title: Characterization of soluble rifamycin oxidase from Curvularia lunata var. aeria.
abstract: 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.
authors.affiliation: Biochemical Engineering Research and Process Development Centre, Institute of Microbial Technology, Chandigarh, India.
authors.forename: U C
authors.initials: UC
authors.lastname: Banerjee
mesh_terms: D004795:Enzyme Stability; D006207:Half-Life; D007700:Kinetics; D008670:Metals / Q000494:pharmacology; D003904:Mitosporic Fungi / Q000201:enzymology*; D010088:Oxidoreductases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012995:Solubility
chemical_list: D008670:Metals; D010088:Oxidoreductases; C037364:rifamycin B oxidase