Comparative Study on Milk Fat Globule Membrane Proteomes in Human and Bovine Milk
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Abstract:
Human milk is the sole food source in the initial stage of an infant’s life. Protein is an important nutrient in human milk, and cow’s milk has been widely used in infant formula as a raw material to replace human milk. In this study, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and liquid chromatography-matrix-assisted laser desorption/ionization-time of flight (LC-MALDI-TOF) proteomic methods were used to isolate and identify the milk fat globule membrane proteins (MFGPs) from human and bovine milk, and significant differences between the MFGPs in the two types of milk were found. The results showed that 488 and 1545 different protein species were identified in milk fat globule membranes of bovine and human milk, respectively. Among these proteins, there were 173 unique proteins in bovine milk fat globule membranes, 1230 unique proteins in human milk fat globule membranes, and 315 proteins found in both human and bovine milk. According to gene ontology (GO) annotations, 37% of biological processes involving human MFGPs were metabolic processes, 55% of molecular functions were for combination, and 34% of human MFGPs participated in constituting cell organelles. Twenty-four human MFGPs were involved in the immune related pathways, mainly for antigen processing and presentation. By comparing with bovine milk, studying the composition and functions of human MFGPs can improve our understanding of the proteins present in human milk, and provide a reference for adding functional proteins to infant formula products.
