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Virtual screening and characteristics of novel umami peptides from porcine type I collagen.
- Source :
-
Food Chemistry . Feb2024, Vol. 434, pN.PAG-N.PAG. 1p. - Publication Year :
- 2024
-
Abstract
- • Virtual strategies were integrated for high-throughput screening of umami peptides. • Six novel umami peptides CN, SM, CRD, GESMTDGF, MS and DGC were identified. • CRD, GESMTDGF, DGC had higher umami intensity and obvious umami-enhancing effects. • Umami-tasting mechanism of peptides was partly revealed by docking with T1R1/T1R3. • H-bonds formed by hydrophilic AAs of T1R1/T1R3 play key roles in umami perception. This study aimed to rapidly and precisely discover novel umami peptides from porcine type I collagen using virtual screening, sensory evaluation and molecular docking simulation. Porcine type I collagen was hydrolyzed in silico and six umami peptide candidates (CN, SM, CRD, GESMTDGF, MS, DGC) were shortlisted via umami taste, bioactivity, toxicity, allergenicity, solubility and stability predictions. The sensory evaluation confirmed that these peptides exhibited umami taste, with CRD, GESMTDGF and DGC displaying higher umami intensity and significant umami-enhancing effects in 0.35% sodium glutamate solution. Molecular docking predicted that Ser 276/384/385 of T1R1 and Asn68, Val277, Thr305, Ser306, Leu385 of T1R3 may also play critical roles in binding umami peptides. The umami taste of peptides may be perceived mainly through the formation of hydrogen bonds with the hydrophilic amino acids of T1R1/T1R3. This work provided a robust procedure and guidance to develop novel umami peptides from food byproducts. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 03088146
- Volume :
- 434
- Database :
- Academic Search Index
- Journal :
- Food Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 172848102
- Full Text :
- https://doi.org/10.1016/j.foodchem.2023.137386