Solubilization of leonardite by an extracellular fraction from Coriolus versicolor

Journal Article · Tue Dec 01 00:00:00 EST 1987 · Appl. Environ. Microbiol.; (United States)

OSTI ID:5433813

Pyne, Jr, J W; Stewart, D L; Fredrickson, J; Wilson, B W

Coriolus versicolor has previously been shown to degrade leonardite, an oxidized form of lignite. An extracellular fraction containing protein purified from a C. 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 by A//sub 280/ and the biuret protein assay. Syringaldazine is a substrate of the polyphenol oxidase formed by C. 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/sup 0/C for 30 min significantly reduced both syringaldazine oxidase and leonardite-biosolubilizing activities. Cyanide, azide, and thioglycolate, which are know inhibitors of syringaldazine oxidase activity of C. versicolor, also inhibited leonardite biosolubilization. From these data, we conclude that the purified protein fraction from C. versicolor contains a syringaldazine oxidase activity that participates in leonardite biosolubilization by enzymatic action.

• Research Organization: Pacific Northwest Lab., Richland, WA
• OSTI ID: 5433813
• Journal Information: Appl. Environ. Microbiol.; (United States), Vol. 53:12
• Country of Publication: United States
• Language: English

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