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Article Abstract
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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC12294777 | PMC |
| http://dx.doi.org/10.3390/foods14142497 | DOI Listing |
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