Uc. Banerjee, CHARACTERIZATION OF RIFAMYCIN OXIDASE IMMOBILIZED ON ALGINATE GEL, Biomaterials, artificial cells, and immobilization biotechnology, 21(5), 1993, pp. 675-683
Rifamycin oxidase of Curvularia luntata was immobilized on alginate ge
l. 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 t
he 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.