Nature uses enzymes to catalyse the biochemical reactions in living organisms. Therefore enzymes generally function under mild reaction conditions (i.e., ambient temperatures in aqueous solvent systems) and possess excellent regio-, chemo-, or stereoselectivity. Application of enzymes as catalysts in the production of chemicals has the potential to serve as a sustainable and efficient alternative to traditional catalysts used in organic synthesis.
In our group we apply enzymes as catalyst to solve the challenging task of synthetic organic chemistry – asymmetric synthesis. In spite of numerous enzymes discovered so far, there are still a lot of knowledges missing about their mechanism and substrate scope. We believe, that thorough investigation of the biochemical properties of the discovered enzymes, will not only help to improve the existing reactions and bring them on the level of industrial application, but also will help to discover new reactions which might be good alternative to the standard chemical methods. Finally, the challenges of narrow substrate scope, poor stereoselectivity and/or insufficient stability can be overcome by application of methods of protein and reaction engineering.
Working on the interface of different bio-branches, such as synthetic and structural biology, biotechnology, bioinformatics and biocatalysis we tend to understand and optimize the enzymatic reactions for the asymmetric synthesis of valuable compounds and thus increase the application of biocatalysts in organic chemistry. Particularly, our research focuses on the development of the efficient biocatalytic processes for the asymmetric carbon-carbon bond formation and synthesis of chiral non-natural amino acids.