Abstract
© 2014, Serbian Chemical Society. All rights reserved. In this study, immobilization of lipase from Candida rugosa on mesoporous manganese dioxide by adsorption 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 MnO 2 and lipase-bound MnO 2 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. The 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 (K m and V max ) were also determined for both free and immobilized lipases. It was observed that there is an increase of the K m value (672.96 mg/ml) and a decrease of the V max value (130.99 U/mg) for the immobilized enzyme comparing with the corresponding values of the free lipase.
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CITATION STYLE
Babaei, M., Karimi, A., & Hejazi, M. (2014). Use of mesoporous MnO2 as a support for immobilization of lipase from Candida rugosa. Chemical Industry and Chemical Engineering Quarterly, 20(3), 371–378. https://doi.org/10.2298/ciceq121009019b
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