Abstract: The immobilization of pancreatin on Alumina (AL) and on Activated Carbon (AC) at different temperatures and contact time was investigated. The amount of immobilized enzyme was estimated by subtracting the content of protein determined in the supernatant after immobilization from the amount of protein used for immobilization. Therefore, the AC had an immobilization rate of 100% for all parameters tested and the AL was much less efficient showing a maximal immobilization rate of 37% using 90 min at 25°C. The operational stability of pancreatin immobilized on the two supports was evaluated by measuring the residual activity of the enzyme after it has been used for up to 20 times to hydrolyze whey. It was observed that the pancreatin immobilized on activated carbon kept its enzymatic activity unchanged (100%) up to 5 times while on alumina it was up to 2 times.