Oxidation of non-phenolic substrates. An expanded role for laccase in lignin biodegradation.
In the presence of substrates such as Remazol Blue and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulphonate) (ABTS), laccases Coriolus (Trametes) versicolor can also oxidize non-phenolic lignin model compounds. Veratryl alcohol (I) and 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)-propane-1,3-diol (III) were oxidized by laccase and mediator to give the alpha-carbonyl derivatives. The beta-1 lignin model dimer, 1-(3,4-dimethoxyphenyl)-2-phenoxy-ethane-1,2-diol (II) was cleaved by laccase in the presence of ABTS to give veratraldehyde and benzaldehyde. On the basis of these observations, we propose that laccase is capable of oxidizing both phenolic and non-phenolic moieties of lignin but that the latter is dependent on the co-presence of primary laccase substrates.
Bourbonnais
R
R
Pulp and Paper Research Institute of Canada, Pointe Claire, Que.
Paice
M G
MG
D001592:Benzyl Alcohols / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D005658:Fungi / Q000201:enzymology; D042845:Laccase; D008031:Lignin / Q000378:metabolism*; D010088:Oxidoreductases / Q000502:physiology*; D010544:Peroxidases / Q000378:metabolism; D010636:Phenols / Q000378:metabolism*; D013379:Substrate Specificity
D001592:Benzyl Alcohols; D010636:Phenols; D008031:Lignin; D010088:Oxidoreductases; D042845:Laccase; D010544:Peroxidases; C042858:lignin peroxidase; C042197:veratryl alcohol