Immobilization of enzyme using natural feldspar for use in the synthesis of oleyl oleate

Abstract

Natural feldspar from Tanah Putih, Gua Musang, Kelantan (Malaysia) was physico-chemically characterized using X-ray Diffraction (XRD), Surface Area and Porosity Analysis (ASAP) and Energy Dispersive X-ray (EDX) techniques. The feldspar was found to be of the potassium (K) type, with major components containing aluminum (Al), and silicon (Si). The feldspar also possesses 38.307 nm mean pore diameter and 18.717 m2/g surface area. Candida rugosa (CRL) was then immobilized onto natural feldspar by physical adsorption method. About 49.96% of protein content was immobilized onto the support. The catalytic activity of the immobilized lipase was determined by the esterification reaction using oleic acid and oleyl alcohol. The effects of various reaction temperatures, stability in organic solvent, and lipase recyclability on the esterification reaction for the native and immobilized lipase were investigated. Feldspar-immobilized lipase exhibited higher activity than that of the native lipase. Immobilized lipase retained its activity ca. 50% even after incubation at high temperature (70°C) with the optimum reaction temperature of 40°C, long incubation in hexane up to 10 days and after ten repeated cycles used. Feldspar-immobilized lipase also showed considerably efficient reusability where it was not easily leached even after being washed with large amount of hexane (20 mL). These results showed that physical adsorption method is suitable for the immobilization of lipase onto feldspar.