Heating Before or After Complexation Differentially Affects Structural and Functional Properties of Whey Protein Isolate-Gallic Acid Complexes.

Hesti Ayuningtyas Pangastuti, Songsak Wattanachaisaereekul, Supatra Karnjanapratum, Praphan Pinsirodom

Abstract read

In one paragraph

Article in Foods (Basel, Switzerland), 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

–field-weighted citation impact

1 · What the graph read from it

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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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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Hesti Ayuningtyas PangastutiFood Technology Program, Faculty of Industrial Technology, Institut Teknologi Sumatera, Terusan Ryacudu Rd., Way Huwi, South Lampung 35365, Lampung, Indonesia.ORCID 0000-0002-7455-372X

Songsak WattanachaisaereekulSchool of Food Industry, King Mongkut's Institute of Technology Ladkrabang, Chalong Krung Rd., Lat Krabang, Bangkok 10520, Thailand.ORCID 0009-0008-9034-9762

Supatra KarnjanapratumFaculty of Agro-Industry, Chiang Mai University, Chiang Mai 50100, Thailand.ORCID 0000-0002-1349-4033

Praphan PinsirodomSchool of Food Industry, King Mongkut's Institute of Technology Ladkrabang, Chalong Krung Rd., Lat Krabang, Bangkok 10520, Thailand.

Funding

King Mongkut's Institute of Technology Ladkrabang RE-KRIS/FF65/27

6 · The paper itself

Abstract

Whey proteins readily form complexes with polyphenols, the structure and functionality of which are influenced by factors such as polyphenol concentration and heat treatment. However, previous studies have largely examined these factors independently, and limited information is available regarding how the sequence of heat application (pre- vs. post-complexation) interacts with varying polyphenol concentrations to modulate the structure-function relationship of whey protein-polyphenol systems. This study investigated the effects of different heating conditions and gallic acid (GA) concentration on structural and functional properties of whey protein isolate-gallic acid (WPI-GA) complexes at pH 7.0. The treatments included native whey protein isolate (WPI), preheated WPI, native WPI-GA complexes, and WPI-GA complexes at two ratios (1:0.5 and 1:1

Indexed as

emulsifying stabilityheating sequenceinterfacial propertiesprotein–polyphenol interactionwhey protein isolate

Identifiers

PMID42195915

DOI10.3390/foods15101714

PMCPMC13205365

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LicenceCC BY

Read underepoch 390

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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.