Vanillin Formation from Ferulic Acid in Vanilla Planifolia Is Catalysed by a Single Enzyme
Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme Gallage, Nethaji Janeshawari; Hansen, Esben Halkjær; Kannangara, Rubini Maya; Olsen, Carl Erik; Motawie, Mohammed Saddik; Jørgensen, Kirsten; Holme, Inger; Hebelstrup, Kim; Grisoni, Michel ; Møller, Birger Lindberg Published in: Nature Communications DOI: 10.1038/ncomms5037 Publication date: 2014 Document version Publisher's PDF, also known as Version of record Citation for published version (APA): Gallage, N. J., Hansen, E. H., Kannangara, R. M., Olsen, C. E., Motawie, M. S., Jørgensen, K., Holme, I., Hebelstrup, K., Grisoni, M., & Møller, B. L. (2014). Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme. Nature Communications, 5(6), [4037]. https://doi.org/10.1038/ncomms5037 Download date: 01. okt.. 2021 ARTICLE Received 19 Nov 2013 | Accepted 6 May 2014 | Published 19 Jun 2014 DOI: 10.1038/ncomms5037 OPEN Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme Nethaji J. Gallage1,2,3, Esben H. Hansen4, Rubini Kannangara1,2,3, Carl Erik Olsen1,2, Mohammed Saddik Motawia1,2,3, Kirsten Jørgensen1,2,3, Inger Holme5, Kim Hebelstrup5, Michel Grisoni6 & Birger Lindberg Møller1,2,3,7 Vanillin is a popular and valuable flavour compound. It is the key constituent of the natural vanilla flavour obtained from cured vanilla pods. Here we show that a single hydratase/lyase type enzyme designated vanillin synthase (VpVAN) catalyses direct conversion of ferulic acid and its glucoside into vanillin and its glucoside, respectively. The enzyme shows high sequence similarity to cysteine proteinases and is specific to the substitution pattern at the aromatic ring and does not metabolize caffeic acid and p-coumaric acid as demonstrated by coupled transcription/translation assays.
[Show full text]