Abstract

This work investigated the effect of treatment of soy protein isolate (SPI) with basic amino acids (BAA) (l-Arginine, l-Histidine, and l-Lysine) at different concentrations prior to spray drying on the beany-flavor and functional properties. The results illustrated that the BAA prominently improved the solubility and emulsifying properties of SPI, and reduced the its release of beany-flavor compounds. Additionally, l-Arginine was more effective in increasing the solubility and emulsifying properties of the SPI than l-Histidine and l-Lysine. Notably, 0.3% l-Arginine improved the solubility, emulsifying activity index, emulsifying stability index of the SPI by 43.5%, 64.2% and 45.3% respectively. Through the headspace solid-phase microextraction gas chromatography-mass spectrometry (HS-SPME-GC-MS) and headspace-gas chromatography-ion mobility spectrometry (HS-GC-IMS), the 0.3% BAA showed the better mitigation effect on the beany flavor of SPI among three addition concentrations. The increased ζ-potential showed that BAA enhanced the electrostatic repulsion of the SPI, facilitating its dissolution and formation of a more stable emulsion system. Surface hydrophobicity and fluorescence spectral results revealed that BAA enhance the exposure of hydrophobic groups, enhancing the stability of oil-water interface and promoting the interaction between beany-flavor compounds and SPI. These findings lay the theoretical groundwork for further research and application of soy protein.

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