Characterization of Rifamycin Oxidase Immobilized on Alginate Gel

Abstract

Rifamycin oxidase of Curvularia lunata was immobilized on alginate gel. The pH and temperature optima of the immobilized enzyme preparation were 6.5 and 50°C, respectively. Transformation reaction was carried out with the immobilized enzyme preparation. It took 8 h for the complete transformation of rifamycin B (10 g/L) to rifamycin S. The immobilized enzyme preparation was found to be mechanically weak even in the presence of CaCl₂ in the reaction mixture. Reusability studies showed that the catalyst can not be repeatedly used very effectively.