Comparative proteomic exploration of whey proteins in human and bovine colostrum and mature milk using iTRAQ-coupled LC-MS/MS

• Published in: International journal of food sciences and nutrition Vol. 68; no. 6; pp. 671 - 681
• Main Authors: Yang, Mei, Cao, Xueyan, Wu, Rina, Liu, Biao, Ye, Wenhui, Yue, Xiqing, Wu, Junrui
• Format: Journal Article
• Language: English
• Published: England Taylor & Francis 01.09.2017; Taylor & Francis Ltd
• Subjects: Animals; Annotations; Biological activity; Biological effects; Bovine milk; Cascades; Cattle; Chromatography, Liquid; Cluster Analysis; Colostrum; Colostrum - chemistry; Cow's milk; Dairy products; Diet; Encyclopedias; Food; Food production; Food science; Gene Ontology; Genomes; human milk; Humans; Infants; lactation phase; Milk; Milk - chemistry; Milk, Human - chemistry; Multivariate statistical analysis; Nutrients; Phagosomes; Principal Component Analysis; Proteins; Proteomics; quantitative proteomics; Statistical analysis; Tandem Mass Spectrometry; Whey; Whey protein; Whey Proteins - chemistry; Whey Proteins - genetics; lactation phase; whey; human milk; Bovine milk; quantitative proteomics
• ISSN: 0963-7486; 1465-3478
• DOI: 10.1080/09637486.2017.1279129

Whey, an essential source of dietary nutrients, is widely used in dairy foods for infants. A total of 584 whey proteins in human and bovine colostrum and mature milk were identified and quantified by the isobaric tag for relative and absolute quantification (iTRAQ) proteomic method. The 424 differentially expressed whey proteins were identified and analyzed according to gene ontology (GO) annotation, Kyoto encyclopedia of genes and genomes (KEGG) pathway, and multivariate statistical analysis. Biological processes principally involved biological regulation and response to stimulus. Major cellular components were extracellular region part and extracellular space. The most prevalent molecular function was protein binding. Twenty immune-related proteins and 13 proteins related to enzyme regulatory activity were differentially expressed in human and bovine milk. Differentially expressed whey proteins participated in many KEGG pathways, including major complement and coagulation cascades and in phagosomes. Whey proteins show obvious differences in expression in human and bovine colostrum and mature milk, with consequences for biological function. The results here increase our understanding of different whey proteomes, which could provide useful information for the development and manufacture of dairy products and nutrient food for infants. The advanced iTRAQ proteomic approach was used to analyze differentially expressed whey proteins in human and bovine colostrum and mature milk.