Project description:Here we studied the glycation of bovine milk proteins by lactose as dominant sugar in milk and hexoses using tandem mass spectrometry (CID and ETD mode). In a bottom-up proteomics approach after enriching glycated peptides by boronate affinity chromatography, first we could identify 260 lactosylated peptides corresponding to 124 lactosylation sites in 28 bovine milk proteins in raw milk, raw colostrum, three brands of pasteurized milk, three brands of UHT milk, and five brands of infant formula. The same regular and additionally two lactose-free milk products (pasteurized and UHT milk) where lactose is enzymatically cleaved into the more reactive hexoses were analyzed in terms of hexosylation sites that resulted in identification of 124 hexosylated tryptic peptides corresponding to 86 glycation sites in 17 bovine milk proteins. In quantitative terms glycation increased from raw milk to pasteurized milk to UHT milk and infant formula, i.e., with the harsher processing conditions. Lactose-free milk contained significantly higher hexosylation degrees than the corresponding regular milk product.
Project description:Pasteurized whole cow milk (Grade A) was purchased from the supermarket. Whole cow milk was centrifuged at 3 000 g at 4°C for 30 min and the fat layer was recovered. The recovered fat was washed with PBS for 20 min at 37°C, and the resuspened mixture was centrifuged again to obtain the milk fat. The wash procedure was repeated three times. Finally, milk fat was washed with MilliQ water to recover the fat globules. Milk fat globules were solubilized with a SDS solution (100 mM Tris-HCl, pH 7.4, 100 mM DTT and 4% SDS) and then incubated in 95°C water bath for 10 min. The mixtures were centrifuged at 14 000 g for 15 min, and the protein samples were collected. S-Trap, FASP, in-gel, and traditional Chl/MeOH, as well as modified chloroform/methanol (Chl/MeOH) or acetone precipitation followed by in-solution digestion without clean-up of tryptic peptides methods were applied to characterization cow MFGM proteome.
Project description:We report the human homologous microRNA profiles in food-grade, bovine-sourced sirloin, heart and adrenal tissue (raw, cooked, and laboratory-prepared pasteurized, freeze-dried extracts)
Project description:We report the human homologous microRNA profiles in food-grade, bovine-sourced sirloin, heart and adrenal tissue (raw, cooked, and laboratory-prepared pasteurized, freeze-dried extracts) Deep miRNA sequencing of sirloin (raw and cooked), heart tissue (raw, cooked, and pastuerized, freeze-dried extracts) and adrenal tissue (raw, cooked, and laboratory-prepared pasteurized, freeze-dried extracts), 3 replicates each process group
