The “FEBS3+ Meeting: XXVIIIth BIOCHEMISTRY CONGRESS of the Czech and Slovak Societies for Biochemistry and Molecular Biology and with participation of Polish and German Biochemical Societies” with the motto “Unlocking of the Secrets of Life”, took place in Prague at the National Technical Library from 7 to 10 September 2025 on the occasion of the 70th anniversary of the founding of the original Czechoslovak Biochemical Society.
Several employees and PhD students from the Center for Interdisciplinary Biosciences, TIP UPJŠ in Košice, actively participated. Prof. Sedlák delivered a lecture titled “Evolution of Haloalkane Dehalogenase by Ribosome Display”, and dr. Tomková presented her findings in a poster entitled “Directed Evolution of Staphylokinase Improves Fibrinolytic Activity”. In addition, Prof. Sedlák and Dr. Tomková also served as chairpersons of the Enzyme and Biotechnology sections, respectively.
Both presented research results are closely related to the implementation of the APBC project.
Prof. Sedlak, in his lecture, focused on haloalkane dehalogenases, microbial enzymes that break down halogenated hydrocarbons. He showcased advanced laboratory techniques – HaloTag technology and ribosome display – which allow optimization of selected enzyme variants to produce more stable forms with improved activity for degrading specific compounds. These findings contribute to advancing the use of these enzymes in biotechnology.
The poster by Dr. Tomkova presented staphylokinase (SAK), a bacterial protein used as a clot-busting drug commonly employed in the treatment of thrombotic diseases such as stroke and heart attack, conditions that cause many deaths worldwide. However, its use is limited by immune reactions in patients. Therefore, within the APBC project, scientists are engineering non-immunogenic SAK variants. The results obtained so far confirm that the new SAK forms show promise as effective and safer thrombolytic therapies, although further improvements in stability are still needed.
