In order to investigate the effect ofleucine residues on the taste ofpeptides, someoligo peptides containing leucine residues were synthesized and their taste was evaluated. The hydrophobicity of leucine residues markedly caused the bitterness of peptides and stronger bitterness was always found when a leucine residue was located at the C-terminus ofpeptides. The possibility of 2 binding sites between the bitter peptides and the bitter taste receptors of the gustation cells was postulated.In recent years, the remarkable progress in protein chemistry has led to advances in food science. Technology for the isolation of flavored peptides from natural sources, and their structural determination and chemical synthesis was very limited in the past but the recent advances in protein chemistry greatly increased its progress. More than one thousand species of flavored peptides have been identified. Their chemical structures, and the properties and intensities of their taste were also determined. Bitter peptide components were isolated from fermented foods, such as ripened cheese, sake, natto and cocoa,1~4) and from enzyme hydrolysates of protein.5~7) Aspartame (Asp-Phe-OMe) was discovered by Mazur et al.8) as a sweetening agent, and a salty peptide (Orn-Tau) was synthesized in the authors' laboratory.9) At present, flavored
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.