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Updated: Dec 8, 2025

HKUST-1 as a Heterogeneous Catalyst for the Synthesis of Vanillin
Published on: July 23, 2016
Vanillyl alcohol oxidase
Tom A Ewing1, Gudrun Gygli2, Marco W Fraaije3
1Wageningen Food & Biobased Research, Wageningen University & Research, Wageningen, The Netherlands.
Abstract:
This review presents a historical outline of the research on vanillyl alcohol oxidase (VAO) from Penicillium simplicissimum, one of the canonical members of the VAO/PCMH flavoprotein family. After describing its discovery and initial biochemical characterization, we discuss the physiological role, substrate scope, and catalytic mechanism of VAO, and review its three-dimensional structure and mechanism of covalent flavinylation. We also explain how protein engineering provided a deeper insight into the role of certain amino acid residues in determining the substrate specificity and enantioselectivity of the enzyme. Finally, we summarize recent computational studies about the migration of substrates and products through the enzyme's structure and the phylogenetic distribution of VAO and related enzymes.
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