Modelling relationship between angiotensin-(I)-converting enzyme inhibition and the bitter taste of peptides

Relationships between angiotensin-(I)-converting enzyme inhibition and the bitter taste of peptides were studied. In cases where ACE inhibition or bitter taste had not been experimentally determined, their activity was estimated using several different peptide quantitative structure–activity relationship (QSAR) models. Significant correlations between increased ACE inhibition and bitterness were found for dipeptides using both observed and QSAR-predicted values. The relationship between ACE inhibition and bitter taste was attributed to the importance of hydrophobicity for both properties. Limited structural variations for dipeptides could make it difficult to have features that limit the effect of C-terminal hydrophobicity, necessary for ACE inhibition, on bitter taste. A similar modelling approach was also done on data from observed bitter oligopeptides derived from milk proteins. The relationship between QSAR-predicted ACE inhibition and observed bitter taste was not as strong as that found for dipeptides. Larger structural variation possibilities for oligopeptides than for dipeptides may thus make it, more feasible to find a highly efficient ACE inhibitory oligopeptide with a negligible bitter taste than a dipeptide.