Characterization of rifamycin oxidase immobilized on alginate gel

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 degrees 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.