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Heating Before or After Complexation Differentially Affects Structural and Functional Properties of Whey Protein
Hesti Ayuningtyas Pangastuti1, Songsak Wattanachaisaereekul2, Supatra Karnjanapratum3,4
1Food Technology Program, Faculty of Industrial Technology, Institut Teknologi Sumatera, Terusan Ryacudu Rd., Way Huwi, South Lampung 35365, Lampung, Indonesia.
Foods (Basel, Switzerland)
|May 27, 2026
Summary
Whey protein isolate (WPI) and gallic acid (GA) complexation is affected by heating sequence and GA concentration. Heat treatments enhance complexation and antioxidant activity but impact foaming and emulsifying properties differently depending on when heat is applied.
Area of Science:
- Food Science
- Protein Chemistry
- Nutraceuticals
Background:
- Whey proteins form complexes with polyphenols, with structure/function influenced by polyphenol concentration and heat.
- Limited data exists on how heat application sequence (pre- vs. post-complexation) interacts with polyphenol concentration.
- Understanding these interactions is crucial for developing functional food ingredients.
Purpose of the Study:
- To investigate the impact of gallic acid (GA) concentration and heat treatment sequence on whey protein isolate (WPI)-GA complex properties.
- To elucidate the structure-function relationships in WPI-GA systems under varying conditions.
Main Methods:
- Prepared WPI-GA complexes at pH 7.0 with GA ratios of 1:0.5 and 1:1 (w/w).
- Applied heat treatment either before or after complexation.
- Analyzed structural properties (turbidity, particle size, zeta potential, fluorescence) and functional properties (antioxidant activity, foaming, emulsification).
Main Results:
- GA addition and heat increased turbidity and particle size, indicating enhanced complexation.
- Higher GA concentration boosted antioxidant activity but reduced foaming capacity.
- Heat treatments influenced foaming and emulsifying properties; preheating decreased foaming, post-heating restored it, and both reduced EAI but increased ESI.
Conclusions:
- GA concentration and heating sequence significantly modulate WPI-GA complexation and functionality.
- Heat treatment sequence plays a critical role in determining the final properties of WPI-GA complexes.
- Findings offer insights for optimizing bioactive-enriched dairy systems through controlled protein-polyphenol interactions.
Keywords:
emulsifying stabilityheating sequenceinterfacial propertiesprotein–polyphenol interactionwhey protein isolateMore Related Videos
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