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In this study, immobilization of lipase from Candida rugosa on mesoporous   manganese dioxide by adsorption method was carried out and the effect of   three immobilization variables including temperature, process time and   enzyme/support ratio on immobilization efficiency were studied. The   characteristics of synthesized MnO2 and lipase-bound MnO2 were investigated   by scanning electron microscopy (SEM), transmission electron microscopy (TEM)   and Fourier Transform Infrared Spectroscopy (FT-IR) methods. The porous   property of the support particles was also studied by X-ray diffraction (XRD)   and Brunauer, Emmett, and Teller (BET) measurements. Thermal stability of   immobilized lipase was determined to be better than that of free enzyme. Also   the operational stability of lipase-bound MnO2 was studied and showed an   almost strong attachment of enzyme to support. The Michaelis-Menten kinetic   parameters (Km and Vmax) were also determined for both free and immobilized   lipases. It was observed that there is an increase of the Km value (672.96   mg/ml) and a decrease of the Vmax value (130.99 U/mg) for the immobilized   enzyme comparing with the corresponding values of the free lipase

Use of mesoporous MnO2 as a support for immobilization of lipase from Candida rugosa