Bovine milk is considered as the raw milk of choice for the production of infant formula. Amino acids in bovine milk, the structural units that make up milk proteins are classified into two groups: free and insoluble-proteome amino acids, which are distributed in different regions (structural domains). In this experiment, we collected bovine colostrum at 0–7 days postpartum and mature milk at 15 days-6 months postpartum for comparative analysis of the insoluble-proteome and free amino acids in them. The results indicated that 9 essential free amino acids and 7 non-essential free amino acids were detected in both milks. Additionally, another non-essential free amino acid was found in bovine colostrum. Among these, 8 essential and 4 non-essential amino acids were found to be significantly more abundant in bovine colostrum than in mature milk (P < 0.05). Among the insoluble-proteome amino acids, 8 essential amino acids and 10 non-essential amino acids were detected simultaneously in both milks. Moreover, the levels of threonine, arginine, serine, cysteine, alanine in bovine colostrum were significantly higher than in mature milk (P < 0.05), while the level of lysine was significantly lower than in mature milk (P < 0.05).

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.

Dairy products are an important part of the dietary structure of Chinese residents. A wide variety of dairy products are commercially available, which are rich in nutrients and contain high-quality protein, various trace elements and functional ingredients including such active ingredients that are beneficial for lipid metabolism as milk calcium, whey, polar lipids and conjugated linoleic acid. Dairy products have the potential to regulate blood lipids and reduce the risk of cardiovascular disease. In addition, dairy products are high-quality carriers of active ingredients, and the active ingredients in milk can synergize with those added to milk to regulate blood lipids or to protect them. For this reason, milk is often used as an ingredient of functional dairy products. Hyperlipidemia is recognized worldwide as one of the risk factors for cardiovascular and cerebrovascular diseases such as atherosclerosis, coronary heart disease and hypertension. Studies have shown that functional milk can aid in regulating blood lipids. This paper reviews the current status of studies on dairy products and lipid metabolism-related health problems, aiming to provide a theoretical basis for the research of functional dairy products.

In order to understand the influence of interaction between the functional components and milk proteins in lipidlowering milk on the effectiveness of the functional components, we investigated the influence of casein and whey protein on the inhibitory effect of epigallocatechin (EGC) against pancreatic lipase, and we also determined the influence on the antioxidant activity of a mixture of EGC and the functional components as well as the influence on the inhibitory effect of a mixture of β-glucan and the functional components on the solubility of cholesterol-containing micelles. The results showed that milk protein could reduce the inhibitory effect of the functional components on pancreatic lipase activity, and decrease their antioxidant activity and their ability to inhibit the solubility of cholesterol-containing micelles.

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.

SDS-PAGE was used for separating the protein components of milk fat globule membranes (MFGMs) from bovine colostrum and milk, and it was found that the compositions of milk fat globule membrane proteins in colostrum and mature milk were different. A total of 628 MFGMs were identified in bovine colostrum and 487 MFGMs in mature milk. Gene ontology (GO) annotation showed that the main role milk fat globule membranes from bovine colostrum and milk played in biological processes was biological regulation. With respect to molecular function, bovine colostrum fat globule membrane proteins had greater binding capacity than mature milk fat globule membrane proteins, and the former was found to exist much more abundantly in extracellular areas than the latter. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis demonstrated that both membrane proteins participated in different metabolic pathways, implicating that bovine colostrum can be further processed into high-quality products.

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.