Purification, Characterization, and Molecular Cloning of a Pyranose Oxidase from the Fruit Body of the Basidiomycete, Tricholoma matsutake(Biochemistry & Molecular Biology)

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概要

• 論文の詳細を見る

• A new H_2O_2-generating pyranose oxidase was purified as a strong antifungal protein from an arbuscular mycorrhizal fungus, Tricholoma matsutake. The protein showed a molecular mass of 250 kDa in gel filtration, and probably consisted of four identical 62 kDa subunits. The protein contained flavin moiety and it oxidized D-glucose at position C-2. H_2O_2 and D-glucosone produced by the pyranose oxidase reaction showed antifungal activity, suggesting these compounds were the molecular basis of the antifungal property. The V_<max>, K_m, and k_<cat>, for D-glucose were calculated to be 26.6U/mg protein, 1.28 mM, and 111/s, respectively. The enzyme was optimally active at pH 7.5 to 8.0 and at 50℃. The preferred substrate was D-glucose, but 1,5-anhydro-D-glucitol, L-sorbose, and D-xylose were also oxidized at a moderate level. The cDNA encodes a protein consisting of 564 amino acids, showing 35.1% identity to Coriolus versicolor pyranose oxidase. The recombinant protein was used for raising the antibody.

• 社団法人日本農芸化学会の論文
• 2003-12-23

著者

• Kuwata Shigeru

  Plant Breeding and Genetics Research Laboratory, Japan Tobacco Inc.

• Kuwata S

  Department Of Chemistry Faculty Of Science Konan University

• Kuwata Shigeru

  Plant Breeding And Genetics Research Laboratory Japan Tobacco Inc.

• Kuwata Shigeru

  Plant Breeding And Genetics Research Laboratory Japan Tobacco Inc.:(present Address)meiji University

• TAKAKURA Yoshimitsu

  Plant Breeding and Genetics Research Laboratory, Japan Tobacco, Inc.

• Takakura Yoshimitsu

  Plant Breeding And Genetics Research Laboratory Japan Tobacco Inc.:(present Address)plant Innovation

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