Immobilization of lipase on β-cyclodextrin grafted and aminopropyl-functionalized chitosan/FeO magnetic nanocomposites: An innovative approach to fruity flavor esters esterification.

The lipase from Bacillus licheniformis NCU CS-5 was immobilized onto β-cyclodextrin (CD) grafted and aminopropyl-functionalized chitosan-coated FeO magnetic nanocomposites (FeO-CTS-APTES-GA-β-CD). Fourier transform infrared spectroscopy, thermogravimetry analysis, X-ray diffraction, scanning electron microscopy and transmission electron microscopy showed that not only the functionalized magnetic nanoparticles were synthesized but also the immobilized lipase was successfully produced. The immobilized lipase exhibited higher optimal pH value (10.5) and temperature (60℃) than the free lipase. The pH and thermal stabilities of the immobilized lipase were improved significantly compared to the free lipase. The immobilized lipase remained more than 80% of the relative activity at temperature of 60 ℃ and pH 12.0. The immobilized lipase also remained over 80% of its relative activity after 28 days of storage and 15 cycles of application. The application of the immobilized lipase in esterification of isoamyl acetate and pentyl valerate showed that maximum esterification efficiency was achieved in n-hexane having 68.0% and 89.2% respectively. Therefore, these results indicated that the FeO-CTS-APTES-GA-β-CD nanoparticles are novel carriers for immobilizing enzyme, and the immobilized lipase can be used as an innovative green approach to the synthesis of fruity flavor esters in food industry.