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

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  • Nethaji J. Gallage

    (Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen
    VILLUM Research Center ‘Plant Plasticity’
    Center for Synthetic Biology: ‘bioSYNergy’)

  • Esben H. Hansen

    (Evolva A/S, Lersø Parkallé 42–44)

  • Rubini Kannangara

    (Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen
    VILLUM Research Center ‘Plant Plasticity’
    Center for Synthetic Biology: ‘bioSYNergy’)

  • Carl Erik Olsen

    (Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen
    VILLUM Research Center ‘Plant Plasticity’)

  • Mohammed Saddik Motawia

    (Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen
    VILLUM Research Center ‘Plant Plasticity’
    Center for Synthetic Biology: ‘bioSYNergy’)

  • Kirsten Jørgensen

    (Plant Biochemistry Laboratory, Faculty of Science, University of Copenhagen
    VILLUM Research Center ‘Plant Plasticity’
    Center for Synthetic Biology: ‘bioSYNergy’)

  • 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
    VILLUM Research Center ‘Plant Plasticity’
    Center for Synthetic Biology: ‘bioSYNergy’
    Carlsberg Laboratory, Gamle Carlsberg Vej 10)

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.

Suggested Citation

  • Nethaji J. Gallage & Esben H. Hansen & Rubini Kannangara & Carl Erik Olsen & Mohammed Saddik Motawia & Kirsten Jørgensen & Inger Holme & Kim Hebelstrup & Michel Grisoni & Birger Lindberg Møller, 2014. "Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme," Nature Communications, Nature, vol. 5(1), pages 1-14, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5037
    DOI: 10.1038/ncomms5037
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    Cited by:

    1. Xu, Lingxia & Liaqat, Fakhra & Sun, Jianzhong & Khazi, Mahammed Ilyas & Xie, Rongrong & Zhu, Daochen, 2024. "Advances in the vanillin synthesis and biotransformation: A review," Renewable and Sustainable Energy Reviews, Elsevier, vol. 189(PA).

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