A pancreatic lipase was immobilized on readily available and inexpensive jute and eggshell matrices. The purity of extracted enzyme was confirmed by SDS-PAGE. The maximum protein load for eggshell was 10.23 mg/g, and for jute, it was 5.7 mg/g. The free enzyme activity retention was greater than 80% for eggshell and 43% for jute. The immobilized lipase was stable over a pH range from 7 to 8 for eggshell and 7.5 to 8.5 for jute with over a temperature range from 25 to 45 C for eggshell and 37 to 40 C for the jute. FTIR data indicated new bonds on the jute upon immobilization. Although no new bond was observed, immobilization data on eggshell fit well with the Langmuir adsorption isotherm model. The model constants, Gamma(max) and K-I. were 13.92 mg/g and 0.382 mL/mg, respectively. Mixed adsorption with both ionic and hydrophobic interactions was observed. Lipase adsorption was reduced significantly in presence of Tween 80, whereas the effect was less in case of ionic strength, pH and temperature. For both matrices, scanning electron microscopy (SEM) was used to demonstrate the changes in surface morphology after immobilization. The performance of eggshell was better than that of jute as a matrix for immobilizing pancreatic lipase. (C) 2012 Elsevier Ltd. All rights reserved.