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Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme
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 in...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Pub. Group
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4083428/ https://www.ncbi.nlm.nih.gov/pubmed/24941968 http://dx.doi.org/10.1038/ncomms5037 |
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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 |
author_facet | 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 |
author_sort | Gallage, Nethaji J. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4083428 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Nature Pub. Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-40834282014-07-09 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 Nat Commun Article 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. Nature Pub. Group 2014-06-19 /pmc/articles/PMC4083428/ /pubmed/24941968 http://dx.doi.org/10.1038/ncomms5037 Text en Copyright © 2014, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by-nc-by/3.0/ This work is licensed under a Creative Commons Attribution 3.0 Unported License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Article 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 |
title | Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme |
title_full | Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme |
title_fullStr | Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme |
title_full_unstemmed | Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme |
title_short | Vanillin formation from ferulic acid in Vanilla planifolia is catalysed by a single enzyme |
title_sort | vanillin formation from ferulic acid in vanilla planifolia is catalysed by a single enzyme |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4083428/ https://www.ncbi.nlm.nih.gov/pubmed/24941968 http://dx.doi.org/10.1038/ncomms5037 |
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