Research Information System
Molecular Catalysis, vol.576, 2025 (SCI-Expanded, Scopus)
Lipases are widely employed in biodiesel production through green synthesis approaches. However, enhancing the performance of these enzymes is crucial for efficient biodiesel synthesis. In this study, a recombinant lipase (Gklip) derived from a thermophilic bacterium was immobilized in a metal-organic framework (Gklip@ZIF-8). Additionally, to improve stability, cross-linking with genipin was performed (Gklip@ZIF-8-genipin). The immobilization process was validated through instrumental analyses including SEM, SEM-EDS, FTIR and TGA/DTG. Biochemical analyses determined that the optimum pH for Gklip and Gklip@ZIF-8 was 8.0, while Gklip@ZIF-8-genipin form had an optimum pH of 7.5. The optimum temperatures were 50 °C for the free enzyme and 60 °C for the both immobilized samples. Thermal stability tests showed that Gklip@ZIF-8 and Gklip@ZIF-8-genipin exhibited 2.74- and 5.86-fold higher stability at 50 °C compared to the free enzyme, respectively. Furthermore, the biodiesel production efficiency of the enzyme samples was evaluated using coconut, cold-pressed sunflower, and flaxseed oils. The free enzyme effectively produced biodiesel from coconut oil, which is rich in short-chain fatty acids, but failed to convert long-chain fatty acid-rich oils like sunflower and flaxseed into biodiesel. In contrast, Gklip@ZIF-8 and Gklip@ZIF-8-genipin efficiently produced biodiesel from all three oil types. The obtained results demonstrate that Gklip@ZIF-8 and Gklip@ZIF-8-genipin can be effectively applied in biodiesel production.