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Purification and properties of bilirubin oxidase fromMyrothecium verrucaria

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Bilirubin oxidase was purified from a culture filtrate ofMyrothecium verrucaria Mv 2,1089 by DEAE-cellulose and Sephadex G-100 column chromatographies. The purified enzyme had a specific activity of 30 U/mg protein and showed a single band on polyacrylamide gel electrophoresis.

Some of the general properties of this bilirubin oxidase were as follows: the optimum pH for the enzyme reaction was 7.5 and the optimum temperature was 50°C. The enzyme was stable at pH ranging from 9.0 to 9.5. The mol wt was calculated to be 61,900–62,700 by SDS-PAGE and gel-filtration technique. The apparentK m value of the bilirubin oxidase was calculated to be 9.4x10-5 mol/L. The enzyme activity was greatly reduced by incubation of bilirubin oxidase with Fe2+, Hg+, NaN3, NH+ 4 , and Zn2+. The enzyme reaction was inhibited in the presence of Ca2+, Hg+, Zn2+, Fe2+, and BSA.

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Jian, G., Xl-xian, L., Pei-sheng, M. et al. Purification and properties of bilirubin oxidase fromMyrothecium verrucaria . Appl Biochem Biotechnol 31, 135–143 (1991).

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