Structural rearrangement of ethanol-denatured soy proteins by high hydrostatic pressure treatment.

The effects of high hydrostatic pressure (HHP) treatment (100-500 MPa) on solubility and structural properties of ethanol (EtOH)-denatured soy β-conglycinin and glycinin were investigated using differential scanning calorimetry, Fourier transform infrared and ultraviolet spectroscopy. HHP treatment above 200 MPa, especially at neutral and alkaline pH as well as low ionic strength, significantly improved the solubility of denatured soy proteins. Structural rearrangements of denatured β-conglycinin subjected to high pressure were confirmed, as evidenced by the increase in enthalpy value (ΔH) and the formation of the ordered supramolecular structure with stronger intramolecular hydrogen bond. HHP treatment (200-400 MPa) caused an increase in surface hydrophobicity (F(max)) of β-conglycinin, partially attributable to the exposure of the Tyr and Phe residues, whereas higher pressure (500 MPa) induced the decrease in F(max) due to hydrophobic rearrangements. The Trp residues in β-conglycinin gradually transferred into a hydrophobic environment, which might further support the finding of structural rearrangements. In contrast, increasing pressure induced the progressive unfolding of denatured glycinin, accompanied by the movement of the Tyr and Phe residues to the molecular surface of protein. These results suggested that EtOH-denatured β-conglycinin and glycinin were involved in different pathways of structural changes during HHP treatment.