Composite gel based on κ-carrageenan-soybean isolate protein/soy protein fibrils: Focus on structural differences and...

The effects of different concentrations of κ-carrageenan (κC) on the structure and gel properties of soybean protein isolate (SPI) and soybean protein fibrils (SPF) were investigated in this work. The interaction between κC and SPI/SPF was explored by SDS-PAGE, FTIR, fluorescence spectroscopy, surface hydrophobicity (H₀). Results indicated that the binding of κC to SPI and SPF is mainly hydrogen bonding and hydrophobic interactions. With the increase of κC concentration, the fluorescence intensity and H₀ of SPI/SPF-κC decrease. When κC was 8 mg/mL, the H₀ of SPI/SPF-κC decreased by 53.56 % and 57.23 % respectively. The addition of κC increased the particle size and turbidity of SPI, while the opposite results for SPF. The gel properties of SPI/SPF-κC were evaluated by texture, rheology and LF-NMR. The results showed that the gel properties of SPF were better than those of SPI, and the addition of κC significantly increased the G', apparent viscosity and resistance to denaturation of the gel. When κC concentration was 8 mg/mL, the hardness of SPI/SPF-κC was 127.2 ± 5.82 g and 134.23 ± 5.89 g, respectively. In conclusion, the fibrillation of proteins and κC can effectively improve the gel properties of SPI gels, which provides a theoretical basis for expanding the high-value utilization of SPI and SPF.