China is blessed with minor species milk resources. Minor species milks from different sources have their own distinctive characteristics in terms of nutrient composition and content as well as functional activity. Oligosaccharides, as important bioactive ingredients in milk, have many significant biological functions. With the aim of providing theoretical reference for the development and utilization of oligosaccharides in minor species milk, this paper reviews recent progress in the research on the types, structures and contents of oligosaccharides in goat milk, donkey milk, buffalo milk, camel milk and horse milk, and it also summarizes the bioactive functions of milk oligosaccharides such as probiotic, antibacterial and anti-inflammatory properties as well as promoting brain development.

Bovine milk contains 2%–5% lipids, secreted by breast epithelial cells and dispersed in the milk in the form of milk fat globules. Most of the milk fat (about 98%) exists in the milk fat globules in the form of glycerolipids, and the rest (about 2%) is polar lipids, including glycerophospholipids, sphingolipids, glycolipids, mainly distributed in the milk fat globule membrane surface. Despite their relative scarcity, milk polar lipids play an indispensable role in the growth and development of mammals. This review introduces readers to the types of polar lipids in milk, and compares the types and quantities of milk polar lipids from different milk sources including cows, buffalo, yak, sheep, goats, donkeys, camels, and humans. Next, this review summarizes the physiological functions of milk polar lipids including inhibition of neutral fat absorption, regulation of intestinal microbial community composition, prevention of cardiovascular disease, prevention of non-alcoholic fatty liver, promotion of cognitive function and nervous system development, and anti-inflammatory effects with a view to providing reference for the research and development of functional milk fat products.

In order to explore the inhibitory effect of bioactive substances on the degradation of milk fat during simulated gastrointestinal digestion, the impact of bioactive substances on the in vitro digestibility of milk proteins was examined as well as the inhibitory effect on pancreatic lipase activity and the micellar solubility of cholesterol. The results showed that the in vitro digestibility of milk proteins was inversely proportional to the concentration of the tested bioactive compounds, which decreased from 90.94% to 68.37% and 86.00% with increasing concentration of epigallocatechin (EGC) and β-glucan, respectively. The inhibitory effect of EGC on pancreatic lipase activity decreased to different extents with increased amount of added milk proteins, and so did the inhibitory effect of β-glucan and a mixed solution of 2.5 g/L β-glucan, 3.0 g/L epigallocatechin gallate (EGCG) and 2.0 g/L EGC on the micellar solubility of cholesterol. The inhibitory effect of this mixture on the degradation of milk fat was stronger than that of β-glucan.

Milk is not only rich in various nutrients, but also contains bioactive substances which have been documented to exert protective effects in the human body. Milk glycoproteins play a role in protecting against pathogen infection, modulating the intestinal flora and regulating the immune system. This paper summarizes the types of protein glycosylation and the methods used to study protein glycosylation and reviews milk glycoprotein composition, glycosylation sites, glycan structure and bioactive functions of milk glycoproteins, aiming at providing useful information for further study and utilization of these important bioactive glycoproteins.

Breast milk is the best source of food for infants and young children, and the whey proteins contained in the milk are the base of nutritional and bioactive substances including bioactive peptides, which play an important role in promoting human health. In this research, the antioxidant activities of peptides prepared by enzymatic hydrolysis of breast milk whey proteins with four different proteases, i.e., neutral protease, alkaline protease, papain and trypsin, were assessed and compared. The hydrolysis conditions were optimized using combination of one-factor-at-a-time method and response surface methodology. Neutral protease was found to be the most suitable enzyme for the production of antioxidant peptides from breast milk whey proteins. The optimal hydrolysis conditions were established as follows: pH 7.21, 50.03 ℃, an enzyme/ substrate ratio of 4 486.68 U/g and 5 h. The effect of hydrolysis parameters on 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity was in the decreasing order: enzyme/substrate (E/S) ratio > temperature > initial pH. Fraction I with the highest antioxidant activity was separated chromatographically with macroporous resin, Sephadex G-25 and Sephadex G-15, which could scavenge 60.31% of DPPH radical.

Milk protein is the most important nutrient in the initial stage of life, and it is abundant in kind and quantity. The composition of milk proteins has been made more complex and tremendously increased through a large number of genetic variations and sufficient protein translation. Proteomics permits one to systematically and integrally study milk proteins to understand the ways milk proteins constitute and regulate some life activities and further obtain a comprehensive and in-depth understanding of the expression levels of milk proteins. This paper describes the main techniques used in proteomics studies, including two dimensional electrophoresis, high performance liquid chromatography (HPLC), isobaric tags for relative and absolute quantitation (iTRAQ), mass spectrometry and bioinformatics techniques. The applications of proteomics in studies on human and bovine milk in particular differential proteomics analysis are discussed. To conclude, proteomics allows a better understanding of human and bovine milk which can provide a theoretical basis for developing infant foods and dairy products.

In this study, proteins from human and bovine milk fat globule membranes were separated using SDS-PAGE and identified by liquid chromatography-mass spectrometry (LC-MS). It was found that 1 076 proteins from human milk fat globule membrane were identified, and 682 proteins from bovine milk fat globule membrane. Among these proteins, 757 specifically expressed proteins were derived from human milk fat globule membrane, and 363 specifically expressed proteins from bovine fat globule membrane, with 319 of these being common to both. According to gene ontology (GO) annotations analysis, human milk fat globule membrane proteins played a more significant role in biological process than did bovine milk fat globule membrane proteins, especially in cellular component organization. The molecular function of human milk fat globule membrane proteins was exerted mainly through binding. In cellular composition, human milk fat globule membrane proteins were more dominant than bovine milk fat globule membrane proteins, and mostly participated in intracellular components. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis showed that there were 15 human milk fat globule membrane proteins involved in the digestion and absorption related KEGG pathway—enzymatic glycolysis. The study of human milk fat globule membrane proteins can improve the accuracy of milk fat globule membrane protein utilization, and the experimental data obtained may provide theoretical reference for future development of functional foods for infants.

In this study, the whey proteins in human and bovine colostrum were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and identified by liquid chromatography-mass spectrometry (LC-MS). A total of 477 whey proteins were identified in human colostrum and 325 in bovine colostrum. Totally, 343 proteins were specifically expressed in human colostrum and 191 in bovine colostum. Moreover, 134 specifically expressed proteins were common to both. Gene ontology (GO) annotation analysis revealed that human colostrum whey proteins played a more important role in bioprocesses especially stress responses than their bovine counterparts. Human colostrum whey proteins exerted functions by binding to other molecules. Human colostrum whey proteins were more important constituents of cellular structures as compared with their bovine counterparts, and they were the most significant constituents of extracellular structures. According to the Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway database, 23 whey proteins in human colostrum were involved in the KEGG pathway related to digestion and absorption, enzymatic glycolysis.