Loofah sponge activated by periodate oxidation as a carrier for covalent immobilization of lipase

摘要

Cellulose in loofah sponge was first oxidized by sodium periodate at positions 2 and 3 of anhydroglucose unit to introduce aldehyde groups, which were able to react with amino groups of lipase to form Schiff’s base, and result in loofah sponge immobilized lipase. The result of periodate oxidation was confirmed by determination of aldehyde group content and analysis of Fourier transform infrared spectra. The optimal pH for both free and immobilized lipases was approximately 7.5. The maximum activity of immobilized lipase was observed at 40 °C, while the free lipase exhibited maximum activity at 37 °C. The immobilized lipase presented improved thermal stability, storage stability, and reusability.