Taste characterization and molecular docking study of novel umami flavor peptides in Yanjin black bone Chicken meat.
Yang. Chaohui C; Ge. Xuehai X; Ge. Changrong C; Zhao. Ping P; Liang. Shuangmin S; Xiao. Zhichao Z
Key Findings
- Five umami‑flavor peptides were isolated from Yanjin black bone chicken meat.
- Two peptides (HE-10 and TP-7) showed the strongest umami taste in sensory tests.
- Molecular docking showed the peptides bind to four key residues (Glu217, Glu148, Asp216, His145) of the T1R1/T1R3 taste receptor via multiple interaction types.
Practical Outcomes
- For biohackers focused on longevity, metabolism, or performance, this research offers no actionable health protocols. The only possible use is for food enthusiasts interested in creating stronger umami flavors in culinary applications.
Summary
The study identified five small proteins from a special chicken that give a strong umami taste. It explains how these peptides interact with taste receptors and form mineral complexes, but it does not discuss any health or performance effects.
Abstract
Five polypeptides with a potential umami taste were isolated and purified from Yanjin black bone chicken. However, the flavor characteristics and umami mechanism have not been clarified. The umami properties of these five peptides were investigated in this work using a range of analytical techniques, computer simulation, and sensory evaluation. HE-10 and TP-7 exhibited the strongest umami flavors. Furthermore, dose-response experiments showed that the umami peptides enhanced umami by generating peptide mineral chelates. Environmental scanning electron microscopy (ESEM) microstructural analyses supported this finding. The molecular docking results indicated that the five polypeptides bind to four critical amino acid residues, namely Glu217, Glu148, Asp216, and His145, of the T1R1/T1R3 receptor. The binding occurred through van der Waals, electrostatic interactions, hydrogen bonding, and hydrophobic interactions. The main surface forces implicated include aromatic interactions, hydrogen bonding, hydrophilicity, and solvent accessibility.
Study Information
pubmed
2024
2024-10-18T00:00:00.000Z
10.1016/j.foodchem.2024.141695
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