Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment

Molecules. 2022 Nov 25;27(23):8221. doi: 10.3390/molecules27238221.

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.

Keywords: NaCl concentration; gel properties; protein interaction; rheological properties; soy protein isolates; ultrasound.

MeSH terms

  • Gels / chemistry
  • Hot Temperature*
  • Hydrophobic and Hydrophilic Interactions
  • Osmolar Concentration
  • Sodium Chloride
  • Soybean Proteins* / chemistry
  • Water / chemistry

Substances

  • Soybean Proteins
  • Gels
  • Water
  • Sodium Chloride

Grants and funding

This research was financially supported by the National Natural Science Foundation of China (32202081) and the National Key Research and Development Plan of China (2021YFC2101402). The authors would like to thank Yuqin Jiang for discussions.