In this thesis, the mechanism of lipase catalyzed synthesis of 4,6-disubstituted-3-cyano-2-pyridones was studied, and for that purpose the simplest molecule, 4,6-dimethyl-3-cyano-2-pyridone, and vitamin B6 precursor, 4-ethoxymethyl-6-methyl-3-cyano-2-pyridone, were synthesized. In order to find the optimal conditions for their synthesis a response surface methodology (RSM) was applied, and the influence of three reaction factors (temperature, enzyme concentration and substrate molar ratio) was investigated. After that, at determined optimal conditions, the kinetic study was performed and the obtained results showed that these reactions can be described with ping-pong bi-ter model with inhibition by cyanoacetamide. The second part of the thesis was focused on the development of the immobilized enzyme with the best catalytic properties. Lipase was adsorbed or covalently bonded on different supports, and the highest enzyme loading, of 1.4 mg per 1 mg of support, was achieved with amino functionalized carbon nanotubes. It was found that immobilized preparations with the highest percentage of retained activity were obtained when lipase was adsorbed on unmodified carbon nanotubes in a high ionic strength buffer (up to 85 %). Immobilized enzymes with the highest total activity were obtained by binding lipase on oxidized carbon nanotubes under conditions that promote covalent binding. Immobilized preparations with the best properties showed high catalytic activity in the synthesis of 4,6-dimethyl-3-cyano-2-pyridone.