title: Combinatorial evaluation of laccase-mediator system in the oxidation of veratryl alcohol.
abstract: Laccases play an important role in the biological break down of lignin and have great potential in the deconstruction of lignocellulosic feedstocks. We examined 16 laccases, both commercially prepared and crude extracts, for their ability to oxidize veratryl alcohol in the presence of various solvents and mediators. Screening revealed complete conversion of veratryl alcohol to veratraldehyde catalyzed by a crude preparation of the laccase from Trametes versicolor ATCC 11235 and the mediator TEMPO in 20 % (v/v) tert-butanol.
authors.affiliation: U.S. Department of Agriculture, Renewable Product Technology Research Unit, National Center for Agricultural Utilization Research, Agricultural Research Service, 1815 North University Street, Peoria, IL 61604, USA.
authors.forename: Troy M
authors.initials: TM
authors.lastname: Larson
authors.forename: Amber M
authors.initials: AM
authors.lastname: Anderson
authors.forename: Joseph O
authors.initials: JO
authors.lastname: Rich
mesh_terms: D001547:Benzaldehydes / Q000378:metabolism; D001592:Benzyl Alcohols / Q000378:metabolism*; D042845:Laccase / Q000302:isolation & purification / Q000378:metabolism*; D010084:Oxidation-Reduction; D055454:Trametes / Q000201:enzymology*
chemical_list: D001547:Benzaldehydes; D001592:Benzyl Alcohols; D042845:Laccase; C042197:veratryl alcohol; C427725:veratraldehyde