BIFIDOGENIC PROPERTIES OF LACTOFERRIN PEPTIDES OF COW MILK

Lactoferrin(LF) has been the focus of intense research lately. Lactoferrin is an 80 kDa iron-binding glycoprotein of the transferrin family that is expressed in most biological fluids and is a major component of the mammalian innate immune system. Cow’s milk whey protein lactoferrin is known as multifunctional protective factor. Lactoferrin possess antimicrobial, antiviral, antioxidant, antineoplastic and anti-inflammatory activity. While being broken down in the gastrointestinal tract, the proteins form peptides that can significantly differ from original polypeptides in physiological properties. Great interest in study of the protective properties of lactoferrin peptides is noticed recently. They appeared to be more active than original native protein. Peptide complex marked as IVLF was isolated from bovine lactoferrin by pepsin hydrolysis. Mass spectrometric researches showed, that the complex consists of 7 peptides with molecular weight less than 3kDa. Their length doesn’t exceed 18 amino acid residues. Animal experimentation shows, that it prevents the formation of chemically induced ulcers in stomach and the development of bowel bacteria overgrowth while using antibiotics. The article studies the influence of the low molecular weight peptide complex obtained by pepsin proteolysis of lactoferrin from cow's milk, on productively significant strains of bifidobacteria, used in dairy industry: Bifidobacterium bifidum and Bifidobacterium аdolescentis. The peptide complex increased the growth of the most bifidobacteria strains in the dose range of 100 to 1000 g/cm3 dose-dependently. There was elucidated the most pronounced growth reaction by strain Bifidobacterium adolescentis B-1.The peptide complex influenced more effective than native lactoferrine at the bifidobacteria growth. The growth activated strain Bifidobacterium аdolescentis B-1 showed antimicrobial activity against pathogenic strain of Escherichia spp.