ArticleCurrent research in food science2025
Hydrodynamic cavitation induced fabrication of soy protein isolate-polyphenol complexes: Structural and functional properties.
Article in Current research in food science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed.
- Fabrication and characterization of walnut protein-polyphenol conjugates from hickory by-products: Structure and interaction mechanism analysis.Food chemistry: X · 2026Article
- Comparative Effects of Soybean Protein Isolate- and Myofibrillar Protein-Based Curcumin Nanocomplexes on the Freeze-Thaw Stability of Surimi.Journal of food science · 2026Article
- Impact of Grape Seed Extract on Flavor and Functionality of Pea Protein Extrudates and Patties.Journal of food science · 2026Article
- Purification of Protein Glutaminase by Cell Surface Display and Krill Protein Modification via Deamidation.Foods (Basel, Switzerland) · 2026Article
- Green Extraction at Scale: Hydrodynamic Cavitation for Bioactive Recovery and Protein Functionalization-A Narrative Review.Molecules (Basel, Switzerland) · 2026Review
- Stability and functionality of bovine lactoferrin powder after 9 years of storage.Current research in food science · 2025Article
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Abstract
The combination of polyphenols and protein can improve the functional characteristics of protein. How to effectively promote the binding of polyphenols to protein is still a difficult topic. In this study, hydrodynamic cavitation (HC) was used to induce the fabrication of complexes between soy protein isolate (SPI) and different polyphenols (tannic acid (TA), chlorogenic acid (CGA), ferulic acid (FA), caffeic acid (CA), and gallic acid (GA)). The effect of HC on the interaction between polyphenols and SPI was investigated, and the structural and functional properties of the formed complexes were characterized. The results showed that HC treatment led to SPI structure stretching, which increased the binding level of polyphenols, especially that of TA (increased from 35.08 ± 0.73% to 66.42 ± 1.35%). The increase in ultraviolet-visible absorption intensity and quenching of fluorescence intensity confirmed that HC enhanced the interaction between polyphenols and protein. HC treatment reduced the contents of free sulfhydryl and amino groups in SPI-polyphenol complexes and altered their Fourier transform infrared spectroscopy, indicating that HC treatment promoted the formation of C-N and C-S bonds between SPI and polyphenols. Circular dichroism spectroscopy indicated that HC treatment altered the secondary structure of SPI-polyphenol complexes, inducing an increase in α-helix and random coil contents and a decrease in β-sheet content. Regarding functional properties, HC treatment improved the emulsification and antioxidant activity of SPI-polyphenol complexes. Therefore, HC is an effective technique for promoting the binding of polyphenols to protein.
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