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Immobilization of lipase from Candida rugosa on Eupergit C supports by covalent attachment |
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| Authors: | Zorica Knezevic Nenad Milosavic Dejan Bezbradica Zivana Jakovljevic Radivoje Prodanovic |
| Affiliation: | aDepartment of Biochemical Engineering, Faculty of Technology and Metallurgy, University of Belgrade, Karnegijeva 4, 11001 Belgrade, Serbia and Montenegro bDepartment of Chemistry, IHTM, Studentski trg 12-16, 11001 Belgrade, Serbia and Montenegro cDepartment for Production Engineering, Faculty of Mechanical Engineering, University of Belgrade, Kraljice Marije 16, 11001 Belgrade, Serbia and Montenegro dDepartment of Biochemistry, Faculty of Chemistry, University of Belgrade, Studentski trg 16, 11001 Belgrade, Serbia and Montenegro |
| Abstract: | The present study compares the results of three different covalent immobilization methods employed for immobilization of lipase from Candida rugosa on Eupergit® C supports with respect to enzyme loadings, activities and coupling yields. It seems that method yielding the highest activity retention of 43.3% is based on coupling lipase via its carbohydrate moiety previously modified by periodate oxidation. Study of thermal deactivation kinetics at three temperatures (37, 50 and 75 °C) revealed that the immobilization method also produces an appreciable stabilization of the biocatalyst, changing its thermal deactivation profile. By comparison of the t1/2 values obtained at 75 °C, it can be concluded that the lipase immobilized via carbohydrate moiety was almost 2-fold more stable than conventionally immobilized one and 18-fold than free lipase. The immobilization procedure developed is quite simple, and easily reproduced, and provides a promising solution for application of lipase in aqueous and microaqueous reaction system. |
| Keywords: | Immobilized enzymes Candida rugosa lipase Eupergit Enzyme deactivation Kinetic parameters Microemulsions |
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