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

Nethaji J. Gallage, Esben H. Hansen, Rubini Kannangara, Carl Erik Olsen, Mohammed Saddik Motawia, Kirsten Jørgensen, Inger Holme, Kim Hebelstrup, Michel Grisoni and Birger Lindberg Møller ()
Additional contact information
Nethaji J. Gallage: Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen
Esben H. Hansen: Evolva A/S, Lersø Parkallé 42–44
Rubini Kannangara: Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen
Carl Erik Olsen: Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen
Mohammed Saddik Motawia: Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen
Kirsten Jørgensen: Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen
Inger Holme: AU Flakkebjerg, Danish Centre for Food and Agriculture, University of Aarhus, Forsøgsvej, DK-4200 Slagelse, Denmark
Kim Hebelstrup: AU Flakkebjerg, Danish Centre for Food and Agriculture, University of Aarhus, Forsøgsvej, DK-4200 Slagelse, Denmark
Michel Grisoni: Centre de Coopération Internationale en Recherche Agronomique pour le Dévelopement, UMR PVBMT
Birger Lindberg Møller: Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen

Nature Communications, 2014, vol. 5, issue 1, 1-14

Abstract: Abstract 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.

Date: 2014
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms5037 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5037

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms5037

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().