Imobilisasi Lipase pada Kitosan Serbuk dengan Metode Pengikatan Silang dan Uji Aktivitas Transesterifikasinya

Abstract

Immobilization lipase on chitosan powder by cross linking technique has been carried out. The research was purposed to determine the optimum condition of immobilization process and catalytic activities of immobilized lipase. Glutaraldehyde was used as cross linking agent in immobilization lipase on chitosan powder. Immobilization was performed under the optimum conditions such as solubility pH of lipase, degree of deacetylation, mole ratio of chitosan and glutaraldehyde, and concentration of enzyme. Immobilized and free lipases were assayed their activity, thermal stability, reused ability, and kinetic parameters for transesterification reaction of palm oil with methanol. Result of the study showed that the optimum conditions of immobilization were occurred when lipase was dissolved in buffer phosphate at pH 6, mole ratio of chitosan and glutaraldehyde 4:1, and 5% for concentration of enzyme. The immobilized lipase has lower thermal stability but has better affinity and reused stability than the free lipase.