Job openings in Program 3

Description of project

The development of bioprocesses for industrial applications has been significantly advanced by omics technologies, bioinformatics, and engineering. It is widely accepted that redox-stress can be a relevant limiting factor with regards to yield and product quality. However, a global, comprehensive and systematic analysis of redox-stress with molecular resolution is lacking. The aim of this project is to extend and optimize our combined redox-proteomics and - metabolite analysis method [1] and apply it to the analysis of different hosts, products, promoter strengths and bioprocesses in collaboration with other key researchers, including Robert Kourist, Oliver Spadiut, Matthias Steiger, Wolfgang Kroutil and Florian Rudroff. Different hosts, such as E. coli, P. pastoris, cyanobacteria and archaea, will be analysed to reveal host dependent differences. Stronger promoters, methanol as inducer, oxidoreductases as biocatalytic products, and an over- or undersupply of nutrients including oxygen during fermentation are expected to increase redox-stress.

Background:

The working group has experience in redox-proteomics and -metabolite analysis [1-2].

Research Objectives

• Elucidation of redox-stress mechanisms and pathways in diverse hosts

• Identification of critical bioprocess parameters causing redox-stress

Methods

• Establishment of redox-proteomics and -metabolite analysis of diverse hosts including E. coli, P. pastoris, cyanobacteria and archaea

• Redox-proteomics and metabolite analyses

• Pathway analysis, gene ontology enrichments

• Product analysis by mass spectrometry

1. Tomin T, Schittmayer M, Sedej S, Bugger H, Gollmer J, Honeder S, Darnhofer B, Liesinger L, Zuckermann A, Rainer PP and Birner-Gruenberger R. Mass spectrometry-based redox proteome profiling of failing human hearts. Int. J. Mol. Sci. 2021, 22, 1787. doi:10.3390/ijms22041787

2. Tomin T, Schittmayer M, Birner-Gruenberger R. Addressing glutathione redox-status in clinical samples by two step alkylation with N-ethylmaleimide isotopologues. Metabolites. 2020, 10(2):71. doi: 10.3390/metabo10020071.

Main supervisor: Univ.-Prof. Ruth Birner-Grünberger

Co-supervisors: Univ.-Prof. Robert Kourist, Univ.-Prof. Oliver Spadiut

Location: TU Wien (Vienna)

Submission Deadline: 31.03.2025

Description of project

This project focuses on redox-neutral biocatalytic transformations using alcohol dehydrogenases (ADHs) to efficiently synthesize chiral lactones, which are valuable building blocks for pharmaceuticals, fragrances, and polymers. By leveraging intramolecular cofactor recycling, we aim to develop asymmetric hydroacylation reactions with broad substrate scope, optimized enzyme performance, and high hydride- and atom-economy.

Background:

The biocatalytic redox transformation of carbonyl compounds can be achieved by nicotinamide-dependent ADHs. The Hall lab has pioneered an ADH-catalyzed disproportionation of aromatic dialdehydes, allowing intramolecular nicotinamide recycling and eliminating the need for stoichiometric NAD(P)+/NAD(P)H. This interconnected cascade couples oxidation and reduction to form lactones in a self-sufficient, redox-neutral manner.

https://doi.org/10.1039/D0CC02509G; https://doi.org/10.1039/C8CS00903A

Aims:

Building on this concept, we aim to establish a stereocomplementary biocatalytic platform for the sustainable synthesis of chiral lactones, focusing on:

• Expanding the substrate scope to (pro)chiral and renewable-derived substrates

• Identifying and optimizing biocatalysts

• Enhancing product yield and selectivity through protein and reaction engineering

Qualifications & Profile requirements:

• Master’s degree in biocatalysis, organic chemistry, or a related discipline

• Hands-on experience with modern methods of organic synthesis and analytical methods (e.g., synthesis under protective atmosphere, flash-column chromatography, HPLC, GC, NMR)

• Interest in becoming familiar with the recombinant production and purification of enzymes

• Previous experience in biocatalysis or enzyme activity assay will be an asset

• Eligible as a graduate student at the University of Graz (Austria)

• Proficiency in English (written and oral)

Main supervisor: Assoc. Prof. Mélanie Hall

Co-supervisor: Assoc. Prof. Regina Kratzer

Location: University of Graz (Heinrichstrasse 28, Graz, Austria)

Submission Deadline: 31.03.2025

Description of project

Enzymatic nitration offers a sustainable route to nitro compounds used as building blocks for polymers, dyes, and pharmaceuticals. By replacing toxic chemical methods, this approach has the potential to transform the production of fine and commodity chemicals, driving innovation toward a cleaner bio-based industry.

Background:

The nitro group is essential in organic synthesis, frequently found in pharmaceuticals, dyes, and polymers. However, current nitration methods rely on toxic reagents and generate significant waste. Enzymatic alternatives remain largely unexplored. While heme-dependent enzymes have shown promise in oxidative nitration, their synthetic potential is untapped.

https://doi.org/10.1021/jacsau.4c00994

Aims:

This project explores heme-dependent oxidoreductases for selective oxidative nitration of renewable feedstocks. Key objectives include:

• Characterizing enzyme activity on model substrates

• Screening enzyme libraries for nitration of renewables

• Investigating catalytic mechanisms and promiscuity

• Scaling up production for high-yield synthesis

Qualifications & Profile requirements:

• Master’s degree in biocatalysis, organic chemistry, or a related discipline

• Hands-on experience with modern methods of organic synthesis and analytical methods (e.g., synthesis under protective atmosphere, flash-column chromatography, HPLC, GC, NMR)

• Interest in becoming familiar with the recombinant production and purification of enzymes

• Previous experience in biocatalysis or enzyme activity assay will be an asset

• Eligible as a graduate student at the University of Graz (Austria)

• Proficiency in English (written and oral)

Main supervisor: Assoc. Prof. Mélanie Hall

Co-supervisor: Asst. Prof. Stefan Hofbauer

Location: University of Graz (Heinrichstrasse 28, Graz, Austria)

Submission Deadline: 31.03.2025

Description of project

Heme containing enzymes can function as highly versatile biocatalysts for a myriad of reactions. From the four heme peroxidase superfamilies known so far, the peroxidase-peroxygenase superfamily is the least studied despite the great variety of catalyzed reactions, ranging from peroxidase and halogenation activities to oxyfunctionalizations. In contrast to cytochromes P450 these oxidoreductases use hydrogen peroxide as cosubstrate and do not need an additional regeneration enzyme, which is an advantage for industrial applications and various other processes.

Within this project the underlying mechanisms of specific, biotechnologically promising reactions will be investigated. By understanding the interplay between substrates, redox-cofactor and catalytically relevant amino acid residues the foundation for specific and targeted engineering will be granted. This will be achieved by structural and functional means using state-of-the-art biochemical, biophysical and structure-solving methods on the heterologously expressed and purified protein.

Background

A heme-thiolate peroxygenase from Aspergillus niger has been expressed, purified and initially characterized in our lab. This is the perfect basis for further in-depth kinetic, biochemical and biophysical investigations of selected variants. Phylogenetic analyses revealed further promising targets to be investigated comparatively and in parallel.

There are still important shortcomings that have to be addressed to convert unspecific peroxygenases (UPOs) from a promising tool for biocatalysis into potent applied biocatalysts. Poor levels of heterologous expression have to be overcome, as well as the presence of undesired peroxidase activities, stability issues and oxidative self-inactivation. This project aims at building a profound basis in understanding heme-thiolate peroxygenases from Aspergillus niger and from thermophile Ascomycota (e.g.  Myceliophthora thermophila) to the fullest. Digging deep into understanding substrate specificities, inactivation mechanisms, kinetic parameters of various oxyfunctionalization activities, redox potentials, structural constraints, conformational stability, and the identification of reactive intermediates during turnover will pay off to rationalize future engineering approaches.

Research Objectives

• understand established catalytic activities

• determine all kinetic parameters of turnover and inhibition

• assess substrate specificity

• minimize/shut down peroxidase activity

• connect findings with alternative and innovative H2O2 supply

Methods

Wild-type and mutant proteins will be characterized by a broad set of biochemical/biophysical methods including (i) X-ray crystallography, (ii) detailed spectral analysis (UV-vis, electron paramagnetic resonance and resonance Raman spectroscopy), and protein-based radicals in different redox- and spin-states (in collaboration with Giulietta SMULEVICH/Federico SEBASTIANI, Department of Chemistry, University of Florence, Italy), (iii) next to steady-state kinetic investigations, time-resolved multi-mixing UV-vis stopped-flow studies in order to analyze pre-steady-state kinetics, substrate specificities and enzymatic activities.  

Main supervisor: Assistant Prof. Stefan Hofbauer

Co-supervisor: Associate Prof. Roland Ludwig, Univ.-Prof. Robert Kourist

Location: BOKU University (Vienna)

Submission Deadline: 31.03.2025

Description of Project

Background

Polystyrene (PS) is among the most widely used polymers, accounting for one-fifth of globally produced polymers and, in some cases, makes up 30% of the total plastic waste in landfills.[1] It is characterized by a high chemical stability, making biological degradation difficult. Currently, PS is considered as non-biodegradable. However, hydroquinone peroxidase derived from the lignin-degrading bacterium Azotobacter beijerinckii was shown to facilitate the breakdown of PS into low molecular weight fragments when the polymer is dissolved in a solvent in a two-phase system.[2] This finding suggests that enzymatic degradation is a viable approach for addressing the environmental impact of PS waste.  

Aims / Hypotheses

 The main goal of this project is to engineer hydroquinone peroxidases to increase their ability to break down polystyrene. To this end, an effective screening system will be developed. Hydroquinone peroxidase from Azotobacter beijerinckii and homologous enzymes will be initially analyzed to assess their catalytic performance. Product profiles, substrate spectra and degradation kinetics will be measured to establish a baseline for enzyme performance and efficacy. A key objective of the project is to enhance the localization of the enzyme by generating chimeras that combine the hydroquinone peroxidase with a dedicated binding domain, which was previously optimized for PS binding.[3] This construct will spatially localize the enzyme activity at the interface between the PS and water phase, thus increasing enzyme-substrate interaction and eliminating the need for solvents. A fluorometric assay using PS-specific fluorophores will be developed to enable the monitoring of the degradation process. This assay will be integrated into a high-throughput screening system, in which PS will be coated as transparent films on 96-well plates. Enzyme activity will be measured either through the quantitative binding of the fluorophore after enzyme treatment or the release of fluorophores co-immobilized within the PS film.

Ancestral peroxidases will be generated through ancestral sequence reconstruction, aiming to identify more robust variants with enhanced degradation capabilities. Using posterior probability scores from the best-performing ancestral variants, combinatorial libraries containing 1,000 to 5,000 variants will be created. The libraries will be screened with the aim of identifying enzymes with enhanced thermal stability, redox stability, and overall enzymatic activity. The resulting data will not only offer insights into the structure-function relationship of the biocatalysts but will also provide training data for AI-assisted models to optimize enzyme performance further.

Once promising enzyme variants are identified, laboratory-scale experiments will be conducted to test the integration of the engineered enzyme system into industrially relevant settings.

Methods

• Recombinant production of extant and ancestral proteins

• GC, GC-MS to determine product profiles

• Quartz crystal microbalance (QCM) and surface plasmon resonance (SPR) for determination of degradation kinetics (collaboration with Rupert Kargl)

• PS coating on 96-well plates and establishing a high-throughput assay (with Rupert Kargl)
  

[1] Tournier et al., Chem Rev 2023; 10;123

[2] Nakamiya et al., J. Ferment. Bioeng 1997; 84:14

[3] Rübsam et al., Biotechnol Bioeng 2018; 115:321

Main supervisor: Univ.-Prof. Robert Kourist

Location: TU Graz

Submission Deadline: 31.03.2025

Description of project

The project aims to investigate artificially designed heme-dependent peroxidases and novel bacterial laccases for the hydroxylation of fatty acids. The peroxidases are intended to perform alpha-hydroxylation, however in contrast to known alpha-hydroxylating peroxidases they should lead to the elusive opposite enantiomer in highly optically pure form.

Background

Previous studies on alpha-hydroxylating enzymes (e.g. 10.1039/d3gc04593e) have shown that all of them are mainly (S)-selective. There is no enzyme known yet, to produce exclusively the (R)-enantiomer. Getting the (R)-enantiomer will allow novel options for upgrading fatty acids e.g. as building blocks for polymers or pharmaceuticals. On the other hand, laccases have not been described for the oxidation of fatty acids in the absence of a mediator yet.

Research objectives

• Regio- and stereoselective hydroxylation of fatty acids using peroxidases and laccases

• Identifying stereo-complementary enzymes

• Substrate scope of novel bacterial laccases

Methods

Enzyme expression, GC/HPLC analytics also on chiral phase, isolation of products, characterization of product (NMR, MS…), Computational tools (sequence search/ enzyme structures), determination of absolute configuration, if required chemical synthesis of reference material.

Qualifications & Profile requirements

• Master’s degree in biocatalysis, organic chemistry, biotechnology, or a related discipline

• Hands-on experience with biocatalysis and analytical methods, experience with organic synthesis is of advantage

• Know-how of compound and enzyme characterization

• Eligible as a graduate student at the University of Graz (Austria) (Klick here for further information)

• Proficiency in English (written and oral)

Main supervisor: Univ.-Prof. Wolfgang Kroutil

Co-supervisor(s): Prov.-Doz. Dr. Doris Ribitsch, Assistant Prof. Stefan Hofbauer, Univ.-Prof. Ruth Birner-Grünberger

Location: University of Graz

Submission Deadline: 31.03.2025

Description of project

The project aims to search for alpha-ketoglutarate (alpha-KG) dependent enzymes for the regio- and stereo-selective functionalisation of fatty acids. alpha-KG dependent enzymes will be evaluated for their ability to regio-selectively hydroxylate fatty acids. Subsequently the stereochemistry of the introduced hydroxy will be determined.

Background

Fatty acids can be considered as easily accessible starting material from natural resources. Chemical methods for fatty acid functionalisation lead in general to an (almost) inseparable mixture of products as soon as not only the alpha-position is concerned. Thus, functionalisation at a specific position of the fatty chain, e.g. hydroxylation or even amination, is elusive with chemical means. Nevertheless, also only few biocatalytic examples have been reported. For instance, there is to the best of our knowledge no specific method for hydroxylation at C4 available.

Research Objectives

Regio- and stereoselective functionalisation of fatty acids using alpha-KG enzymes

Investigation of substrate scope

Evaluation of applications for transforming fatty acids to more valuable products

Methods

Enzyme expression, GC/HPLC analytics also on chiral phase, isolation of products, characterization of product (NMR, MS…), Computational tools (sequence search/ enzyme structures), determination of absolute configuration, if required chemical synthesis of reference material.

Qualifications & Profile requirements

• Master’s degree in biocatalysis, organic chemistry, biotechnology, or a related discipline

• Hands-on experience with biocatalysis and analytical methods, experience with organic synthesis is of advantage

• Know-how of compound and enzyme characterization

• Eligible as a graduate student at the University of Graz (Austria) (Klick here for further information)

• Proficiency in English (written and oral)

Main supervisor: Univ.-Prof. Wolfgang Kroutil

Co-supervisor(s): Univ.-Prof. Chris Oostenbrink, Assistant Prof. Stefan Hofbauer, Univ.-Prof. Ruth Birner-Grünberger

Location: University of Graz

Submission Deadline: 31.03.2025

Enzymes are highly powerful and potent tools in nature. In this project we want to repurpose ROS producing enzymes for potential use in degradation of synthetic polymers. Candidate enzymes will be thoroughly studied to understand their structure function relationship to the fullest in order to have a solid basis for engineering approaches that ultimately yield highly efficient and stable “blockbuster” enzymes.

Background

The degradation of biopolymers requires a suite of specific enzymes secreted by plant biomass degrading microorganisms. For synthetic polymers, especially the difficult to depolymerize polyolefines, like polyethylene or polypropylene, such specific enzymes have not been evolved by organisms yet. Instead of combining a series of enzymes with different activities, the proposed strategy involves enzymes producing reactive compounds that start depolymerization reactions of recalcitrant polymers. Bacterial ROS producing oxidoreductases will act as a starting point in this project.

Aims

In this project, enzymes producing ROS species, hypohalous acids and other radicals will be screened, produced, characterized and engineered. Special focus will be put on the thermal and turnover stability of these “blockbuster” enzymes and various methods will be used to engineer stable producers of highly reactive species. The produced enzymes will be distributed in the COE to be studied with biopolymers in Program 1 and polyolefines in Program 3.

Methods

• Genomic-, microorganism- and activity screening methods

• Enzyme expression and purification

• Biochemical characterization (protein analysis and kinetic measurements)

• Protein engineering methods

• Application in processes and process engineering

Main supervisor: Assistant Prof. Stefan Hofbauer

Co-supervisor: Associate Prof. Roland Ludwig

Location: BOKU University (Vienna)

Submission Deadline: 31.03.2025

Background

Enzymes as bioelectrocatalysts need to be connected to an electrode. Chemical immobilization methods lead to random orientations of the enzyme on the electrode and deactivation. The oriented immobilization of enzymes in a monolayer can be achieved by peptide or protein sequences/modules that bring the enzymes in productive contact with the electrode.

Aim

In this project, bioelectrocatalysts will be fused with metal-binding peptides or protein binding modules for carbon or redox polymers to immobilize them on electrode materials (e.g. platinum, gold, carbon, redox polymers). For this purpose, metal-binding peptides will be screened by phage display and naturally occurring protein binding modules will be screened and engineered. Candidate Peptides and proteins will be tagged to bioelectrocatalysts for oriented immobilization and the reactions electrochemically investigated.

Methods

• Affinity screening (fluorescence microscopy, SPR)

• Phage display screening of metal-binding peptides using model metal surfaces

• Protein engineering (Rational design) of protein binding modules

• Recombinant protein expression and purification

• Biochemical and electrochemical characterization

Main supervisor: Prov.-Doz. Dr. Doris Ribitsch

Co-supervisor: Associate Prof. Roland Ludwig

Location: BOKU University (Tulln)

Submission Deadline: 31.03.2025

Description of project

Development of efficient bio-electrocatalytic systems based on advanced understanding, and engineering, of the functional interactions between enzymes and electrode surfaces; design of enzymes and surfaces for optimized interaction for mediated or direct electron transfer with electrodes

Background

Bio-electrocatalysis is promising to perform chemical transformations with minimal use of reagents and low waste produced. The design of electrochemical reactors often requires that enzyme catalysts are immobilized on the electroactive surfaces of electrodes. Electrode materials (e.g., metals, carbon) are often poorly suitable to provide an interface for interaction with the enzyme catalysts for immobilization. The project aims to deepen the understanding of enzyme interactions with electrode materials in order to enable more efficient engineering of functional bio-interfaces in, and for, electrochemical transformations.

Research Objectives

• Exploring and optimizing enzyme interactions with carbon-based electron surfaces

• Designing enzymes for improved active adsorption on electrodes

• Engineering of enzyme-surface interactions for direct electron transfer

• Characterization of enzyme electrodes for mediated and direct electron transfer

Methods

Electrochemical analysis and characterization (e.g., cyclic voltammetry, impedance spectroscopy); characterization of enzyme-surface interactions (e.g., atomic force microscopy, fluorescence microscopy); enzyme function assessment on surface and in solution; enzyme engineering (e.g., development of fusion proteins); analysis and characterization of enzyme binding to electrode surfaces; protein biochemistry (expression, purification, stability).

Main supervisor: Univ.-Prof. Bernd Nidetzky

Co-supervisor: Associate Prof. Roland Ludwig

Location: TU Graz

Submission Deadline: 31.03.2025

Description of project

Enzymes are omnipresent in biological systems and are key components of circular bioengineering efforts. Catalyzing chemical reactions, they invariably are involved in the making and breaking of chemical bonds. Moreover, many of the enzymes that are central to the COE are metalloenzymes or driven by either light or electron transfer. All of these properties require the inclusion of quantum mechanical methods in appropriate in silico descriptions. Arguably, enzymes are most efficiently described by hybrid quantum and classical mechanical approaches (QM/MM). In this project we will further develop the description of QM/MM Hamiltonians using advanced QM methods and machine-learned potentials.

Background

The computaitonal inefficiency of most quantum mechanical methods hamper either a full description of enzymes at the QM level or a sufficiently extensive sampling to describe both enthalpic and entropic effects appropriately. QM/MM approaches offer solutions that combine the best of both worlds. Molecular dynamics simulations can be coupled with a plethora of QM methods, specifically suitable for specific questions. Recently tremendous progress has been made in the use of machine-learned potentials, which learn quantum mechanical interactions from an appropriate training set. The inclusion of these methods in QM/MM settings, furthermore, allows us to resolve interfacial limitations of traditional QM/MM methods. Inclusion of reactivity and enzymatic properties of proteins through electrostatic and dynamics effects are among the next challenges to tackle computationally.

Research Objectives

• Description of enzymatic reactions via QM/MM methods

• Inclusion of dynamic effects in quantum mechanical descriptions of heme proteins

• Inclusion of enzymatic reactivity in machine-learned hybrid QM/MM calculations

Methods

Quantum mechanical calculations, molecular dynamics simulations, Buffer Region Neural Network approach, free-energy calculations

Main supervisor: Univ.-Prof. Chris Oostenbrink

Co-supervisor: Assistant Prof. Stefan Hofbauer

Location: BOKU University (Vienna)

Submission Deadline: 31.03.2025

Description of project

EcoFusion: Pioneering Light, Air, and Nature for Plastic and PFAS Degradation and Recycling

The goal of this project is to find a new and better way to deal with plastic and PFAS pollution. Right now, we often dispose of plastic in ways that harm the environment. The project suggests a new method to recycle plastics by creating a special enzyme that uses light, and air to break down plastics and PFAS in water. The primary aim of this project is to discover an improved method for upcycling these plastics and PFAS into valuable materials, aligning with the concept of a sustainable and closed-loop society. The innovative aspect of this initiative involves the utilization of specialized proteins capable of generating reactive oxygen species (ROS) upon light exposure. These proteins are affixed to additional elements to facilitate sticking to plastic surfaces. This unique approach targets microplastics and aims to solve the pollution problem.

Background

The group has experience with flavin enzymes and with the analysis of reactive oxygen species. Additionally, the group has gained experience in surface analytics of plastics and the analysis of degradation products by NMR and MS/MS methods.

Research Objectives

• Design and production of plastic and PFAS degrading enzymes.

• Analysis of the degradation products and elucidation of degradation mechanism.

• Utilization of the degradation products for the productions of novel chemicals.

Methods

• Selection of potential enzyme candidates for the degradation of plastic and PFAS.

• Cloning and expression in Escherichia coli and subsequent isolation, purification and characterization of these enzymes.

• Testing on their degradation activities.

Main supervisor: Associate Prof. Florian Rudroff

Co-supervisor: Univ.-Prof. Katharina Schröder

Location: TU Wien (Vienna)

Submission Deadline: 31.03.2025

Background

In today's industrialized world, technical waste streams, containing diverse compounds, such as metal ions, microplastics, and very different organic molecules, are generated at an unprecedented rate. These waste streams, if not managed effectively, contribute to environmental pollution and resource depletion. Upcycling of these technical waste streams offers a viable solution to mitigate environmental impact while maximizing resource efficiency. By repurposing and transforming discarded materials into valuable products, upcycling helps to reduce landfill waste, lower carbon emissions, and promote a circular economy. Upcycling technical waste streams not only conserves natural resources but also opens up economic opportunities by creating new value-added products from discarded materials.

In this project very different liquid and gaseous waste streams, from food industry, biorefinery (in collaboration with Katharina Schröder), syngas production, as well as gasification, will be tested for their suitability to be used as substrates/growth medium for a variety of different microorganisms (cyanobacteria, Archaea, yeasts, bacteria). Based on spent media analyses, physiological strain characterization as well as Redox proteomics (in collaboration with Ruth Birner-Grünberger), strains will be either metabolically engineered (in collaboration with Matthias Steiger) or respective bioprocesses will be designed. Depending on the microorganism, value generation will be assessed (e.g. water remediation, native cell constituents, use as feed or fertilizer) and recombinant strains will be generated to increase value generation (in collaboration with Florian Rudroff). The overall goal is to make use of the wealth of microbial diversity to upcycle different liquid and gaseous industrial waste streams.

Research Objectives

• What are different industrial waste streams composed of? What is the batch-to-batch variability? What is a proper analytical concept to assess the respective composition (PAT)?

• Which microorganisms can use the contained energy source, nitrogen and phosphate, as well as trace elements?

• How does the redox proteome change for the different microorganisms grown on defined media vs. these waste streams?

• How can the organisms be engineered to make use of the waste streams?

• How can the respective bioprocesses be designed to be efficient and as sustainable as possible?

• What is a suitable PAT strategy to allow scalable and reproducible bioprocesses?

• How does the environmental footprint compare to state-of-the-art bioprocesses?

• Can these bioprocesses be described in models?

• Can these bioprocesses by intensified to further decrease the environmental footprint – even model-based?

Methods

• Analysis of waste stream composition (HPLC, IC, GC)

• Bioreactor cultivations in batch, fed-batch and continuous mode (scale 0.1-10 L)

• Series of analytical technologies (e.g. HPLC, spectroscopy, protein analytics, analyses for physiology, viability, productivity, etc)

• OMICs fingerprints of selected samples in collaboration with Ruth Birner-Grünberger

• Strain engineering in collaboration with Matthias Steiger

• Data evaluation and interpretation

• Bioprocess modeling

Main supervisor: Univ.-Prof. Oliver Spadiut

Co-supervisor: Assistant Prof. Matthias Steiger, Univ.-Prof. Ruth Birner-Grünberger

Location: TU Wien (Vienna)

Submission Deadline: 31.03.2025