Evidence map›Paper›PMID 41036457›Full record

ArticleFood chemistry: X2025

Plant-derived insoluble protein aggregates: Formation mechanisms, influencing factors, solubilization, functional properties, and applications.

Yanli Ji, Jie Xue, Jiayang Wu, Chenxi Fan, Endian Guo, Hui Yang

Abstract read
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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Editorial Special issue:Food chemistry: X · 2026
    Article
  4. Article
  5. Harnessing theFood chemistry: X · 2026
    Article
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.

Yanli JiFood science college, Shenyang Agricultural University, Shenyang 110866, Liaoning, China.
Jie XueFood science college, Shenyang Agricultural University, Shenyang 110866, Liaoning, China.
Jiayang WuFood science college, Shenyang Agricultural University, Shenyang 110866, Liaoning, China.
Chenxi FanFood science college, Shenyang Agricultural University, Shenyang 110866, Liaoning, China.
Endian GuoFood science college, Shenyang Agricultural University, Shenyang 110866, Liaoning, China.
Hui YangFood science college, Shenyang Agricultural University, Shenyang 110866, Liaoning, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant protein is a high-quality protein resource and has been widely used in various fields of the food industry. However, during food processing, especially thermal processing, enzymatic hydrolysis and enzymatic cross-linking, insoluble protein aggregates are inevitably formed. Hydrogen bonds, hydrophobic interactions and van der Waals forces are the main forces that maintain the structural stability of insoluble protein aggregates, and the structure of insoluble protein aggregates could be changed by physical, chemical and enzymatic hydrolysis treatments to improve their solubility or reduce the degree of formation. At present, due to the insufficient utilization of insoluble protein aggregates, they are often discarded or used as raw material for animal feed, resulting in a large waste of plant protein resources. This paper summarizes the formation mechanism, influencing factors, functional properties and applications of insoluble protein aggregates, which provides a theoretical basis for further research and expansion of insoluble protein aggregates in the food industry.

Indexed as

Formation mechanismInsoluble protein aggregatesPotential applicationProtein solubility

Identifiers

PMID41036457
PMCPMC12483645

What OpenQuestion holds

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LicenceCC BY-NC
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.