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