Evaluation of the bitter-masking potential of food proteins for EGCG by a cell-based human bitter taste receptor assay and binding studies

J Agric Food Chem. 2013 Oct 23;61(42):10010-7. doi: 10.1021/jf4030823. Epub 2013 Oct 15.

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. β-Casein, in particular, and several gelatins are known as strong binders of EGCG, contrary to β-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, β-casein showed the strongest effect, with a maximum reduction of hTAS2R39 activation of about 93%. A similar potency was observed for Na-caseinate. β-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. β-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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Caseins / chemistry
  • Caseins / metabolism*
  • Catechin / analogs & derivatives*
  • Catechin / chemistry
  • Catechin / metabolism
  • Female
  • Humans
  • Kinetics
  • Male
  • Protein Binding
  • Receptors, Cell Surface / chemistry
  • Receptors, Cell Surface / metabolism*
  • Taste*

Substances

  • Caseins
  • Receptors, Cell Surface
  • TAS2R39 protein, human
  • Catechin
  • epigallocatechin gallate