A Novel Enzyme, L-Tryptophan Oxidase, from a Basidiomycete, Coprinus sp. SF-1 : Purificationa and Characterization

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A basidiomycete, Coprinus sp. SF-1,was found to produce an L-Trp-oxidizing enzyme by screening from the culture collection of our laboratory. After solubilization by 1M NaSCN from the particulate fraction of disrupted cells of the strain, the enzyme was purified about 76-fold to essential homogeneity. The enzyme had a molecular mass of about 420 kDa and the subunit molecular mass was 68 kDa. The enzyme contained 1 mol of non-covalently bound FAD per mol of the subunit. It catalyzed the simultaneous reactions of oxidative deamination and oxygenative decarboxylation of L-Trp to form indolepyruvic acid and indole-3-acetamide, the former of which was further oxidized to indole-3-a-cetic acid. The molar ratio of the respective reaction products was about 9 : 1. The enzyme specifically oxidized L-Trp, and slightly acted on L-Phe and L-Tyr. The K_m for L-Trp was about 0.5 mM in both oxidase and oxygenase reactions. Thus, the enzyme is novel one and was tentatively designated "L-Trp oxidase (deaminating and decarboxylating)". The optimum pHs of oxidase and oxygenase activities were 7.0 and 9.0,respectively. The optimum temperatures of both activities were 50℃. The enzyme was stable at pH 6.0-10.5 and below 50℃, and 4℃ for 1 year.
社団法人日本農芸化学会の論文
2000-07-23