This study investigates the use of lipases from *Geotrichum candidum* 4013 for the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine (DHPA) in dimethylformamide. The lipases were immobilized on chitosan beads to improve their catalytic properties and reusability. Five commercially available lipases (from hog pancreas, *Aspergillus niger*, *Candida antarctica*, *Pseudomonas fluorescens*, and *Mucor miehei*) were also tested. The results showed that the lipase from *Candida antarctica* was the most efficient in terms of chemical yield, while the lipase from *Aspergillus niger* produced lower yields. The immobilized lipases from *G. candidum* 4013 exhibited reduced catalytic activity compared to their free forms, possibly due to the immobilization process. The reusability of the immobilized lipases was evaluated, and they retained 70% of their initial activity after two runs. The study highlights the potential of lipases in the synthesis of prodrugs and the importance of enzyme immobilization for improving catalytic performance and reusability.This study investigates the use of lipases from *Geotrichum candidum* 4013 for the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine (DHPA) in dimethylformamide. The lipases were immobilized on chitosan beads to improve their catalytic properties and reusability. Five commercially available lipases (from hog pancreas, *Aspergillus niger*, *Candida antarctica*, *Pseudomonas fluorescens*, and *Mucor miehei*) were also tested. The results showed that the lipase from *Candida antarctica* was the most efficient in terms of chemical yield, while the lipase from *Aspergillus niger* produced lower yields. The immobilized lipases from *G. candidum* 4013 exhibited reduced catalytic activity compared to their free forms, possibly due to the immobilization process. The reusability of the immobilized lipases was evaluated, and they retained 70% of their initial activity after two runs. The study highlights the potential of lipases in the synthesis of prodrugs and the importance of enzyme immobilization for improving catalytic performance and reusability.