Vanillate hydroxylase from the white rot basidiomycete Phanerochaete chrysosporium |
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| Authors: | Yasuo Yajima Akio Enoki Mary B. Mayfield Michael H. Gold |
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| Affiliation: | (1) Department of Chemistry and Biochemical Sciences, Oregon Graduate Center, 97005 Beaverton, Oregon, USA |
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| Abstract: | A soluble enzyme fraction from Phanerochaete chrysosporium catalyzed the oxidative decarboxylation of vanillic acid to methoxy-p-hydroquinone. The enzyme, partially purified by ammonium sulfate precipitation, required NADPH and molecular oxygen for activity. NADH was not effective. Optimal activity was displayed between pH 7.5–8.5. Neither EDTA, KCN, NaN3, nor o-phenanthroline (5 mM) were inhibitory. The enzyme was inducible with maximal activity displayed after incubation of previously grown cells with 0.1% vanillate for 30h.Abbreviations MHQ Methoxy-p-hydroquinone - GLC gas liquid chromatography - TMSi trimethylsilane - TLC thin layer chromatography |
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| Keywords: | Basidiomycete Vanillic acid Vanillate hydroxylase Monooxygenase Methoxy-p-hydroquinone Lignin biodegradation Phanerochaete chrysosporium |
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