Abstract:
A possibility of nanostructuring protein systems is demonstrated based on whey
electroactivation. Whey as a raw material is not only a valuable by-product available in
most of the cheese-production industry areas, it is also relatively cheap, with high
nutritional value and several functionalities, with unique properties, which allows the
study of nano-sized structures of whey proteins. Various non-uniform isolations of protein
fractions in the protein-mineral complexes (PMCs) at the electroactivation of the studied
whey is determined, first of all, by the properties of each fraction separately and by their
behavior at the electrochemical action. The experimental data on the isolation of Beta-
Lactoglobulin (β-Lg), the most abundant whey protein, are presented; the aggregation of
β-Lg in the PMCs via various mechanisms and modes has been presented by the authors
earlier. The isolation of Alpha-Lactalbumin (α-La) in the PMCs upon the electroactivation
of whey differs from the isolation of β-Lg in the PMCs. Electroactivation of whey allowed
the formation of high molecular weight protein compounds. Three fractions of casein: ‒α-
CSN, β CSN, and κ-CSN, with a molecular weight of 37, 33, and 46 kDa, respectively,
were identified. The electroactivation of whey and the extractions in the PMCs ennobled
with certain protein fractions allowed to specify different sedimentation and isolation
mechanisms of the whey proteins: the formation of a calcium phosphate caseinate
complex; salinization of proteins; and sedimentation of proteins in their isoelectric point.