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

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Standard

Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme. / Gallage, Nethaji J ; Hansen, Esben H; Kannangara, Rubini; Olsen, Carl Erik; Motawia, Mohammed Saddik; Jørgensen, Kirsten; Holme, Inger; Hebelstrup, Kim; Grisoni, Michel; Møller, Birger Lindberg.

I: Nature Communications, Bind 5, 4037, 19.06.2014, s. 1-14.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Gallage, NJ, Hansen, EH, Kannangara, R, Olsen, CE, Motawia, MS, Jørgensen, K, Holme, I, Hebelstrup, K, Grisoni, M & Møller, BL 2014, 'Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme' Nature Communications, bind 5, 4037, s. 1-14. https://doi.org/10.1038/ncomms5037

APA

Gallage, N. J., Hansen, E. H., Kannangara, R., Olsen, C. E., Motawia, M. S., Jørgensen, K., ... Møller, B. L. (2014). Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme. Nature Communications, 5, 1-14. [4037]. https://doi.org/10.1038/ncomms5037

CBE

Gallage NJ, Hansen EH, Kannangara R, Olsen CE, Motawia MS, Jørgensen K, Holme I, Hebelstrup K, Grisoni M, Møller BL. 2014. Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme. Nature Communications. 5:1-14. https://doi.org/10.1038/ncomms5037

MLA

Vancouver

Gallage NJ, Hansen EH, Kannangara R, Olsen CE, Motawia MS, Jørgensen K o.a. Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme. Nature Communications. 2014 jun 19;5:1-14. 4037. https://doi.org/10.1038/ncomms5037

Author

Gallage, Nethaji J ; Hansen, Esben H ; Kannangara, Rubini ; Olsen, Carl Erik ; Motawia, Mohammed Saddik ; Jørgensen, Kirsten ; Holme, Inger ; Hebelstrup, Kim ; Grisoni, Michel ; Møller, Birger Lindberg. / Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme. I: Nature Communications. 2014 ; Bind 5. s. 1-14.

Bibtex

@article{fb30276c04834772970e25ce46ba0b18,
title = "Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme",
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.",
author = "Gallage, {Nethaji J} and Hansen, {Esben H} and Rubini Kannangara and Olsen, {Carl Erik} and Motawia, {Mohammed Saddik} and Kirsten J{\o}rgensen and Inger Holme and Kim Hebelstrup and Michel Grisoni and M{\o}ller, {Birger Lindberg}",
year = "2014",
month = "6",
day = "19",
doi = "10.1038/ncomms5037",
language = "English",
volume = "5",
pages = "1--14",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme

AU - Gallage, Nethaji J

AU - Hansen, Esben H

AU - Kannangara, Rubini

AU - Olsen, Carl Erik

AU - Motawia, Mohammed Saddik

AU - Jørgensen, Kirsten

AU - Holme, Inger

AU - Hebelstrup, Kim

AU - Grisoni, Michel

AU - Møller, Birger Lindberg

PY - 2014/6/19

Y1 - 2014/6/19

N2 - 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.

AB - 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.

U2 - 10.1038/ncomms5037

DO - 10.1038/ncomms5037

M3 - Journal article

VL - 5

SP - 1

EP - 14

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 4037

ER -