Soybean isolate protein complexes with different concentrations of inulin by ultrasound treatment: Structural and functional properties

• DOI: 10.1016/j.ultsonch.2024.106864
• Publication Date: 2024-03-30T02:02:52Z
• Authors: Mengmeng Wang; Sai Yang; Na Sun; Tingting Zhu; Ziteng Lian; Shicheng Dai; Jing Xu; Xiaohong Tong; Huan Wang; Lianzhou Jiang
• Keywords: Functional properties; Glycine max; Acoustics. Sound; QC221-246; Inulin; Structure; 04 agricultural and veterinary sciences; Chemistry; Sonication; Soybean protein isolate; Ultrasonic Waves; Ultrasound; Soybean Proteins; Original Research Article; 0405 other agricultural sciences; QD1-999

The effects of ultrasound and different inulin (INU) concentrations (0, 10, 20, 30, 40 mg/mL) on the structural functional properties soybean isolate protein (SPI)-INU complexes were hereby investigated. Fourier transform infrared spectroscopy showed that SPI was bound to INU via hydrogen bonding. All samples a decreasing then increasing trend α-helix content with concentration. SPI-INU by an concentration 20 mg/mL (U-2) had lowest α-helix, highest random coils greatest flexibility, indicating proteins most tightly in U-2. Both UV intrinsic fluorescence indicated it hydrophobic interactions between SPI. addition prevented exposure tryptophan tyrosine residues form more compact tertiary structure compared alone, caused further unfolding This combined effect significantly altered SDS-PAGE Native-PAGE displayed formation through non-covalent INU. ζ-potential particle size U-2 minimized as low −34.94 mV 110 nm, respectively. Additionally, free sulfhydryl groups, solubility, emulsifying foaming improved, best results for U-2, respectively 0.25, 3.51 μmoL/g, 55.51 %, 269.91 25.90 137.66 % 136.33 %. Overall, this work provides theoretical basis improving plant proteins.