My research is concerned with the design of new enzymes, proteins that can catalyze a reaction.

Here I am particularly interested in the question of how to change specificity, one of the special and advantageous properties of enzymes. Enzymes have adapted binding pockets for substrates. When a suitable substrate is bound in the binding pocket, a reaction can occur there and a product is formed. This is catalyzed (accelerated) by certain amino acids ("active site") in the binding pocket reactions.

In biotechnological processes or for the biocatalytic production of certain chemical building blocks, it is often necessary for enzymes to convert substrates other than those that originally fit into their binding pocket.

The properties of the binding pocket can also be changed so that a different substrate can be bound. However, during this process the shape (folding) of the protein can also be changed. This would lead to the loss of its catalytic ability, since the active site would also change. The binding pocket can be adapted to a certain degree only.

My approach to achieve new specificities is to transfer the active site to other proteins that have differently shaped binding pockets. To achieve this goal, I apply programs and algorithms that can calculate the amino acid sequence and folding of proteins. On the one hand, classical methods are used for this purpose, on the other hand, those based on Deep Learning. The primary goal is to design new proteases, i.e. enzymes that break bonds between amino acids.

Press release TU Graz: Enzyme research between cholera and targeted design
ResearchGate

Project funding

Funding: EUR 642,450