Immobilization of proline activated lipase within metal organic framework (MOF)

The immobilization of enzyme with enhanced catalytic activity is the major challenge. In this work, we have activated the lipase in the presence of proline and successfully immobilized into zeolitic imidazolate framework (ZIF)-8 by biomineralization method. The prepared lipase-proline MOF exhibited 135% enhanced catalytic activity as compared to free counterpart. Further, it exhibited four-fold improved thermal stability with respect to native enzyme after immobilization. In Michaelis-Menten kinetic studies, K_m values for lipase-proline MOF were found to be lower, whereas, it exhibited higher V_max than lipase-MOF and free lipase. The lipase-MOF and lipase-proline MOF were showed 56% and 72% residual activity, respectively after six cycles of reuse.