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Characterization of soluble rifamycin oxidase from Curvularia lunata var. aeria
Author(s) -
Banerjee U. C.
Publication year - 1993
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1993.tb01421.x
Subject(s) - rifamycin , sephadex , enzyme , oxidase test , metal ions in aqueous solution , enzyme assay , nuclear chemistry , yeast extract , chemistry , chromatography , metal , biology , biochemistry , fermentation , organic chemistry , antibiotics
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° and 40°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 K m (rifamycin B) value of 0.67 mmol l ‐1 and a V max of 11 μmol h ‐1 ml. Three metal ions, Fe 2+ , Ag + and Hg 2+ , inhibited the enzyme in the 10–20 mmol l ‐1 metal ion concentration range. Catalytic activity was not affected by the chelating agent, EDTA.