S. L Gilani - Faculty of Chemical Engineering, Noshirvani University of Technology, Babol, Iran
G. D. Najafpour - Faculty of Chemical Engineering, Noshirvani University of Technology, Babol, Iran
A. A Moghadamnia - Department of Pharmacology and Physiology, School of Medicine, Babol University of Medical Sciences, Babol, Iran
Azlina Harun Kamaruddin - School of Chemical Engineering, Engineering Campus, Universiti Sains Malaysia, Seri Ampangan, ۱۴۳۰۰ Nibong Tebal, Seberang Prai Selatan, Pulau Pinang, Malaysia

Industrial application of lipase requires efficient methods to immobilize the enzyme, yielding a biocatalyst with high activity and stability compared to free lipase. In the present study, porcine pancreas lipase was immobilized to chitosan beads utilizing its amino group. Lipase was first immobilized to chitosan beads by activating its amino groups with glutaraldehyde. The glutaraldehyde concentrations based on immobilization efficiency of lipase on chitosan bead were optimized. The maximum immobilization efficiency nearly 70% was obtained in value of 3% v/v glutaraldehyde concentration. The optimum pH and temperature of immobilized lipases on chitosan bead and chitosan bead activated by glutaraldehyde were determined as the immobilization efficiency under the variety of pH (50 mM phosphate buffer for pH 6.5–8.5) and temperature (20–40°C). Similar optimum temperature (40°C) was found for both chitosan bead and chitosan bead activated by glutaraldehyde. In compare of chitosan bead, the optimum pH for the immobilized lipase on chitosan bead activated by glutaraldehyde was slightly shifted toward acidic region (6.5).

Porcine Pancreas Lipase, Chitosan Bead, Glutaraldehyde, Immobilization Efficiency