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Contribution of Human Oral Cells to Astringency by Binding Salivary Protein/Tannin Complexes

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    Contribution of Human Oral Cells to Astringency by Binding Salivary Protein/Tannin Complexes
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    † REQUIMTE\LAQV, Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade do Porto, Rua do Campo Alegre, 687, 4169-007 Porto, Portugal
    ‡ Grupo de Investigación en Polifenoles. Unidad de Nutrición y Bromatología, Facultad de Farmacia, Universidad de Salamanca, Campus Miguel de Unamuno, E 37007 Salamanca, Spain
    § Parc Tecnològic del Vi, VITEC, Carretera de Porrera, 43730 Falset, Spain
    *E-mail: [email protected]
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    Journal of Agricultural and Food Chemistry

    Cite this: J. Agric. Food Chem. 2016, 64, 41, 7823–7828
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    https://doi.org/10.1021/acs.jafc.6b02659
    Published September 18, 2016
    Copyright © 2016 American Chemical Society
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    Abstract

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    The most widely accepted mechanism to explain astringency is the interaction and precipitation of salivary proteins by food tannins, in particular proline-rich proteins. However, other mechanisms have been arising to explain astringency, such as binding of tannins to oral cells. In this work, an experimental method was adapted to study the possible contribution of both salivary proteins and oral cells to astringency induced by grape seed procyanidin fractions. Overall, in the absence of salivary proteins, the extent of procyanidin complexation with oral cells increased with increasing procyanidin degree of polymerization (mDP). Procyanidin fractions rich in monomers were the ones with the lowest ability to bind to oral cells. In the presence of salivary proteins and for procyanidins with mDP 2 the highest concentrations (1.5 and 2.0 mM) resulted in an increased binding of procyanidins to oral cells. This was even more evident for fractions III and IV at 1.0 mM and upper concentrations. Regarding the salivary proteins affected, it was possible to observe a decrease of P-B peptide and aPRP proteins for fractions II and III. This decrease is greater as the procyanidins’ mDP increases. In fact, for fraction IV an almost total depletion of all salivary proteins was observed. This decrease is due to the formation of insoluble salivary protein/procyanidin complexes. Altogether, these data suggest that some procyanidins are able to bind to oral cells and that the salivary proteins interact with procyanidins forming salivary protein/procyanidin complexes that are also able to link to oral cells. The procyanidins that remain unbound to oral cells are able to bind to salivary proteins forming a large network of salivary protein/procyanidin complexes. Overall, the results presented herein provide one more step to understand food oral astringency onset.

    Copyright © 2016 American Chemical Society

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    This article is cited by 31 publications.

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    Journal of Agricultural and Food Chemistry

    Cite this: J. Agric. Food Chem. 2016, 64, 41, 7823–7828
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.jafc.6b02659
    Published September 18, 2016
    Copyright © 2016 American Chemical Society
    Request reuse permissions

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