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Coriolus versicolor has previously been shown to degrade leonardite, an oxidized form of lignite. An extracellular fraction containing protein purified from aC. versicolor culture solubilized leonardite in vitro. Expression of the activity did not require the presence of leonardite and appeared during idiophase. During ion-exchange and gel filtration column chromatography, leonardite-biosolubilizing activity eluted with syringaldazine oxidase activity and with protein, as measured byA 280 and the biuret protein assay. Syringaldazine is a substrate of the polyphenol oxidase formed byC. versicolor . Comparison of leonardite-biosolubilizing activity with the effects of chelators and surface-active agents on leonardite showed that biosolubilization was not due to either surfactant or chelating ability. Heat treatment of the preparation at 60°C for 30 min significantly reduced both syringaldazine oxidase and leonardite-biosolubilizing activities. Cyanide, azide, and thioglycolate, which are known inhibitors of syringaldazine oxidase activity ofC. versicolor , also inhibited leonardite biosolubilization. From these data, we conclude that the purified protein fraction fromC. versicolor contains a syringaldazine oxidase activity that participates in leonardite biosolubilization by enzymatic action.

Solubilization of Leonardite by an Extracellular Fraction from Coriolus versicolor