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

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 5minutes. 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). Graphical abstract
Source: Journal of Molecular Catalysis B: Enzymatic - Category: Biochemistry Source Type: research