Evidence map›Paper›PMID 38005254›Full record

ArticleMolecules (Basel, Switzerland)2023

Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping.

Jianan Zhang, Yang Liu, Liwen Jiang, Tiantian Zhao, Guowan Su, Mouming Zhao

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 29% of its field
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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Review
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

6 authors at 3 institutions in 1 country.

Jianan ZhangSchool of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.ORCID 0000-0001-5820-547X
Yang LiuCollege of Food Science and Technology, Hunan Agricultural University, Changsha 410125, China.
Liwen JiangCollege of Food Science and Technology, Hunan Agricultural University, Changsha 410125, China.
Tiantian ZhaoSericulture & Agri-Food Research Institute, Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, China.ORCID 0000-0003-4092-1261
Guowan SuSchool of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
Mouming ZhaoSchool of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
South China University of Technology · CNHunan Agricultural University · CNGuangdong Academy of Agricultural Sciences · CN

Funding

Foundation of Guangdong Province 2022A1515011543Guangzhou Science and Technology Project 2023A04J0764National Natural Science Foundation of China 32102117the fellowship of China Postdoctoral Science Foundation 2021M691068
6 · The paper itself

Abstract

To enhance the understanding of enzymatic hydrolysis and to accelerate the discovery of key bioactive peptides within enzymatic products, this research focused on elastin as the substrate and investigated the variations in peptide profiles and the production of key bioactive peptides (those exceeding 5% of the total) and their impacts on the biological activity of the hydrolysates. Through the application of advanced analytical techniques, such as stop-flow two-dimensional liquid chromatography and ultra-high-performance liquid chromatography-tandem mass spectrometry, the research tracks the release and profiles of peptides within elastin hydrolysates (EHs). Despite uniform peptide compositions, significant disparities in peptide concentrations were detected across the hydrolysates, hinting at varying levels of bioactive efficacy. A comprehensive identification process pinpointed 403 peptides within the EHs, with 18 peptides surpassing 5% in theoretical maximum content, signaling their crucial role in the hydrolysate's bioactivity. Of particular interest, certain peptides containing sequences of alanine, valine, and glycine were released in higher quantities, suggesting Alcalase

Indexed as

ElastinPeptidesAnimalsCattleHydrolysisPancreatic ElastasePeptide MappingProtein HydrolysatesElastinPancreatic ElastasePeptidesProtein Hydrolysates2D LC-MSelastase inhibitory activityelastin peptidesenzymatic cleavage patternspeptide fingerprinting

Identifiers

PMID38005254
PMCPMC10673124
OpenAlexW4388635130

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.