Purification and Properties of Pyranose Oxidase from Coriolus versicolor

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概要

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• Coriolus versicolor KY2912 grown on a medium containing glucose, sucrose or glycerol produced pyranose oxidase. Pyranose oxidase (glucose-2-oxidase) was purified by HPA-75 chromatography, Sepharose 4B and Sephadex G-100 gel filtration, and hydroxyapatite chromatography. The purified enzyme preparation showed a single protein band on acrylamide gel electrophoresis. The highest activity was obtained when D-glucose was employed as substrate and molecular oxygen as electron acceptor. The enzyme was most active at pH 6.2 and 50°C, stable in the pH region between 5.0 and 7.4, and the activity was completely lost above 70°C. The activity was inhibited by Ag+, Cu2+ and PCMB. The enzyme contained FAD covalently bound to the polypeptide chain. The enzyme consisted of identical subunits with a molecular weight of 68, 000, and showed a total molecular weight of 220, 000.

• 社団法人 日本農芸化学会の論文

著者

• Nakanishi Toru

  Tokyo Research Laboratory Kyowa Hakko Kogyo Co. Ltd.

• MACHIDA Yozo

  Tokyo Research Laboratory, Kyowa Hakko Kogyo Co.

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