Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme

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  • Nethaji J Gallage, Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Danmark
  • Esben H Hansen, Evolva A/S, Danmark
  • Rubini Kannangara, Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Danmark
  • Carl Erik Olsen, Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Danmark
  • Mohammed Saddik Motawia, Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Danmark
  • Kirsten Jørgensen, Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Danmark
  • Inger Holme
  • Kim Hebelstrup
  • Michel Grisoni, Centre de Coopération Internationale en Recherche Agronomique pour le Dévelopement, Frankrig
  • Birger Lindberg Møller, Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Danmark
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. VpVAN localizes to the inner part of the vanilla pod and high transcript levels are found in single cells located a few cell layers from the inner epidermis. Transient expression of VpVAN in tobacco and stable expression in barley in combination with the action of endogenous alcohol dehydrogenases and UDP-glucosyltransferases result in vanillyl alcohol glucoside formation from endogenous ferulic acid. A gene encoding an enzyme showing 71% sequence identity to VpVAN was identified in another vanillin-producing plant species Glechoma hederacea and was also shown to be a vanillin synthase as demonstrated by transient expression in tobacco.
OriginalsprogEngelsk
Artikelnummer4037
TidsskriftNature Communications
Vol/bind5
Sider (fra-til)1-14
Antal sider14
ISSN2041-1723
DOI
StatusUdgivet - 19 jun. 2014

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