Evidence map›Paper›PMID 42389335›Full record

ArticleFood chemistry: X2026

High hydrostatic pressure-induced structural remodeling of walnut meal protein and its functional implications: Integrated experimental and molecular dynamics insights.

Weiqian Wang, Guoli Yan, Jianbing Li, Yang Tian, Feng Zhang, Muhammad Aaqil, Yuwei Guo, Jingchuan Zheng, Lijun You, Cunchao Zhao

Abstract read
In one paragraph

Article in Food chemistry: X, 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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1 · What the graph read from it

What it found

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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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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

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4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Weiqian WangCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Guoli YanYunnan Plateau Characteristic Agricultural Industry Research Institute, Yunnan Agricultural University, Kunming 650201, China.
Jianbing LiYunnan Linghe Berry Biological Technology Co., Ltd., Dali 671003, China.
Yang TianCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Feng ZhangCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Muhammad AaqilCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Yuwei GuoCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Jingchuan ZhengCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
Lijun YouSchool of Food Science and Engineering, South China University of Technology, Wushan Road 381, 510640 Guangzhou, Guangdong, China.
Cunchao ZhaoCollege of Food Science and Technology, Yunnan Agricultural University, Kunming 650201, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Walnut meal protein (WMP) represents an underutilized plant protein resource with considerable application potential. However, the molecular basis underlying its structural responsiveness to high hydrostatic pressure (HHP) remains insufficiently elucidated. This study systematically investigated the effects of HHP (100-600 MPa, 5-20 min) on the structural, physicochemical, and functional properties of WMP by integrating spectroscopic analyses with molecular dynamics simulations. HHP markedly reduced solubility (48.4% to 4.6% at 600 MPa, 20 min) while increasing turbidity and particle size, indicating pressure-induced aggregation. Surface hydrophobicity and absolute zeta potential increased, whereas free sulfhydryl content decreased by up to 64.81%, reflecting unfolding followed by intermolecular association. Circular dichroism revealed reduced α-helix content with increased β-sheet and random coil structures, and fluorescence spectroscopy confirmed tertiary structural perturbation and enhanced hydrophobic exposure. These structural transitions significantly improved functional performance, with emulsifying activity index reaching 33.9 m

Indexed as

High hydrostatic pressureMolecular dynamics simulationsProtein aggregationStructure–function relationshipWalnut meal protein

Identifiers

PMID42389335
PMCPMC13319703

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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.