Chemical characterization of the oligosaccharides in Bactrian camel (Camelus bactrianus) milk and colostrum.

Bactrian camel milk and colostrum are commonly used as foods in Mongolia, whose people believe that these products promote human health. It has been hypothesized that milk oligosaccharides are biologically significant components of human milk, acting as receptor analogs that inhibit the attachment of pathogenic microorganisms to the colonic mucosa, and as prebiotics, which stimulate the growth of bifidobacteria within the infant colon. To evaluate their biological significance, we studied the oligosaccharides present in samples of Bactrian camel milk and colostrum. Using (1)H-nuclear magnetic resonance spectroscopy, we identified and characterized the following oligosaccharides of camel colostrum: Gal(ß1-4)[Fuc(α1-3)]Glc (3-fucosyllactose), Gal(ß1-3)Gal(ß1-4)Glc (3'-galactosyllactose), Gal(ß1-6)Gal(ß1-4)Glc (6'-galactosyllactose), Neu5Ac(α2-3)Gal(ß1-4)Glc (3'-sialyllactose), Neu5Ac(α2-6)Gal(ß1-4)Glc (6'-sialyllactose), Neu5Ac(α2-3)Gal(ß1-3)Gal(ß1-4)Glc (sialyl-3'-galactosyllactose), Neu5Ac(α2-6)Gal(ß1-4)GlcNAc(ß1-3)Gal(ß1-4)Glc (sialyllacto-N-tetraose c), Neu5Ac(α2-3)Gal(ß1-3)[Gal(ß1-4)GlcNAc(ß1-6)]Gal(ß1-4)Glc (sialyllacto-N-novopentaose a), Gal(ß1-3)[Neu5Ac(α2-6)Gal(ß1-4)GlcNAc(ß1-6)]Gal(ß1-4)Glc (sialyllacto-N-novopentaose b); and Neu5Ac(α2-6)Gal(ß1-4)GlcNAc(ß1-3)[Gal(ß1-4)GlcNAc(ß1-6)]Gal(ß1-4)Glc (monosialyllacto-N-neohexaose). The oligosaccharides in the mature camel milk were characterized as 3'-galactosyllactose, Gal(ß1-3)[Gal(ß1-4)GlcNAc(ß1-6)]Gal(ß1-4)Glc (lacto-N-novopentaose I), and 3'-sialyllactose.

Short communication: evidence for the presence of a putative odorant-binding protein in bovine colostrum.

Using a combination of PAGE and mass spectrometry for protein identification, we obtained evidence that a putative odorant-binding protein, designated hypothetical protein LOC517854, occurs in bovine colostrum. This protein, termed as a putative bovine colostral odorant-binding protein (bcOBP), consists of 172 AA residues, including a putative 16-AA signal peptide. The theoretical isoelectric point value and molecular mass of the full-length sequence of bcOBP were calculated to be 4.57 and 19604.18, respectively. The highest sequence similarity (83%) was observed with a potential pheromone transporter, Allergen Bos d 2. An odorant-binding protein derived from bovine nasal mucosa showed relatively low sequence similarity (52%) against bcOBP. Its biological function is unclear, but pheromone transport could be considered. This is the first report of a putative odorant-binding protein in bovine colostrum.