%A U C Banerjee
%O Copyright of this article belongs to  Wiley/ Blackwell 
%J Letters in applied microbiology
%T Characterization of soluble rifamycin oxidase from Curvularia lunata var. aeria.
%X Curvularia lunata var. aeria was grown on yeast extract, peptone and carboxymethylcellulose (YPC) medium for the production of extracellular rifamycin oxidase. The enzyme was partially purified through a Sephadex G-75 column. The half lives of rifamycin oxidase at 30 degrees and 40 degrees C were 9 d and 100 min, respectively. The activation and deactivation energies of the partially purified enzyme, calculated from Arrhenius plots, were 5.80 and 35.10 kcal mol-1, respectively. The enzyme exhibited a Km (rifamycin B) value of 0.67 mmol l-1 and a Vmax of 11 mumol h-1.ml. Three metal ions, Fe2+, Ag+ and Hg2+, inhibited the enzyme in the 10-20 mmol l-1 metal ion concentration range. Catalytic activity was not affected by the chelating agent, EDTA.
%N 1
%P 1-3
%V 17
%D 1993
%I Wiley/Blackwell Scientific Publications
%L open418