Evidence map›Paper›PMID 41146685›Full record

ArticleFood chemistry: X2025

Discovery and mechanistic profiling of novel kokumi peptides from Wuding chicken soup.

Chunfang Yang, Yanfei Du, Guiying Wang, Jia Liu, Jiayan Tan, Shuai Tang, Yuan Liu, Hongbin Pan, Guozhou Liao

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Food chemistry: X, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Chunfang YangCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Yanfei DuCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Guiying WangCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Jia LiuCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Jiayan TanCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Shuai TangCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Yuan LiuSchool of Food Science and Engineering, Ningxia University, Yinchuan 750021, China.
Hongbin PanCollege of Animal Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Guozhou LiaoLivestock Product Processing and Engineering Technology Research Center of Yunnan Province, Yunnan Agricultural University, Kunming 650201, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study aims to identify potential kokumi peptides in Wuding chicken soup. To enrich oligopeptides, the preparation process was optimized, and a combined approach using ultrafiltration and gel filtration chromatography was employed for separation and purification. Sensory analysis was then integrated to screen and identify kokumi peptides. And an in-depth study was conducted on the binding mechanism of peptides and calcium-sensing receptors (CaSR). Fifteen kokumi peptides were identified, of which four (LPVPAFN, SAAPAAPVPA, VPAFNVING, and AGFAGDDAPR) were selected for detailed analysis. The primary active sites mediating the interaction between these peptides and the CaSR were identified as Arg 66, Ser 303, Ser 147, Glu 297, and Arg 69, with hydrophobic interactions and hydrogen bonding serving as the predominant binding forces. As the first discovery in Wuding chicken soup, this study establishes a methodological framework for kokumi peptide screening in local chicken varieties and advances structure-activity relationship insights for future applications.

Indexed as

CaSRHydrogen bondingHydrophobic interactionKokumi peptidesWuding chicken

Identifiers

PMID41146685
PMCPMC12554036

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Registered trials

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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.