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

Contribution of Human Oral Cells to Astringency by Binding Salivary Protein/Tannin Complexes.
复制标题

人类口腔细胞通过结合唾液蛋白/单宁复合物对涩味的贡献。

DOI:
10.1021/acs.jafc.6b02659
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发表时间:
2016
影响因子:
6.1
通讯作者:
V. Freitas
V. Freitas
中科院分区:
农林科学1区
文献类型:
--
作者:
Susana Soares;Raúl Ferrer;Elsa Brandão;M. Silva;N. Mateus;V. Freitas

文献摘要

被引文献

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最被广泛接受的解释收敛的机制是食物单宁与唾液蛋白的相互作用和沉淀,特别是富含脯氨酸的蛋白质。然而,已经出现了其他解释收敛的机制,例如单宁与口腔细胞的结合。在这项工作中,采用了一种实验方法来研究唾液蛋白和口腔细胞在葡萄籽原花青素组分诱导收敛中的可能贡献。总体而言,在没有唾液蛋白的情况下,原花青素与口腔细胞的络合程度随着原花青素聚合度(MDP)的增加而增加。富含单体的原花青素部分与口腔细胞的结合能力最低。在唾液蛋白存在的情况下,对于含有MDP 2的原花青素,最高浓度(1.5和2.0 mM)导致原花青素与口腔细胞的结合增加。对于1.0 mM及以上浓度的组分III和IV,这一点更加明显。对于受影响的唾液蛋白,可以观察到组分II和组份III的P-B肽和APRP蛋白的减少。这种下降随着原花青素的MDP的增加而更大。事实上,对于组分IV,观察到几乎完全耗尽了所有唾液蛋白。这种减少是由于形成了不溶性唾液蛋白/原花青素复合体。总之,这些数据表明,一些原花青素能够与口腔细胞结合,唾液蛋白与原花青素相互作用,形成唾液蛋白/原花青素复合体,该复合体也能够与口腔细胞相连。未与口腔细胞结合的原花青素能够与唾液蛋白结合,形成唾液蛋白/原花青素复合体的大型网络。总体而言,本文提出的结果为了解食物口腔收敛的开始提供了更多的步骤。
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.