Abstract: In order to clarify the differences in bovine milk fat globular membrane proteins during different lactation periods, milk fat globular membrane proteins in bovine colostrum and mature milk were characterized by quantitative proteomics. The differentially abundant proteins between the two groups were identified and analyzed by bioinformatics. A total of 763 proteins were identified in this study, of which 197 were shared by the two groups. Meanwhile, 80 differentially abundant proteins were further identified, of which, 41 were up-regulated while the rest were down-regulated (bovine colostrum/mature milk). Bioinformatics analysis of the differentially abundant proteins demonstrated that the main cellular components involving these proteins were exosomes, extracellular space, and extracellular regions. The main metabolic pathways involving them were metabolic pathways, purine metabolism, phenylalanine metabolism, tyrosine metabolism, pyruvate metabolism, and glycolysis/gluconeogenesis. Furthermore, 31 key proteins that could interact with other proteins were identified, including haptoglobin and 2-phospho-D-glycerol acid hydrolase. These findings will help to understand the changes of milk protein composition and its functionality during lactation, and lay the foundation for the deep processing of bovine dairy products.

Key words: bovine colostrum; bovine mature milk; milk fat globule membrane proteins; quantitative proteomics