Comparative Study on Lipase Immobilized onto Organo-Cation Exchanged Kaolin and Metakaolin: Surface Properties and Catalytic Activity

Clay mineral has received much attention to be used as biocatalysts as it is cheaper, easily available and environ-mentally friendly. However, the use of unmodified clay, in particular kaolin for enzyme immobilization showed un-suitability of this support due to its negative charge. In this study, the hydrophobic properties of kaolin and me-takaolin (kaolin heated to 650 °C) were adjusted by the intercalation with benzyltriethylammonium chloride (BTEA-Cl), at concentrations 2.0 times the cation exchange capacities (CEC) of the clays. The supports were then used for immobilization of lipase from Candida rugosa (CRL). From the study, the highest percentage of lipase im-mobilization was achieved (70.14%), when organo-modified metakaolin (2.0 MK) was used. The supports as well as the immobilized biocatalysts were then characterized by X-ray diffraction, Fourier transform infrared spectrosco-py, scanning electron microscopy, and nitrogen adsorption techniques. Comparisons of the efficiencies of immobi-lized with free CRL in the synthesis of nonyl hexanoate showed that immobilized CRL achieved enzymatic activi-ties of between 5.24×10−3 to 3.63×10−3 mmol/min/mg, while free CRL achieved enzymatic activity of 3.27×10−3 mmol/min/mg after 5 h of reaction at 30 ℃. The immobilized CRLs also maintained 70.81% – 80.59% thermostabil-ities at 70 ℃ as compared to the free CRL (28.13%). CRL immobilized on 2.0 NK and 2.0 MK also maintained 38.54% and 62.56%, respectively, of the initial activities after 10 continuous cycles, showing the excellent stability and reusability of the immobilized lipases, suitable as substitute for expensive, hazardous catalysts used in indus-tries.