Lipase immobilization on glutaraldehyde activated graphene oxide/ chitosan/cellulose acetate electrospun nanofibrous membranes and its application on the synthesis of benzyl acetate

In this research, lipase Km12 was immobilized on the glutaraldehyde-activated graphene oxide/chitosan/cellulose acetate nanofibers (GO/Chit/CA NFs) prepared by the electrospinning method. This immobilized lipase exhibited a higher activity value than the free lipase in the acidic pH region. This enzyme showed a 10 degrees C shift in the maximum temperature activity. Results displayed that the Vmax value of NFs-lipase was 0.64 mu mol/min, while it was gained 0.405 mu mol/min for the free lipase. The activity of NFs-lipase was reserved 100% after 10 min maintaining at 60 degrees C, in which the free lipase only kept 75% of its original activity. Moreover, a 20% enhancement in the lipase activity was observed for NFs-lipase after 180 min of incubation at 60 degrees C, compared to the free enzyme. Reusability studies exhibited that the immobilized lipase well-kept 80% of its original activity after 10 cycles of reusing. Results displayed that 14% of the protein was leaked from NFs-lipase at the same condition. Transesterification results indicated that the free lipase exhibited 65% and 85% conversation level of benzyl acetate after 12 and 24 h of incubation. Besides, the immobilized lipase showed 80% and 95% conversation level at the same condition. These results indicated the high performance of free and immobilized lipase in the production of benzyl acetate for applications in the perfume and cosmetic industries.

Automated summary

The immobilized lipase exhibited higher activity in acidic pH and a temperature shift, showing 100% activity retention at 60°C after 10 min. 20% enhancement in activity and 80% retention after 10 cycles of reuse were observed. The leak of protein and improved conversion level in transesterification indicated the potential of immobilized lipase in industrial applications.