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A bilirubin oxidase produced by Penicillium sp. strain LAM 91-89 was purified and partially characterized. The enzyme was purified about 70 folds from culture broth by ethanol precipitation, first and second Sephadex G-200 column chromatography with overall yield of 12%. The molecular weight of the enzyme was estimated to be 53,000 dalton by SDS-PAGE. The optimum pH and temperature was 8.5 and 40℃, respectively. The enzyme was stable in the pH range 6∼10 and below 40℃. Activity of the enzyme was increased by Che addition of Mg^(2+) but was gretly inhibited by Ag^(2+), Hg^(2+), Mn^(2+), Pb^(2+), iodoacetate, p-chloromercurobenzoic acid and sodium dodecyl sulfate. Among various substrates, bilirubin was favorably reacted and K_m value for bilirubin was 6.67 μmole.
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