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Wine and Grape Tannin Interactions with Salivary Proteins and Their Impact on Astringency: A Review of Current Research
Astringency is an important characteristic of red wine quality. The sensation is generally thought to be produced by the interaction of wine tannins with salivary proteins and the subsequent aggregation and precipitation of protein-tannin complexes. The importance of wine astringency for marketabili...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6259628/ https://www.ncbi.nlm.nih.gov/pubmed/21399572 http://dx.doi.org/10.3390/molecules16032348 |
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author | McRae, Jacqui M. Kennedy, James A. |
author_facet | McRae, Jacqui M. Kennedy, James A. |
author_sort | McRae, Jacqui M. |
collection | PubMed |
description | Astringency is an important characteristic of red wine quality. The sensation is generally thought to be produced by the interaction of wine tannins with salivary proteins and the subsequent aggregation and precipitation of protein-tannin complexes. The importance of wine astringency for marketability has led to a wealth of research on the causes of astringency and how tannins impact the quality of the sensation, particularly with respect to tannin structure. Ultimately, the understanding of how tannin structure impacts astringency will allow the controlled manipulation of tannins via such methods as micro-oxygenation or fining to improve the quality of wines. |
format | Online Article Text |
id | pubmed-6259628 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62596282018-12-07 Wine and Grape Tannin Interactions with Salivary Proteins and Their Impact on Astringency: A Review of Current Research McRae, Jacqui M. Kennedy, James A. Molecules Review Astringency is an important characteristic of red wine quality. The sensation is generally thought to be produced by the interaction of wine tannins with salivary proteins and the subsequent aggregation and precipitation of protein-tannin complexes. The importance of wine astringency for marketability has led to a wealth of research on the causes of astringency and how tannins impact the quality of the sensation, particularly with respect to tannin structure. Ultimately, the understanding of how tannin structure impacts astringency will allow the controlled manipulation of tannins via such methods as micro-oxygenation or fining to improve the quality of wines. MDPI 2011-03-11 /pmc/articles/PMC6259628/ /pubmed/21399572 http://dx.doi.org/10.3390/molecules16032348 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review McRae, Jacqui M. Kennedy, James A. Wine and Grape Tannin Interactions with Salivary Proteins and Their Impact on Astringency: A Review of Current Research |
title | Wine and Grape Tannin Interactions with Salivary Proteins and Their Impact on Astringency: A Review of Current Research |
title_full | Wine and Grape Tannin Interactions with Salivary Proteins and Their Impact on Astringency: A Review of Current Research |
title_fullStr | Wine and Grape Tannin Interactions with Salivary Proteins and Their Impact on Astringency: A Review of Current Research |
title_full_unstemmed | Wine and Grape Tannin Interactions with Salivary Proteins and Their Impact on Astringency: A Review of Current Research |
title_short | Wine and Grape Tannin Interactions with Salivary Proteins and Their Impact on Astringency: A Review of Current Research |
title_sort | wine and grape tannin interactions with salivary proteins and their impact on astringency: a review of current research |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6259628/ https://www.ncbi.nlm.nih.gov/pubmed/21399572 http://dx.doi.org/10.3390/molecules16032348 |
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