Dairy Foods III M125   Isolation of protein fractions of serum of milk by preparative disc-electrophoresis. V. Yukalo*1, O. Tsisaryk2, and K. Datsyshyn1, 1Ternopil Ivan Pul’uj National Technical University, Ternopil, Ukraine, 2Lviv National University of Veterinary Medicine and Biotechnology, Lviv, Ukraine. More than hundreds of different bioactive peptides are located in the primary structure of milk serum proteins. β-Lactoglobulin (β-LG), α-lactalbumin (α-LA), serum albumin (SA), lactoferrin and immunoglobulins belong to the bioactive peptides precursors. For the study and use of bioactive peptides, it is necessary at the first stage to select their homogeneous precursors. The purpose of the study was to isolate homogeneous precursors of bioactive peptides from serum proteins by preparative electrophoresis in a polyacrylamide gel. Homogeneity of protein fractions at different stages of their selection was analyzed by analytical disc-electrophoresis (Davis system) for acidic neutral proteins. The protein concentration was determined by spectrophotometer (SF-46, λ = 280 nm). In this case, previously established absorption coefficients (D1% 1cm) were used: 12.3 for total serum protein, 9.6 for β-LG, 20.9 for α-LA, 6.9 for SA, 9.91 for lactoferrin and 13.6 for immunoglobulins. Homogeneous fractions for identification of milk serum proteins were isolated by double gel-filtration on Sephadex G-100 (fine). Preparative electrophoresis was performed on a modified apparatus of Stadier type. Milk serum was isolated after precipitation of caseins at the isoelectric point. From the 3 variants of the anode electrophoretic systems (discelectrophoresis with sodium dodecyl sulfate, disc-electrophoresis in the native conditions, electrophoresis in the presence of uric acid), disc-electrophoresis in the native conditions was selected due to its efficiency and accessibility. The isolation of homogeneous fractions included preparative disc-electrophoresis, identification of fractions, their extraction and drying. Based on the results of 5 preparative electrophoresis, it was shown that the total protein yield was 67.9% (P < 0.05). Among fractions, the immunoglobulins had the lowest yield (0.9999. The recoveries of various concentration of furosine in different liquid milk samples ranged from 78.4 to 112.6%, with relative standard deviations of 0.1 to 6.7%. Moreover, 34 liquid milk samples were measured for their furosine concentrations. The results (furosine content of 4.0–6.8, 9.1–14.2, and 148.3–197.6 mg/100g protein for raw milk, pasteurized milk, and UHT milk samples, respectively) indicated the furosine amounts increased with increasing heat load applied. Therefore, this simple and quick UPLC method can be used to test furosine concentration in liquid milk. Key Words: furosine, UPLC, liquid milk M149   Intestinal cells exposed to different thermo treated bovine milk exhibited diverse gene expressive pattern. H. Yang1,2, N. Zheng1,2, and J. Wang*1,2, 1State Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing, China, 2Key Laboratory of Quality & Safety Control for Dairy Products of Ministry of Agriculture, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing, China. Consumption of raw milk may pose a health threat due to a possible contamination with certain pathogens. Thermal processing can guarantee microbial safety, but this procedure meanwhile alters the physicochemical property of milk and denatures original bioactive components. To assess whether these changes could lead to diverse functional consequences, 4 types of bovine milk (raw, pasteurized, UHT sterilized, and in-can sterilized) were digested in vitro and then applied to culture human intestinal Caco-2 cells. Subsequent transcriptomic analysis demonstrated that the genome expressive patterns of cells under the condition of raw milk and pasteurised milk were quite similar, definitely distinct from UHT and in-can sterilized group. Compared with raw milk group, 3, 662, and 1,904 differentially expressed genes (DEG, absolute fold change >1.5 and false discovery rate