ArticleFood chemistry: X2024
pH-induced interface protein structure changes to adjust the stability of tilapia protein isolate emulsion prepared by high-pressure homogenization.
Article in Food chemistry: X, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- Protein-lipid interactions in food matrices and their roles in gastrointestinal lipid digestion.Food chemistry: X · 2026Review
- Dextran chain length dictates the interfacial properties of Maillard-conjugated 11S globulin: a molecular mechanism study.Food chemistry: X · 2026Article
- Green Fabrication of Keratin Nanoparticles from Yak Horn by Steam Flash Explosion: Structure-Property Evolution.Biomolecules · 2026Article
- Molecular Interplay Between Plant Proteins and Polyphenols: pH as a Switch for Structural and Functional Assembly.Foods (Basel, Switzerland) · 2025Article
- pH-Dependent Effect of Lecithin on Lupin-Protein-Based Egg Custard Mimics.Journal of food science · 2025Article
- Physical Processing-Assisted pH Shifting for Food Protein Modification: A Comprehensive Review.Foods (Basel, Switzerland) · 2025Review
- Green development of whey protein-based complex system for the intestinal delivery of curcumin: Focus on formation mechanism, stability, andFood chemistry: X · 2025Article
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6 authors.
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Abstract
The pH is a crucial external factor affecting the structure and emulsification characteristics of proteins. The current study aimed to reveal the correlation between the secondary structure changes and tilapia protein isolate (TPI) emulsion stability under different pH (3.0-10.0) prepared by high-pressure homogenization. The results showed that TPI with significantly increased solubility and emulsifying properties when the pH keep away from the isoelectric point (pH 5.0). Meanwhile, TPI emulsions presented significantly enhanced stability (with decreased particle size, increased zeta potential, creaming index close to 0, and uniform dispersion of droplets) at pH 3.0 and 10.0. Interface-adsorbed protein mainly consists of a myosin-heavy chain and actin, and the secondary structure was significantly influenced by pH and high-pressure homogenization. The α-helix will be transformed into β-sheet and β-turn when pH is closer to pH 5.0. However, the high-pressure homogenization induced α-helix conversion to β-sheet. The correlation analysis revealed that emulsion stability is positively correlated with α-helix and negatively correlated with β-sheet. This work provides a deep insight into the correlation between secondary structure changes and the stability of TPI emulsion as affected by pH to offer an alternative way to enhance TPI emulsion stability.
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