Abstract
This paper carried out a comparative analysis of different types of electrophoretic systems which were used for the analysis of casein complex from cow milk (polyacrylamide gel electrophoresis: for the neutral and acidic native conditions, in gradient variant, the presence of sodium dodecyl sulphate or with including urea). Taking into attention the separation efficiency, complexity of electrophoretic system, the impact of system components, we have selected the anode system of the homogeneous gel in the presence of urea as the basis for the preparation of casein fractions. It also changed the composition and the structure of the electrophoretic apparatus. The changes allow purification of casein fractions up to several grams during one stage of treatment (for 5 hours). The purified casein fractions were tested for the homogeneity and have been recommended for using in the biomedical researches, including the processes of the formation of the bioactive peptides.
Highlights
To date, progress has been made in the study of the structure and physicochemical properties of caseins, namely, it found their fractional composition, determined primary structure
We have conducted a comparative study of different anodic electrophoretic polyacrylamide gel systems, which were previously used for the analysis of total casein and its fractions [7] [10] [14]
The results of disc electrophoresis with SDS and disc electrophoresis in gradient polyacrylamide gel (PAGE) showed that these systems are not effective for the separation of the total casein
Summary
Progress has been made in the study of the structure and physicochemical properties of caseins, namely, it found their fractional composition, determined primary structure. Casein can affect on the physiological functions of various body systems of mammalians Such regulation may be realized on the level of some products of the limited proteolysis of caseins during the normal digestion at the influence of the enzymes of the gastrointestinal tract. It established that bioactive peptides can be formed from casein protein in dairy products by the action of proteolytic enzymes of lactic acid bacteria and milk coagulate drugs. These results led to the further development and expansion of ideas about the biological significance of protein in the diet, including natural dietary proteins—caseins, which some authors call pro-hormones of dietary hormones—formones (from food hormones) [4]
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