ArticleMolecules (Basel, Switzerland)2022
Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment.
Article in Molecules (Basel, Switzerland), 2022. 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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Who cites it
7 citing papers in PubMed.
- Hofmeister effect on the local structure, network mechanics, and water retention of soy protein isolate-tannic acid-κ-carrageenan ternary gels.Food chemistry: X · 2026Article
- Integration of Nonlinear Rheology and CFD Simulation to Elucidate the Influence of Saturated Oil on Soy Protein Concentrate Behavior During High-Moisture Extrusion.Gels (Basel, Switzerland) · 2025Article
- Effect of Extraction Methods and Preheat Treatments on the Functional Properties of Pumpkin Seed Protein Concentrate.ACS food science & technology · 2025Article
- Ultrasonic Treatment of Soybean Protein Isolate: Unveiling the Mechanisms for Gel Functional Improvement and Application in Chiba Tofu.ACS omega · 2024Article
- Binary Pea Protein-Psyllium Hydrogel: Insights into the Influence of pH and Ionic Strength on the Physical Stability and Mechanical Characteristics.Gels (Basel, Switzerland) · 2024Article
- Article
- Dopamine alters phage morphology to exert an anti-infection effect.Frontiers in microbiology · 2023Article
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Authors and funding
8 authors.
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Abstract
This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (p < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (p < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition.
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