Lignin degradation and detoxification of lignin-derived products. Demethylates eucalyptus hard wood lignin. Has high activity against the non-phenolic heterocyclic compound ABTS, and lower activity against the phenolic substrates syringic acid, caffeic acid, syringaldazine, vanillic acid, catechol and levodihydroxyphenylalanine. 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O Binds 4 Cu cations per monomer. Strongly inhibited by sodium azide, sodium cyanide, Li(+), Sn(+), Hg(2+), and the disulfide-reducing agents beta-mercaptoethanol, dithiothreitol and thioglycolic acid. Moderately inhibited by Mn(2+) and Fe(2+), inhibition by these metal ions is stronger at 0.1 mM than at 1 mM. Moderately inhibited by Cu(2+). Optimum pH is 3.0 with ABTS as substrate, activity decreases sharply as pH increases, and no activity is seen at pH 7.0. Optimum pH is 4.0 with syringic acid as substrate, 5.0 with caffeic acid, syringaldazine, vanillic acid or catechol as substrate, and 6.0 with levodihydroxyphenylalanine as substrate. Inactive after 3 hours incubation at pH 2.0, retains 20% of its activity after 24 hours at pH 3.0 and 90% of its activity after 24 hours at pH 9.0. Optimum temperature is 60 degrees Celsius. Shows 50% of its maximal activity at 20 degrees Celsius. Has a half-life of 53 minutes at 50 degrees Celsius, 23 minutes at 60 degrees Celsius, and less than 2 minutes at 70 degrees Celsius. On the 2D-gel the determined pI of this protein is: 4, its MW is: 64 kDa. Belongs to the multicopper oxidase family.