Oxidation of milled wood lignin with laccase, tyrosinase and horseradish peroxidase

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Comparison of lignin peroxidase, horseradish peroxidase and laccase in th6 oxidation of methoxybenzenes

Philip J. KERSTEN,* 11 B. KALYANARAMAN,t Kenneth E. HAMMEL,4 Bengt REINHAMMAR§ and T. Kent KIRK*¶ * Forest Products Laboratory, USDA Forest Service, Madison, WI 53705 and Department of Bacteriology, University of Wisconsin, Madison, WI 53706, tNational Biomedical ESR Center, Medical College of Wisconsin, Milwaukee, WI 53226, $Department of Chemistry, SUNY College of Environmental Sciences and F...

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Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes.

Lignin peroxidase oxidizes non-phenolic substrates by one electron to give aryl-cation-radical intermediates, which react further to give a variety of products. The present study investigated the possibility that other peroxidative and oxidative enzymes known to catalyse one-electron oxidations may also oxidize non-phenolics to cation-radical intermediates and that this ability is related to th...

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Oxidation of NAD dimers by horseradish peroxidase.

Horseradish peroxidase catalyses the oxidation of NAD dimers, (NAD)2, to NAD+ in accordance with a reaction that is pH-dependent and requires 1 mol of O2 per 2 mol of (NAD)2. Horseradish peroxidase also catalyses the peroxidation of (NAD)2 to NAD+. In contrast, bacterial NADH peroxidase does not catalyse the peroxidation or the oxidation of (NAD)2. A free-radical mechanism is proposed for both ...

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Mechanism of Oxidation by Horseradish Peroxidase Compound

Binding of p-cresol to native horseradish peroxidase was investigated by differential spectrophotometry, and the value lo3 Kdiss = 3 M was obtained at neutral and acid pH; binding is not competitive with that of cyanide and hydroxide. The Soret region spectrum of Compound II of the enzyme was measured in the steady state at pH 4.26, 6.89, and 10.95, and the differences were found to be too smal...

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Laccase- and peroxidase-free tyrosinase production by isolated microbial strain.

Laccase- and peroxidase-free tyrosinase has commercial importance in the production of L-3, 4-dihydroxyphenylalanine (L-DOPA), which is mainly used in the treatment of Parkinson's disease. In the present study, isolation of an actinomycetes microbial strain capable of producing only tyrosinase is reported. Among all soil isolates, three individual colonies revealed black color around the colony...

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ژورنال

عنوان ژورنال: Applied Microbiology and Biotechnology

سال: 2004

ISSN: 0175-7598,1432-0614

DOI: 10.1007/s00253-004-1800-6