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

M.C. Bohin, W.S.U. Roland, H. Gruppen, R.J. Gouka, H.T.W.M. Hijden, P. Dekker, G. Smit, J.P. Vincken

Research output: Contribution to journalArticleAcademicpeer-review

19 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)10010-10017
JournalJournal of Agricultural and Food Chemistry
Volume61
Issue number42
DOIs
Publication statusPublished - 2013

Keywords

  • green tea catechins
  • astringency
  • perception
  • htas2r39

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