Effect of Secondary Structure determined by FTIR Spectra on Surface Hydrophobicity of Soybean Protein Isolate

Abstract

The Fourier transform infrared spectroscopy (FTIR) was employed to study the relationship between secondary structure and surface hydrophobicity in different sorts of soy protein isolate. The results show that the surface hydrophobicity increases with the decrease of α-helix content, and decreases with the increase of β-sheet and random coil content. There is no significant relationship between β-turn and the surface hydrophobicity.