Abstract
Milk fat globule membrane (MFGM) proteins have been shown to be very sensitive to processing. This study aims to investigate the thermos-stability of human, bovine, and caprine MFGM proteins after pasteurization. The milk fat globule size was determined using confocal laser scanning microscopy. The MFGM proteins were characterized using SDS-PAGE and label-free proteomic techniques. The results indicated that pasteurization didn’t influence the MFGs size distributions in these three species. A total of 1104, 632, and 137 proteins were identified in human, bovine, and caprine MFGM, respectively. The significantly changed proteins after pasteurization were mainly involved in lipid syntheses and secretion as well as immune response. In addition, the changes of these proteins also differed among species, and a higher thermo-sensitivity was observed in human and caprine MFGM proteins than bovine MFGM proteins. In sum, pasteurization affected MFGM protein composition in different extent among three species.
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