Evidence map›Paper›PMID 39483023›Full record

ArticleAnimal bioscience2025

Identification of umami peptides and mechanism of the interaction with umami receptors T1R1/T1R3 in pigeon meat.

Yue Zheng, Mengnan Cao, Dengyong Liu

Abstract read
In one paragraph

Article in Animal bioscience, 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.

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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

3 authors.

Yue ZhengCollege of Food Science and Technology, Bohai University, Jinzhou 121013, China.
Mengnan CaoCollege of Food Science and Technology, Bohai University, Jinzhou 121013, China.
Dengyong LiuCollege of Food Science and Technology, Bohai University, Jinzhou 121013, China.

Funding

Bohai University 0522xn05902Science and Technology Poject of Shenyang, Liaoning Povince 22-316-2-03
6 · The paper itself

Abstract

objectivePigeon meat offer an ideal source for extracting fresh flavor peptides. These peptides not only enhance the taste of food but also have potential health benefits, including providing low-sugar, low-sodium, and low-calorie options for individuals with conditions like diabetes, hypertension, and obesity. Therefore, further research into the pigeon industry holds promise for addressing both economic and nutritional needs.

methodsTo explore umami peptides and their molecular binding mechanisms with umami receptor type 1 member 1 in pigeon meat, an enzymatic hydrolysate product is isolated, analyzed, and subjected to sensory evaluation. Fifteen peptides with high freshness characteristics are separated and identified by ultrafiltration, gel separation, reverse performance liquid chromatography, and nano-liquid chromatography-tandem mass spectrometry (nano-LC-MS/MS).

resultsThe molecular docking results show that the amino acid residue Glu128 is a common ligand binding site for all of the fresh-flavored peptides to taste T1R1/T1R3 receptors and it exerts freshness-presenting effects with 15 fresh-flavored peptides through hydrogen bonding, electrostatic interactions, salt bridges, and hydrophobic interactions.

conclusionThis study provides a theoretical basis and technical support for the subsequent development of flavor peptide products in pigeon meat.

Indexed as

Molecular DockingPigeon MeatSeparation and PurificationStructural IdentificationUmami Peptide

Identifiers

PMID39483023
PMCPMC11917414

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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.