Characterization of Mucor miehei lipase immobilized on polysiloxane-polyvinyl alcohol magnetic particles

Mucor miehei lipase was immobilized on magnetic polysiloxane-polyvinyl alcohol particles by covalent binding. The resulting immobilized biocatalyst was recycled by seven assays, with a retained activity around 10% of its initial activity. K-m and V-max were respectively 228.3 muM and 36.1 U mg of protein(-1) for immobilized enzyme. Whereas the optimum temperature remained the same for both soluble and immobilized lipase (45degreesC), there was a shift in pH profiles after immobilization. Optimum pH for the immobilized lipase was 8.0. Immobilized enzyme showed to be more resistant than soluble lipase when assays were performed out of the optimum temperature or pH.