Bitterness-masking peptides for epigallocatechin gallate identified through peptide array analysis

Abstract

Bitterness-masking agents support the intake of functional food ingredients, which taste bitter. However, evidence-based methodology to find bitterness-masking agents remains to be established. In the present study, focusing on the fact that a bitter tastant-binding compound is expected to have a bitterness-masking effect, several epigallocatechin gallate (EGCg)-binding peptides were identified from the amino acid sequence of ribulose 1,5-bisphosphate carboxylase/oxygenase using peptide array technology. Deletion analysis and alanine scanning analysis of these peptides revealed that electrostatic interaction contribute strongly to the binding mechanism. EGCg-binding peptides identified in this study, namely, MHFRVLAKALR and FTGLKSTSAFPVTRK, successfully suppressed the activation of the bitter-taste receptor hTAS2R39 by administration of EGCg. These results suggest that peptide array technology can be used to screen bitterness-masking peptides.