Characterization of a new aryl-alcohol oxidase secreted by the phytopathogenic fungus Ustilago maydis.
2016
M, Couturier | Y, Mathieu | A, Li | D, Navarro | E, Drula | M, Haon | S, Grisel | R, Ludwig | Jg, Berrin | Biodiversité et Biotechnologie Fongiques (BBF) ; Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM) | Universität für Bodenkultur Wien = University of Natural Resources and Life Sciences [Vienne, Autriche] (BOKU) | Architecture et fonction des macromolécules biologiques (AFMB) ; Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS) | FUNLOCK - ANR-13-BIME-0002-01 | European Project: 613549,EC:FP7:KBBE,FP7-KBBE-2013-7-single-stage,INDOX(2013)
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Show more [+] Less [-]English. The discovery of novel fungal lignocellulolytic enzymes is essential to improve the breakdown of plant biomass for the production of second-generation biofuels or biobased materials in green biorefineries. We previously reported that Ustilago maydis grown on maize secreted a diverse set of lignocellulose-acting enzymes including hemicellulases and putative oxidoreductases. One of the most abundant proteins of the secretome was a putative glucose-methanol-choline (GMC) oxidoreductase. The phylogenetic prediction of its function was hampered by the few characterized members within its clade. Therefore, we cloned the gene and produced the recombinant protein to high yield in Pichia pastoris. Functional screening using a library of substrates revealed that this enzyme was able to oxidize several aromatic alcohols. Of the tested aryl-alcohols, the highest oxidation rate was obtained with 4-anisyl alcohol. Oxygen, 1,4-benzoquinone, and 2,6-dichloroindophenol can serve as electron acceptors. This GMC oxidoreductase displays the characteristics of an aryl-alcohol oxidase (E.C.1.1.3.7), which is suggested to act on the lignin fraction in biomass.
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