Abstract
In this study, experimental samples of extensive enzymatic hydrolysates of bovine colostrum and whey, inclusion complexes of β cyclodextrin with dairy peptides were derived. 1.6 fold increase in the degree of proteolysis was established for whey hydrolysate compared to cleaved first milk. A significant decline in the bitterness of peptide constituents of clathrates was recorded versus samples of initial extensive hydrolysates. The thermogravimetric analysis confirmed the formation of inclusion complexes of cyclic oligosaccharide with dairy peptides. The Ames test demonstrated comparable induced mutation rates for samples of hydrolysates and clathrates. Antimutagenic activity of the samples reached 23.9–28.3 % when tested on strain Salmonella typhimurium TA 98 and 19.4–21.8 % on strain TA 100. According to the impedimetric method, the antibacterial potential of extensive colostrum hydrolysate exceeded the action of cleaved whey against Escherichia coli ATCC 8739 and Staphylococcus aureus ATCC 6538. Enhanced antibacterial activity was found for whey and colostrum peptide fractions included in clathrates with a cyclic oligosaccharide. β cyclodextrin complexing preserved antimutagenic capacity, promoted antibacterial effect, and improved organoleptic properties of milk peptides. These advantages acquire maximum relevance during the clathrate upgrading of specialized nutrition formulas.
Highlights
Enzymatic hydrolysates of dairy proteins are potential sources of biologically active peptides with antioxidant, antimutagenic, hypotensive, antimicrobial, immunomodulatory, and other effects [1-4]
Enhanced antibacterial activity was found for whey and colostrum peptide fractions included in clathrates with a cyclic oligosaccharide. β-cyclodextrin complexing preserved antimutagenic capacity, promoted antibacterial effect, and improved organoleptic properties of milk peptides
It was found that proteolysis degree in samples of extensive whey and first milk hydrolysates reached 37.2 and 22.7 %, while the percentage of a low molecular mass fraction equaled 39.0 and 30.8 %, respectively
Summary
Enzymatic hydrolysates of dairy proteins are potential sources of biologically active peptides with antioxidant, antimutagenic, hypotensive, antimicrobial, immunomodulatory, and other effects [1-4]. Proteolytic enzymes of microbial, animal, and plant origin with diverse mechanisms of catalytic action are used to produce hydrolysates with specified parameters (cleavage degree, molecular mass distribution of peptides, biological activities) [5–8]. Partial hydrolysates of proteins with a medium and profound degree of hydrolysis (extensive hydrolysates) are distinguished. Concentrates of dairy proteins are chosen as the optimal substrates for hydrolysis. Colostrum (first milk) differs significantly from regular milk in nutritional value and composition of biologically active components. Colostrum is characterized by a high content of valuable whey proteins, immune factors, and natural antioxidants, allowing it to refer it to promising hydrolysate sources [16– 20]
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