OBTAINING AND CHARACTERISTICS OF MANNAN-PEPTIDE NANOHYBRID

Bioactive peptides belong to a new generation of biologically active regulators with a wide range of important physiological effects. This determines the prospects for their use in functional foods as dietary supplements and medicine. The main source of such bioactive peptides is cow's milk. It contains proteins, which include 80% caseins. Like other bioactive compounds, they are exposed to unwanted changes in technological processes and during transit along the gastrointestinal tract. In order to improve their stability and increase bioavailability, conjugates obtained by the Maillard reaction have recently been used. Currently, it is positioned as a promising way to prevent the destructive impact of external factors. This article highlights the results of studies designed to determine the feasibility of casein fragmentation with papain to obtain bioactive peptides and the subsequent creation on their basis of a nanohybrid with a mannan component by the Maillard reaction. Enzymatic hydrolysis of sodium caseinate with papain was carried out with varying the duration of the hydrolysis process (30, 60, 120, 180, 240 min). The yield of protein proteolysis products depending on the duration of the process ranged from 77.8% to 83.9%.Enzymatic hydrolysis of sodium caseinate contributed to a significant increase in the products of its fragmentation mass fraction of amine Nitrogen – from 4561.4 to 5687.5 mg/100 g (4.6–5.7%), which is 3.5–4.4 times more than the content of free amino groups in the original sodium caseinate. Among them, almost 1/2 arebioactive peptidescontaining up to 20 amino acid residues.The mannan-peptide nanohybrid was incubated with biopeptides with modified coffee mannan, which had the ability to dissolve in water.The reaction mixture was exposed to 60 oC for 6 h. The yield of lyophilized product was 38.1%, the mass fraction of mannan reached 10.6-10.9%, and peptides, respectively, – 89.1–89.4%. The protective effect of the polysaccharide component against the peptide component was evaluated in vitro in a pepsin-trypsin system. It was found that the stability of peptides in the nanohybrid is much higher than in the original hydrolyzate. The use of the created nanohybrid is possible both to obtain protective shells of labile biologically active substances and to increase the bioavailability of peptides when they are included in dietary supplements and functional foods.