Extensive enzymatic hydrolysates of bovine colostrum and whey were derived using a highly active serine protease (alcalase), molecular mass distribution of peptides was characterized, and antioxidant properties of hydrolysates were studied. Split protein ratio was shown to increase 1.6 times in whey hydrolysates, whereas mass spectrometry revealed peptides with lower molecular mass in colostrum hydrolysate. The presence of low molecular mass fraction was associated with cleavage of colostrum casein into short chain peptides, compared to whey proteins possessing a tertiary structure responsible for relative resistance to proteolysis. According to fluorimetric studies, hydrolysis with alcalase and subsequent ultrafiltration raised 4.7 and 5.1-fold antioxidant properties of peptide fractions of whey and colostrum, respectively. Application prospects of whey/colostrum hydrolysates as ingredients of specialized formulas of baby, sports and dietetic nutrition have been demonstrated.

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