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

Autor: Harry T. W. M. van der Hijden, Harry Gruppen, Wibke S. U. Roland, Jean-Paul Vincken, Robin J. Gouka, Gerrit Smit, Maxime C. Bohin, Peter J. T. Dekker
Jazyk: angličtina
Rok vydání: 2013
Předmět:
Zdroj: Journal of Agricultural and Food Chemistry 61 (2013) 42
Journal of Agricultural and Food Chemistry, 61(42), 10010-10017
ISSN: 0021-8561
DOI: 10.1021/jf4030823
Popis: 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. ß-Casein, in particular, and several gelatins are known as strong binders of EGCG, contrary to ß-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, ß-casein showed the strongest effect, with a maximum reduction of hTAS2R39 activation of about 93%. A similar potency was observed for Na-caseinate. ß-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. ß-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.
Databáze: OpenAIRE