Molecular model for astringency produced by polyphenol/protein interactions
Molecular model for astringency produced by polyphenol/protein interactions
复制标题
DOI：
10.1021/bm0345110
复制
发表时间：
2004-05-01
影响因子：
6.2
通讯作者：
Williamson, MP
中科院分区：
文献类型：
--
作者：
Jöbstl, E;O'Connell, J;Williamson, MP
多酚是造成许多饮料和食品涩味的原因。这被认为是由多酚与碱性唾液富含脯氨酸蛋白（PRP）的相互作用引起的。人们普遍认为，涩味的分子来源是多酚结合后PRP的沉淀以及随之而来的口腔粘膜层的变化。在这里，我们使用各种生物物理技术上的一个简单的模型系统，结合β-酪蛋白表没食子儿茶素没食子酸酯（EGCG）。我们发现，在低的EGCG比例，小的可溶性多分散颗粒形成，这agegate形成更大的颗粒作为EGCG的添加。当蛋白质与多酚结合时，蛋白质有一个初始的压实，但随着加入EGCG，由于加入了EGCG，颗粒的尺寸随后增加，然后聚集和沉淀。这些结果表明与已知的食品中的涩味是一致的。
Polyphenols are responsible for the astringency of many beverages and foods. This is thought to be caused by the interaction of polyphenols with basic salivary proline-rich proteins (PRPs). It is widely assumed that the molecular origin of astringency is the precipitation of PRPs following polyphenol binding and the consequent change to the mucous layer in the mouth. Here, we use a variety of biophysical techniques on a simple model system, the binding of beta-casein to epigallocatechin gallate (EGCG). We show that at low EGCG ratios, small soluble polydisperse particles are formed, which agaregate to form larger particles as EGCG is added. There is an initial compaction of the protein as it binds to the polyphenol, but the particle subsequently increases in size as EGCG is added because of the incorporation of EGCG and then to aggregation and precipitation. These results are shown to be compatible with what is known of astringency in foodstuffs.