Structural Assessment and Catalytic Oxidation Activity of Hydrophobized Whey Proteins

Chemical modification of whey proteins allows manipulation of their characteristics, such as surface charge and hydrophobicity. Herein, we report the influence of hydrophobization accomplished by a preacetylation stage and a subsequent combined acetylation-heating process on some characteristics of whey proteins. Hydrophobization extensively (≥90%) acetylated the available free amino groups of whey proteins. The produced protein particles were nanoscaled (75 nm) and had a significantly low isoelectric point (3.70). Hydrophobization increased the β-sheet content of whey proteins and significantly decreased the solvent exposure of tyrosine residues. It also conferred a less compact tertiary structure to the proteins and decreased the extent of disulfide-bond formation by heating. The mobility of α-lactalbumin in nonreducing electrophoresis gel increased as a consequence of hydrophobization. Then, the ability of whey proteins to catalyze hydroquinone autoxidation was examined, and it was found that the activity decreased as a result of hydrophobization. The catalytic activity of the proteins was associated with the free-amino-group content, which determined the extent of cation-π attractive interactions; -potential, which determined the extent of anion-π repulsive interactions; and π-stacking between hydrophobic residues and the electron cloud of the quinone ring.