Analysis of novel umami peptides in Dengchuan beef and their taste mechanism: Integrated peptidomics, machine learning and molecular simulation studies.

Wentao Zheng, Yunmei Chai, Yuzhu Wang, Xue Yang, Jinze He, Qing Li, Guangqiang Wei, Aixiang Huang, Yufang Li

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Article in Current research in food science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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9 authors.

Wentao ZhengCollege of Food Science and Technology, Yunnan Agricultural University, Kunming, Yunnan, 650201, China.

Yunmei ChaiCollege of Food Science and Technology, Yunnan Agricultural University, Kunming, Yunnan, 650201, China.

Yuzhu WangCollege of Food Science and Technology, Yunnan Agricultural University, Kunming, Yunnan, 650201, China.

Xue YangCollege of Food Science and Technology, Yunnan Agricultural University, Kunming, Yunnan, 650201, China.

Jinze HeCollege of Food Science and Technology, Yunnan Agricultural University, Kunming, Yunnan, 650201, China.

Qing LiCollege of Animal Science and Technology, Yunnan Agricultural University, Kunming, Yunnan, 650201, China.

Guangqiang WeiCollege of Food Science and Technology, Yunnan Agricultural University, Kunming, Yunnan, 650201, China.

Aixiang HuangCollege of Food Science and Technology, Yunnan Agricultural University, Kunming, Yunnan, 650201, China.

Yufang LiCollege of Food Science and Technology, Yunnan Agricultural University, Kunming, Yunnan, 650201, China.

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6 · The paper itself

Abstract

This study revealed the umami peptides in Dengchuan beef (DB) and its umami mechanism through peptidomics combined with molecular simulation technology. A total of 4220 peptides were identified by LC-MS/MS, among which five novel umami peptides (ER-10, GK-10, DR-11, EA-11, and HY-12) were screened via virtual screening. Sensory evaluation and electronic tongue analysis confirmed the umami properties of these peptides, with ER-10 and DR-11 exhibiting significant umami-enhancing effects. Molecular simulations revealed that Lys155, Gln52, Ser109, Ser216, Arg255, Ser217 and Met151 were identified as the potential key residues for the stable binding of the five peptides to the T1R1/T1R3 receptor. Among these interactions, hydrogen bonding played a dominant role, followed by hydrophobic and electrostatic interactions. Notably, the residues such as Arg, Phe, Trp and Lys are considered to be key contributors to the umami activity of peptides. This study provides new insights into the structure-activity relationships of meat-derived umami peptides.

Indexed as

Dengchuan beefKey amino acid residuesMolecular simulationTaste characteristicsUmami peptide

Identifiers

PMID42824709

DOI10.1016/j.crfs.2026.101570

PMCPMC13629223

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.