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Combinatorial evaluation of laccase-mediator system in the oxidation of veratryl alcohol

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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.

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Authors and Affiliations

  1. 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

    Troy M. Larson, Amber M. Anderson & Joseph O. Rich

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  1. Troy M. Larson
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  2. Amber M. Anderson
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  3. Joseph O. Rich
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Correspondence to Joseph O. Rich.

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Names are necessary to report factually on available data; however, the USDA neither guarantees nor warrants the standard of the product, and the use of the name by USDA implies no approval of the product to the exclusion of others that may also be suitable. USDA is an equal opportunity provider and employer.

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Larson, T.M., Anderson, A.M. & Rich, J.O. Combinatorial evaluation of laccase-mediator system in the oxidation of veratryl alcohol. Biotechnol Lett 35, 225–231 (2013). https://doi.org/10.1007/s10529-012-1078-1

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