High hydrostatic pressure modulation of whey protein-malvidin derivative complexes: Mechanisms, structural changes, and stability.

Youzhi Zhao, Fengxian Qin, Yanzhuo Liu, Naiqun Zhao, Mingjie Hu, Liankui Wen, Xinyao Liu, Zhitong Wang

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Article in Food chemistry: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed

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2 citing papers in PubMed.

Research Progress on Protein-Polyphenol Interaction Mechanisms and Structure-Activity Relationship Modified by Physical Fields.Foods (Basel, Switzerland) · 2026
Review
Effect of high hydrostatic pressure onFrontiers in nutrition · 2026
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8 authors.

Youzhi ZhaoCollege of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China.

Fengxian QinSchool of Life Science, Changchun Sci-Tech University, Changchun, Jilin 130600, China.

Yanzhuo LiuCollege of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China.

Naiqun ZhaoCollege of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China.

Mingjie HuCollege of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China.

Liankui WenCollege of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China.

Xinyao LiuCollege of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China.

Zhitong WangCollege of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study investigated how high hydrostatic pressure (HHP) modulates the structural and functional properties of whey protein isolate (WPI) complexes with Malvidin-3-O-6-[acrylic acid-(2-hydroxy,4-carboxy-cyclohexanol) ester]-guaiacol (MV3ACEC). HHP at 350 MPa maximized the binding ratio (78.41 ± 0.94%) and thermal stability (denaturation temperature: 123.76 °C) of WPI-MV3ACEC, while reducing particle size (237 nm) and enhancing system stability (zeta potential: 12.7 mV). Structural analyses revealed HHP-induced conformational changes in WPI-MV3ACEC, including decreased α-helix and increased β-sheet content. Molecular simulations confirmed optimal binding affinity (-7.8 kcal/mol) at 350 MPa, dominated by van der Waals forces. HHP-treated complexes retained antioxidant activity and improved gastrointestinal stability, with MV3ACEC retention reaching 38.17% ± 0.86% post-intestinal digestion. These findings elucidate the binding mechanisms between WPI and MV3ACEC under HHP, providing novel insights for designing functional dairy products.

Indexed as

High hydrostatic pressureMalvidin derivativeStructural and functional propertiesWhey protein isolate

Identifiers

PMID41674695

DOI10.1016/j.fochx.2026.103596

PMCPMC12887362

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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.