Immobilization of pancreatic lipase on chitin and chitosan

In this study, porcine pancreatic lipase (EC 3.1.1.3)was immobilized on chitin and chitosan by adsorption and subsequent crosslinking with glutaraldehyde, which was added before (conjugation)or after (crosslinking)washing unbound proteins. Conjugation proved to be the better method for both supports. The properties of free and immobilized enzymes were also investigated and compared. The results showed that the pH optimum was shifted from 8.5 to 9.0 for both the immobilized enzymes. Also, the optimum temperature was shifted from 30 to 408C for chitinenzyme and to 458C for chitosan-enzyme conjugates. The immobilization ef?ciency is low, but the immobilized enzymes have good reusability and stability (storage and operational). Besides these properties, the immobilized lipases were also suitable for catalyzing esteri?cation reactions of fatty acids and fatty alcohols, both with a medium chain length. According to our results, esteri?cation activities of immobilized lipases were two- and four-fold higher for chitosan- and chitin-enzyme, than for the free enzyme, respectively. The immobilization procedure shows a great potential for commercial applications of the immobilized lipase, a relatively low cost commercial enzyme.