4.7 Article

Label-free quantitative proteomic analysis of milk fat globule membrane proteins in porcine colostrum and mature milk

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FOOD CHEMISTRY
卷 426, 期 -, 页码 -

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ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2023.136447

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Proteomics; Milk fat globule membrane; Porcine colostrum; Porcine mature milk; Kyoto Encyclopedia of Genes and Genomes

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This study used label-free quantitative proteomics to analyze and compare milk fat globule membrane (MFGM) proteins in porcine colostrum and porcine mature milk. A total of 3917 and 3966 MFGM proteins were identified in colostrum and mature milk, respectively. Of these, 3807 proteins were common to both groups, with 303 proteins showing significant differential expression. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analyses revealed the functions and pathways associated with the differentially expressed MFGM proteins. These findings provide crucial insights into the functional diversity of MFGM proteins in porcine milk and offer theoretical guidance for future research and development.
Milk fat globule membrane (MFGM) proteins are nutritional components with various biological functions. This study aimed to analyze and compare MFGM proteins in porcine colostrum (PC) and porcine mature milk (PM), via label-free quantitative proteomics. In total, 3917 and 3966 MFGM proteins were identified in PC and PM milk, respectively. A total of 3807 common MFGM proteins were found in both groups, including 303 significant differentially expressed MFGM proteins. Gene Ontology (GO) analysis revealed that the differentially expressed MFGM proteins were mainly related to the cellular process, cell, and binding. The dominant pathway of the differentially expressed MFGM proteins was related to the phagosome according to Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis. These results reveal crucial insights into the functional diversity of MFGM proteins in porcine milk during lactation and provide theoretical guidance for the development of MFGM proteins in the future.

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