Degorska_2025_Int.J.Biol.Macromol_318_145174

This study focuses on the development of a biocatalytic system based on lipase from Pseudomonas fluorescens immobilized on a poly(acrylamide)- and poly(ionic liquid)-based hydrogel. It was established that temperature significantly impacts polymerization rate of the monomers used, leading to the application of 70 degreesC for 30 min for the most suitable hydrogel structure. Under these conditions, the polymerization of PIL and PAM reached 63.5 % and 90.9 %, respectively. The produced hydrogel with immobilized lipase was characterized by improved by around 30 % chemical and thermal stability as compared to native enzyme and provided a suitable environment for successful lipase deposition, proven by elution of <2 % of the enzyme from the support. What is more, it was established that a higher enzyme loading resulted in greater catalytic activity, providing over 30 % higher performance after 10 reusability cycles. High enzymatic activity and enantioselectivity demonstrated by the produced system was proved in dynamic kinetic resolution of atenolol reaching over 55 % reaction yield, that was over 40 % higher as free counterpart, and attaining 100 % enantiomeric excess for the final (S)-atenolol ester.