Abstract
Fractional specificity of biological action and ability to form bioactive peptides, which have a positive effect on different physiological systems of the body in the processes of proteolysis and digestion, are characteristic for whey proteins. Prospects for the production and application of whey protein fractions are related to the necessity of their composition control. The comparative analysis of the electrophoretic systems previously used for the milk protein analysis was carried out for the creation of an express analysis method of whey protein fractions. These are the anode disc electrophoresis system in the presence of sodium dodecyl sulfate, the Davis disc electrophoresis system for acidic proteins in native conditions, the system in a homogeneous polyacrylamide gel with urea. The Davis disc electrophoresis system for acidic proteins was chosen as the basis. For the adaptation of this system to the requirements of express analysis, the stacking polyacrylamide gel was removed from its composition and the concentration of the separating gel was reduced. The difference in the composition of electrode buffer and gel buffer ions was used to provide the high separation efficiency of protein fractions. This allows saving the effect of protein concentration in the whey sample on the first stages of electrophoresis. The position of the basic whey protein fractions on electrophoregrams was established with the help of homogeneous marker proteins (β-lactoglobulin and whey albumin). Аn accessible electrophoresis system in the slabs of a homogeneous polyacrylamide gel for serial express analysis of the fractional composition of whey proteins has been proposed as a result of researches. The system allows reliable identification of four protein fractions (α-LA, β-LG, BSA and IG). Close average values and standard deviations of the content of these fractions in 15 whey samples of one milk batch, obtained by the densitometry of three electrophoregrams: β-LG (37.3±4.2, 36.5±2.8; 38.3±2.7), α-LA (15.8±1.5, 15.8±1.3, 16.4±1.1), BSA (8.2±1.1, 8.0±1.0, 9.4±1.1), IG (17.6±1.9, 17.4±1.5, 16.8±1.5) testify about good reproducibility of the method. The proposed method may be useful for the express identification of the basic whey protein fractions, which are precursors of biologically active peptides.
Highlights
Whey proteins are one of the two basic milk protein fractions
The International Committee on the nomenclature and methodology of milk proteins recommends the use of a one-dimensional anode disc electrophoresis system with sodium dodecyl sulfate for the analysis of whey proteins [5]
Davis disc electrophoresis system in native conditions for acidic and neutral proteins [15], analytical and express variants of the homogeneous polyacrylamide gel (PAG) electrophoretic system with urea for the analysis of casein complex proteins [15, 16] were used for selecting the electrophoretic system for whey protein express analysis
Summary
Whey proteins are one of the two basic milk protein fractions. They comprise about 20 % of all milk proteins and are valuable by their amino acid composition. The discovery, in recent decades, of bioactive peptides with a wide range of biological effects in the composition of basic whey proteins provides new opportunities for the processing of whey proteins. This may be the creation of valuable natural functional ingredients based on biologically active peptides [2]. Peptides with a certain biological activity are isolated from different fractions [3] In this regard, the task emerged to develop industrial methods for obtaining separate milk whey protein fractions, which are precursors of bioactive peptides. Such a method may be important in establishing the authenticity of the composition of whey-containing protein products
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