSc

SynthER – Reshaping the Yeast ER
Inspired by professional secretory mammalian cells, the WWTF funded project SynthER envisages to biomimic their endoplasmic reticulum (ER) architecture in yeast and plants. I will hence work on reshaping the ER in the yeast Komagataella phaffii. The project will go beyond mere physical ER expansion by tailoring functionality through orthogonal and combinatorial expression of synthetic ER shaping proteins, and the new morphologies will be monitored by a wide range of microscopic methods and quantitative image analyses. Taken together, SynthER addresses a timely research topic through a pioneering synthetic biology approach with significant potential for advancing both the scientific understanding of secretory pathway plasticity and impacting technological applications, thus benefiting medicine and biotechnology.

email: dorian.stadlmayer(at)boku.ac.at
phone: +43 1 47654-79032, 79042
 

Fiona Spreitzer, MSC

The prediction of recombinant protein production levels is a notoriously difficult task. Even small changes in the amino acid sequence, such as those introduced through mutagenesis in protein engineering, can significantly impact protein stability and production yields.
Currently, we are screening model protein libraries with fully randomized surface patches for differences in expressibility. Using yeast surface display and cell sorting, we can simultaneously sort millions of protein variants by their expression level. Based on DNA and amino acid sequences in each expression category we calculate descriptors (e.g. composition, physiochemical parameters, distances between certain amino acids) and determine their importance for explaining expression differences via machine learning. With this naïve approach we can identify and rank both expected and surprising parameters contributing to the displayed protein level. Ultimately, this study aims to provide deeper insights into surface properties dictating protein expressibility and secretability.

email: fiona.spreitzer(at)boku.ac.at
phone: +43 1 47654-79034, 77265