ArticleUltrasonics sonochemistry2021
Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex.
Article in Ultrasonics sonochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed.
- Ultrasound-assisted edible emulsion coatings for postharvest preservation: Cavitation-guided interfacial remodeling, droplet-to-coating translation, and scalable sonoprocessing.Ultrasonics sonochemistry · 2026Article
- Effect of High-Pressure Processing on the Physicochemical and Emulsifying Properties of Pea Protein Isolate.Foods (Basel, Switzerland) · 2026Article
- Exploring the influences of ultrasound-assisted glycosylated modification on chickpea protein isolate: insights into structural, functional, and interfacial properties.Ultrasonics sonochemistry · 2026Article
- Spray Dried Lysozyme Microspheres: Morphological Evolution and Enzymatic Activity Retention.Pharmaceutical research · 2026Article
- Sonication integrated with micronization: structural modification to improve the in-vitro digestibility, functional, and antioxidant properties of red pepper seed protein isolate.Ultrasonics sonochemistry · 2026Article
- Time-Dependent Effects of Ultrasonic Modification of Soy Protein Concentrate on the Mixolab Rheology of Enriched Dough.Foods (Basel, Switzerland) · 2026Article
- Strategies for enhancing protein solubility: methods, applications, and prospects.NPJ science of food · 2026Review
- Effect of vortex fluidic device and its combined treatment with ultrasonication on the conformational changes of soy protein isolate.Ultrasonics sonochemistry · 2025Article
- Comparative Analysis of Structural Characterisation and Gel Properties of Blended/Co-Precipitated Soy-Pea Dual-Protein.Foods (Basel, Switzerland) · 2025Article
- Physical Processing-Assisted pH Shifting for Food Protein Modification: A Comprehensive Review.Foods (Basel, Switzerland) · 2025Review
- Synergistic effects of mannoprotein and ultrasound on the interfacial properties, flavor, and structure of yeast protein.Ultrasonics sonochemistry · 2025Article
- Medium Internal Phase Emulsions Stabilized by Soy Protein Isolates: Protein Solubility Effect and Stabilization Mechanism.Foods (Basel, Switzerland) · 2025Article
- Effects of Ultrasound Treatment on Emulsifying Properties of Pea Protein Isolates Obtained from Four Different Pea Flour Varieties.Foods (Basel, Switzerland) · 2025Article
- Effect of surface dielectric barrier discharge plasma on the physicochemical properties of soy protein isolate-chia seed gum complex.Food chemistry: X · 2025Article
- Modulating the Structural, Thermal and Techno-Functional Properties of Sesame Protein Isolate Using Nonthermal Techniques.Food science & nutrition · 2025Article
- High-intensity ultrasound-assisted extraction for functionalized pistachio meal protein concentrate.Journal of food science · 2025Article
- Soybean isolate protein complexes with different concentrations of inulin by ultrasound treatment: Structural and functional properties.Ultrasonics sonochemistry · 2024Article
- Physicochemical and Functional Properties ofACS omega · 2024Article
- Effects of Pulsed Electric Field on the Physicochemical and Structural Properties of Micellar Casein.Polymers · 2023Article
- Effect of Freezing on Soybean Protein Solution.Foods (Basel, Switzerland) · 2023Article
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Abstract
In this study, a soy protein isolate (SPI)-pectin (PC) complex was prepared, and the effects of different high intensity ultrasound (HIU) powers on the structure and solubility of the complex were studied. Fourier transform infrared (FTIR) spectroscopy analysis exhibited that with increasing HIU power, the α-helix content of the SPI in the complex was significantly reduced, and the random coil content increased; however, an opposite trend appeared after higher power treatments. Fluorescence spectra showed that HIU treatment increased the fluorescence intensity of the complex, and the surface hydrophobicity was increased. The trend of the protein structure studied by Raman spectroscopy was similar to that of FTIR and fluorescence spectroscopy. When the HIU treatment was performed for 15 min and at 450 W power, the particle size of the complex was 451.85 ± 2.17 nm, and the solubility was 89.04 ± 0.19 %, indicating that the HIU treatment caused the spatial conformation of the protein to loosen and improved the functional properties of the complex. Confocal laser scanning microscopy (CLSM) revealed that the complex after HIU treatment exhibited improved dispersibility in water and smaller particle size. Gel electrophoresis results indicated that HIU treatment did not affect the protein subunits of the complex. Therefore, the selection of a suitable HIU treatment power can effectively improve the structural properties and solubility of SPI in the complex, and promote the application of the SPI-PC complex in food processing and industries.
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