Effect of Homogenization at a Lower Pressure on Structural and Functional Properties of Soy Protein Isolate

In this paper, the effects of homogenization at low pressure (1~40 MPa) on structural and functional properties of soy protein isolates (SPI) are investigated. Homogenization at low pressure increase solubility, surface hydrophobicity, emulsification activity and foaming capacity of SPIs, these all functional properties increases and then decreases with the homogenization pressure. Whereas, emulsion stability and foaming stability of SPIs treated by homogenization initially decrease and then increase with homogenization pressure. There is a dramatic decrease in hardness, springiness and cohesiveness of homogenized SPI gels. Generally, homogenization at low pressure do not change the subunit composition of SPIs. It is observed that, when the homogenization pressure is lower than 10 MPa than there is no significant impact on structural change. The content of β-sheet decreased, while unordered structure significantly increased, when the homogenization pressure increased from 10 MPa to 20 MPa. Furthermore, the content of β-sheet increases, when the content of the other structures decreases with the increasing homogenization pressure. The maximum emission wavelength (λmax) for SPIs increases with homogenization pressure increases from 10 Mpa to 20 Mpa, which is attributed to the gradual structural unfolding exposing more hydrophobic residues in protein surface. While, the decreased λmax of SPIs treated with 20 Mpa to 40 Mpa homogenization corresponds to the protein aggregation. It can be deduced that appropriate selection of homogenization pressure is important for improving the functional properties of SPIs.