Characterization of the monolignol oxidoreductase AtBBE-like protein 15 L182V for biocatalytic applications

Sabine Pils, Kordula Schnabl, Silvia Wallner, Marko Kljajic, Nina Kupresanin, Rolf Breinbauer, Jörg Schrittwieser, Michael Fuchs, Wolfgang Kroutil, Bastian Daniel*, Peter Macheroux

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Monolignol oxidoreductases from the berberine bridge enzyme-like (BBE-like) protein family (pfam 08031) catalyze the oxidation of monolignols to the corresponding aldehydes. In this report, we explore the potential of a monolignol oxidoreductase from Arabidopsis thaliana (AtBBE-like protein 15) as biocatalyst for oxidative reactions. For this study we employed a variant with enhanced reactivity towards oxygen, which was obtained by a single amino acid exchange (L182V). The pH and temperature optima of the purified AtBBE-like protein 15 L182V were determined as well as the tolerance toward organic co-solvents; furthermore the substrate scope was characterized. The enzyme has a temperature optimum of 50 °C and retains more than 50% activity between pH 5 and pH 10 within 5 min. The enzyme shows increased activity in the presence of various co-solvents (10–50% v/v), including acetonitrile, 2-propanol, 1,4-dioxane, and dimethyl sulfoxide. Primary benzylic and primary or secondary allylic alcohols were accepted as substrates. The enantioselectivity E in the oxidation of secondary alcohols was good to excellent (E>34 to >200).
Original languageEnglish
Pages (from-to)S6-S14
JournalJournal of Molecular Catalysis B
Issue numberSuppl.1
Publication statusPublished - 2016

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