Related Experiment Video
Updated: Aug 17, 2026
Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Preparation and properties of lipases immobilized on different supports
Ayten Sağiroğlu1, Ali Kilinç, Azmi Telefoncu
1Faculty of Sciences and Letters, Department of Chemistry, Trakya University, Edirne, Turkey.
Abstract:
Porcine pancreatic lipase and Candida cylindracea lipase were immobilized on Celite and Amberlite IRA-938. Activities and stabilities of immobilized lipases were investigated. The immobilized lipase derivatives on Celite exhibited grater residual activity and more resistance to thermal inactivation than their immobilized counterpart on Amberlite IRA-938. The apparent optimum temperatures of the immobilized lipases were 7-10 degrees C higher than that of the free enzymes. The native lipase and lipases immobilized on Celite showed same behaviors of pH dependence. But the pH optimum values for lipases immobilized on Amberlite IRA-938 were shifted to the acidic region relative to that of free enzymes. The stabilities of free and immobilized lipases were also investigated.
