Evidence map›Paper›PMID 42332376›Full record

ArticleJournal of the science of food and agriculture2026

Impact of gamma irradiation on the structural, functional and physicochemical properties of pea protein isolate.

Madina Aitmagambetova, Rong Bai, Jing Xi, Aidana Rakhimova, Wu Ding

Abstract read
In one paragraph

Article in Journal of the science of food and agriculture, 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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0citing papers in PubMed
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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

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Madina Aitmagambetova *College of Food Science and Engineering, Northwest A&F University, Yangling, China.
Rong Bai *College of Food Science and Engineering, Northwest A&F University, Yangling, China.
Jing XiCollege of Food Science and Engineering, Northwest A&F University, Yangling, China.
Aidana RakhimovaCollege of Food Science and Engineering, Northwest A&F University, Yangling, China.
Wu DingCollege of Food Science and Engineering, Northwest A&F University, Yangling, China.

Funding

National Key Research and Development "Fourteenth Five-Year Plan" project number: 2021YFD1600705-04. Key R&D projects number in Shaanxi Province: 2023-YBNY-160. Shaanxi Province Technology Innovation Guidance Special Project number: 2022QFY12-07.
6 · The paper itself

Abstract

backgroundThe properties of pea protein isolate (PPI), comprising a sustainable plant-derived protein for which the full functional potential in complex food matrices remains unrealized as a result of inherent limitations in food applications, are investigated in this work under gamma (γ) irradiation (0-10 kGy). The study used non-thermal physical treatment, namely γ irradiation, using ionizing radiation from a

resultsFourier transform infrared spectroscopy deconvolution revealed irradiation-induced changes: partial unfolding of secondary structures (α-helix/β-sheet), whereas scanning electron microscopy showed fragmented morphology (4-8 kGy) and aggregated clusters. Functional properties peaked at 8 kGy with solubility, emulsifying activity and water/oil-holding capacity, whereas 10 kGy enhanced emulsion stability but reduced solubility because of disulfide cross-linking.

conclusionThis study establishes 8 kGy as the critical threshold for balancing structural flexibility and functionality of PPI, providing a non-thermal strategy for tailoring plant proteins in next-generation foods. Physicochemical studies linked these changes to disulphide bond breaking, free sulfhydryl dynamics and fluorophore exposure. These results highlight γ irradiation as a flexible approach to modify PPI activity, hence balancing structural changes with particular dietary applications. © 2026 Society of Chemical Industry.

Indexed as

Pea ProteinsPisum sativumEmulsionsFood IrradiationGamma RaysProtein Structure, SecondarySolubilitySpectroscopy, Fourier Transform InfraredEmulsionsPea Proteinspea protein isolateprotein modificationprotein propertiesγ irradiation

Identifiers

PMID42332376
PMCPMC13543741

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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.