4.7 Article

Evaluation of the Bitter-Masking Potential of Food Proteins for EGCG by a Cell-Based Human Bitter Taste Receptor Assay and Binding Studies

期刊

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 61, 期 42, 页码 10010-10017

出版社

AMER CHEMICAL SOC
DOI: 10.1021/jf4030823

关键词

flavonoid-protein interaction; complexation; beta-casein; caseinate; gelatin; EGCG; bitterness; ultrafiltration; sensory; hTAS2R

资金

  1. Food and Nutrition Delta of the Ministry of Economic Affairs, The Netherlands [FND 08018, FND 08019]

向作者/读者索取更多资源

Epigallocatechin gallate (EGCG) has been ascribed to several health benefits, but its bitter taste influences the liking of products with high concentrations of this compound. beta-Casein, in particular, and several gelatins are known as strong binders of EGCG, contrary to beta-lactoglobulin. The current study aimed at relating the EGCG-binding characteristics of those proteins and their food-grade equivalents to their effects on reducing bitter receptor activation by EGCG in vitro and their bitter-masking potential in vivo. Also in the bitter receptor assay, beta-casein showed the strongest effect, with a maximum reduction of hTAS2R39 activation of about 93%. A similar potency was observed for Na-caseinate. beta-Lactoglobulin had little effect on bitter receptor activation, as expected based on its low binding affinity for EGCG. The bitter-masking potential of Na-caseinate was confirmed in vivo using a trained sensory panel. beta-Lactoglobulin also slightly reduced EGCG bitter perception, which could not be directly related to its binding capacity. The bitter receptor assay appeared to be a valid tool to evaluate in vitro the efficacy of food proteins as complexing agents for masking bitterness.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据