Protein⁻Phenolic Interactions as a Factor Affecting the Physicochemical Properties of White Bean Proteins.

This study was conducted with an aim to determine the interactions of pure phenolic compounds (gallic acid, ferulic acid, chlorogenic acid, quercetin, apigenin, and catechin) and phenolics from plant extracts (green tea and green coffee) with protein fractions of white bean (albumins and globulins). The physicochemical properties of complexes were established through an analysis of the UV-Vis spectrum; relative content of free amino groups, thiol groups, and tryptophan residues; chromatographic (SE-HPLC) and electrophoretic (SD-PAGE, Native-PAGE) properties; and conformational changes reflected by Fourier transform infrared spectra. Further, the effect of pH and ionic strength on the solubility and stability of complexes as well as the binding capacity of phenolics to proteins were determined. Results show that, in most cases, phenolics significantly affected the measured parameters; however, the effects were strongly differentiated by the type of phenolic compounds and protein fraction that were applied. Moreover, it may be that changes in the properties of complexes are reflected in the biological nature of proteins and phenolic compounds such as their bioavailability and physiological activity. However, due to the structural complexity of proteins, and the multitudinous factors that affect their interactions, such studies are a great and long-term challenge for the domain of food science.