Conformational changes and functional properties of whey protein isolate-polyphenol complexes formed by non-covalent interaction.

The present study was conducted to evaluate the non-ovalent modifications of whey protein isolate (WPI) with gallic acid (GA), chlorogenic acid (CA) and epigallocatechin gallate (EGCG). The structural and functional properties of WPI before and after binding with GA, CA and EGCG were investigated. Results showed that free sulfhydryl groups and surface hydrophobicity significantly decreased in WPI after binding with phenolic compounds. Significant structural alterations in complexes were demonstrated, characterized by a red-shifted maximum emission wavelength in intrinsic fluorescence spectroscopy, and a significant decrease in α-helix and β-sheet and a remarkable increase in β-turn and random coil contents in fourier transform infrared (FTIR) spectroscopy. Moreover, the presence of three polyphenols induced enhanced solubility, foaming and emulsifying capacities of WPI. These findings suggest the feasible application of GA, CA and EGCG to improve the functional properties of WPI and the potential uses of WPI-polyphenol complexes in food industries.