Structural and Functional Properties of Soy Protein Isolates Modified by Soy Soluble Polysaccharides.

Aiming to achieve the modification to soy protein isolate (SPI) by soy soluble polysaccharides (SSPS), electrically driven complex systems were first established in the environment of pH 3.0, and then reconstituted SPI particles with different SPI-SSPS ratios were obtained under freeze-drying process. Through this treatment, the structures of SPI particles were partly unfolded and adsorbed SSPS mainly via hydrophobic interactions and hydrogen bonding with larger particle sizes. The adherence of SSPS decreased the surface hydrophobicity of reconstituted SPI particles, but exerted not much influence on the emulsifying and foaming activities and increased the corresponding stabilities due to enhancing the unfolded extent of structure and improving the conformation flexibility. Reconstituted SPI-SSPS particles might rearrange and link each other due to the presence of SSPS on the air-water interface to better stabilize these systems. At SPI-SSPS ratio of 10:1, lower temperature was required to form gels with lower gel intensity and porous structure. The findings provide a further comprehension to the relationship between structures and functional properties of SPI modified by SSPS and the feasibility of applying these reconstituted particles to needed areas.