The study of the physico-chemical, the biological properties and the peptide composition of the pepsin hydrolysate of cow’s colostrum

Peptides are biologically active substances with different spectrum of action. Studies of the physicochemical properties of pepsin hydrolyzate of cow colostrum have been carried out. The enzymatic digest of bovine colostrum has a high protein content of 9.16 % and a low fat content of 0.25 %. A precipitate of the hydrolyzate was obtained by centrifugation at 3900 rpm for 10 minutes. Two fractions R (1) and R (2) were isolated from the sediment from the pepsin hydrolyzate of cow colostrum on a MALDI-TOF mass spectrometer. It has been established that the peptide chain R (1), consisting of 6 amino acid residues in different sequences, forms a polypeptide of 11 amino acids. Peptide R (2) refers to polypeptides: its chain includes 7 repeating amino acid residues. The molecular weight of the peptide R (1) is 1.7 kDa, the peptide R (2) - 7 kDa. According to the scientific database NCBI, peptide R (1) refers to the little-studied peptide “Nuclear receptor 2C2-associated protein, Bos taurus”, peptide R (2) refers to peptides “14 kDa phosphohistidine phosphatase, Pongo abelii” whose biological functions have not been studied. When studying the cytotoxicity of the isolated peptides in the composition of the bovine colostrum hydrolyzate on HEG 293 cells using the Neutral Red Assay method with a 24-hour incubation, it was found that the cytotoxicity of the studied hydrolyzate at concentrations from 0.1 to 0.5 mg/ml ranges from 0.9 to -6, 30, which indicates its absence. The antimicrobial and antimicrobial activity of cow colostrum hydrolyzate against E. Coli, B. Subtilis and C. Albicans has been proven.