Analysis of Protein Degradation and Umami Peptide Release Patterns in Stewed Chicken Based on Proteomics Combined with Peptidomics Approach

Proteomics combined with peptidomics approaches were used to analyze the protein degradation and the release pattern of umami peptides in stewed chicken. The results showed that a total of 422 proteins were identified, of which 273 proteins consistently existed in samples stewed for 0-5 h. Myosin heavy chain exhibited the highest abundance (26.29-30.26%) throughout the stewing process. The proportion of proteins under 20 kDa increased progressively with the duration of stewing and reached 61% at 4-5 h of stewing. A total of 8018 peptides were detected in the soup samples, and 2323 umami peptides were identified using the prediction platforms iUmami-SCM, UMPred-FRL, Umami_YYDS, and TastePertides-DM. Umami peptides derived from titin (accession number A0A8V0ZZ81) were determined to be the most abundant, accounting for 24% of the total umami peptides, and Val534 and Lys33639 were the key N-terminal and C-terminal amino acids of these umami peptides. Abundance analysis showed that the umami peptides KK16 and SK18 ranked among the top 5 in the samples stewed for 0-5 h, and they were most abundant in the 3 h stewed samples. The results obtained will provide data support for promoting the industrialization of high-quality chicken soup products.