Abstract
Microbial lipase from Mucor miehei and Candida rugosa were immobilized by covalent binding onto magnetized polysiloxane polyvinyl alcohol particles (POS-PVA). The resulting immobilized derivatives were evaluated in aqueous solution (olive oil hydrolysis) and organic solvent (butyl butyrate synthesis). Higher catalytic activities were found when the coupling procedure was made with M. miehei lipase. Immobilized M. miehei lipase also showed a better operational stability and a higher half-life than C. rugosa lipase after the successive batches of esterification. The performance of C. rugosa immobilized derivative was constrained by the low lipase loading used in the immobilizing step. Further information regarding the both immobilized derivatives was also obtained through chemical composition (FTIR).
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