Abstract:

The structure-activity relationship between peptides and flavor was studied on chicken broth made by the
traditional cooking process. The chicken broth stewed for three hours was fractionated using ultrafiltration membranes
with molecular weight cut-offs of 10, 5 and 3 kD. The peptidomics in the fraction (molecular weight < 3 kD) which had the
strongest umami taste were analyzed by high performance liquid chromatography-mass spectrometry (HPLC-MS). Totally
93 peptides with high proportion of umami and sweet amino acids and low proportion of hydrophobic amino acids were
sequenced. Peptide bonds with hydrophilic amino acids were preferentially cleaved during the heating process. The peptides
were mainly derived from muscle proteins, collagens, enzymes and antibodies.

Key words: chicken broth, peptide, umami, hydrophilic amino acids, hydrophobic amino acids