Exquisite stability and catalytic performance of immobilized lipase on novel fabricated nanocellulose fused polypyrrole/graphene oxide nanocomposite: Characterization and application.

This work was performed to describe the facile procedure of a novel nanobiocatalyst, nano cellulose fused polypyrrole/graphene oxide nanocomposite for the efficacious immobilization of lipase, a versatile hydrolytic enzyme having potential applications in industries. The fabricated nanocomposite was characterized using Fourier transform infrared spectroscopy, differential thermal analysis, thermogravimetric analysis, X-ray diffraction, scanning electron microscopy, atomic force microscopy, transmission electron microscopy, and Candida rugosa lipase was immobilized onto nanocomposite through physical adsorption. The catalytic efficiency and operational stabilities of immobilized lipase were improved significantly compared to the free lipase. The reusability profile outcomes showed that the immobilized lipase formulation was an outstanding nanobiocatalyst as it retained 85% of its original catalytic activity after 10 cycles of application. The nanobiocatalyst was employed for the synthesis of the fruit flavour compound, ethyl acetoacetate. The immobilized lipase successfully synthesised flavour compound in solvent free media and n-hexane having 27.5% and 75.5% ester yields respectively. Moreover, these outcomes demonstrating graphene oxide modified carrier induced stabilization, amended solvent tolerance and operational stability of immobilized enzyme, will have quintessential influence on practical scale up of biotechnological industries.