Porcine milk proteins: A review (original) (raw)
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Nomenclature of the proteins of cows' milk--sixth revision
Journal of dairy science, 2004
This report of the American Dairy Science Association Committee on the Nomenclature, Classification, and Methodology of Milk Proteins reviews changes in the nomenclature of milk proteins necessitated by recent advances of our knowledge of milk proteins. Identification of major caseins and whey proteins continues to be based upon their primary structures. Nomenclature of the immunoglobulins consistent with new international standards has been developed, and all bovine immunoglobulins have been characterized at the molecular level. Other significant findings related to nomenclature and protein methodology are elucidation of several new genetic variants of the major milk proteins, establishment by sequencing techniques and sequence alignment of the bovine caseins and whey proteins as the reference point for the nomenclature of all homologous milk proteins, completion of crystallographic studies for major whey proteins, and advances in the study of lactoferrin, allowing it to be added t...
2020
Processing milk into dairy products leaves a large portion of milk protein, which can be used in many ways. Milk protein is<br> composed of casein and whey protein. Casein is predominate bovine milk protein, which forms large colloidal particles and present in the<br> form of casein micelles. Whey is liquid by products in chess manufacturing or liquid obtained from remove fat and casein from milk.<br> Generally, protein, especially milk protein, has multiple functions in food, such as emulsification, foam formation and stability.<br> Condensed milk protein is a high quality protein that is found naturally in the milk. These milk powders provide powerful and nutritious<br> multifunctional nutrients for the global food and beverage industry due to their high protein content. Milk Protein also consider high<br> quality protein and provide various nutritional benefits, which should be included into the diets. The objective of this review is to<br&g...
Milk Proteins - From Structure to Biological Properties and Health Aspects
InTech eBooks, 2016
Mammalian milk is a complex fluid mixture of various proteins, minerals, and lipids, which play an important role in providing nutrition and immunity to the newborn. Casein proteins, which form about 80% of the bovine milk proteins, form large colloidal particles with calcium phosphate to form casein micelles, which for many years have been an important subject of interest. Casein micelles are composed of four main types of proteins: α S1-casein, α S2-casein, β-casein, and k-casein. These constituent casein proteins lack well-defined secondary and tertiary structure due to large amount of propyl residues. These micelles are being extensively studied because of their importance in functional behavior of milk and various milk products. However, the exact structure and nature of these casein micelles are still under debate. These different casein proteins possess different functional properties due to their primary amino acid sequence.
Proteins profile in milk from three species of ruminants
Notulae Scientia Biologicae, 2011
Milk proteins, caseins and whey proteins, are very important nutritionally, as they contain all essential aminoacids in optimal proportions and are the most important source of bioactive peptides. These peptides are protein fragments resulting from enzymatic hydrolysis of milk proteins, which carry numerous beneficial effects on the cardiovascular, nervous, gastrointestinal and immune systems. In this research, total proteins, caseins and whey proteins respectively, were dosed in milk from three species of ruminants-cow, goat and sheep, using a very sensitive method, Bradford photometric method. The highest content of total proteins was obtained in sheeps' milk (65.92 mg/ml) and the lowest in cows' milk (40.03 mg/ml), intermediate values occurring in goats' milk (46.79 mg/ml). The lowest amount of caseins was found in cow milk (28.26 mg/ml), followed by sheep milk (42.55 mg/ml) and goat milk (44.03 mg/ml). When the case of whey proteins, the highest values occur in sheep milk (23.36 mg/ml) and the lowest in cow milk (11.79 mg/ml), goat milk having intermediate values (17.7 mg/ml). The results obtained indicate the dependence of protein concentration in milk of the studied ruminant species and stresses the importance of including goat and sheep milk in daily diet, along with cow milk, for an optimal intake of protein.
Asian-Australasian Journal of Animal Sciences, 2015
Milk composition is an imperative aspect which influences the quality of dairy products. The objective of study was to compare the chemical composition, nitrogen fractions and amino acids profile of milk from buffalo, cow, sheep, goat, and camel. Sheep milk was found to be highest in fat (6.82%±0.04%), solid-not-fat (11.24%±0.02%), total solids (18.05%±0.05%), protein (5.15%±0.06%) and casein (3.87%±0.04%) contents followed by buffalo milk. Maximum whey proteins were observed in camel milk (0.80%±0.03%), buffalo (0.68%±0.02%) and sheep (0.66%±0.02%) milk. The non-protein-nitrogen contents varied from 0.33% to 0.62% among different milk species. The highest r-values were recorded for correlations between crude protein and casein in buffalo (r = 0.82), cow (r = 0.88), sheep (r = 0.86) and goat milk (r = 0.98). The caseins and whey proteins were also positively correlated with true proteins in all milk species. A favorable balance of branched-chain amino acids; leucine, isoleucine, and valine were found both in casein and whey proteins. Leucine content was highest in cow (108±2.3 mg/g), camel (96±2.2 mg/g) and buffalo (90±2.4 mg/g) milk caseins. Maximum concentrations of isoleucine, phenylalanine, and histidine were noticed in goat milk caseins. Glutamic acid and proline were dominant among non-essential amino acids. Conclusively, current exploration is important for milk processors to design nutritious and consistent quality end products.
Proteomics of major bovine milk proteins: Novel insights
International Dairy Journal, 2017
Milk proteomics covers the identification, characterisation and quantification of milk proteins. Its applications vary from the basic composition of milk proteins to their post-translational modifications (PTMs), occurring naturally or via processing and storage. Through the combination of liquid chromatography or two-dimensional gel electrophoresis with advanced mass spectrometry, milk proteomics has revealed PTMs that affect milk protein structural and functional properties. This review discusses detection by proteomics-based methods with special emphasis on natural and process induced PTMs in the major bovine milk proteins. The review covers the importance of milk proteomics in determining PTMs, especially those formed by heat treatment and during storage, and highlights some breakthroughs in PTM studies. Furthermore, aspects and applications of quantitative proteomics on milk proteins and bioinformatics are covered. ___________________________________________________________________________________ 1998). Milk from other species have been included in other reviews (Cunsolo, Muccilli, Saletti & Foti, 2011; El-Salam, 2014) and will not be included here. Overall, bovine milk proteins and related peptides can be classified into four different groups: caseins (α S1-, α S2-, βand κ-caseins), serum proteins [αlactalbumin (α-La), β-lactoglobulin (β-Lg), bovine serum albumin (BSA), immunoglobulins (Igs) and a range of other minor whey proteins], proteose peptones (low molecular weight peptides derived from caseins and well as proteose peptone component 3, called PP3) and membrane [mostly milk fat globule membrane (MFGM)] proteins (Table 1).
New data on the proteins of rabbit (Oryctolagus cuniculus) milk
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1995
The main rabbit milk proteins have previously been prepared by reversed-phase HPLC of the acid-precipitated material ('whole casein') and of its supernatant (acid whey). Most of them were nearly homogeneous on SDS-PAGE. Among those isolated from whole casein, ~st-, P-and g-caseins, as well as whey acidic protein (WAP) were identified by N-terminal sequencing. After further internal sequencing, two unknown proteins were found to be the putative products, ~a-and ~s2b-caseins of two recently sequenced transcripts from rabbit mammary gland. Each whole casein component gave several bands on IEF. For K-casein, this was probably due to uneven glycosylation as in all g-caseins studied so far. For the other whole casein components, including WAP, the number of bands roughly reflected the number of potential phosphorylation sites predicted from the sequences. For ~st-and ~2-caseins polymorphism could be detected. From acid whey, in addition to WAP, which was a minor component, reversed phase HPLC separated three proteins. These were ~-lactalbumin, transferrin and serum albumin, on the basis of their apparent molecular weights deduced from SDS-PAGE. WAP was a major component of the native whey obtained by ultracentrifugation of rabbit milk. It was found to consist of two identical subunits linked by at least one disulfide bridge.
Recent progress of porcine milk components and mammary gland function
Journal of Animal Science and Biotechnology, 2018
As the only nutritional source for newborn piglets, porcine colostrum and milk contain critical nutritional and immunological components including carbohydrates, lipids, and proteins (immunoglobulins). However, porcine milk composition is more complex than these three components. Recently, scientists identified additional and novel components of sow colostrum and milk, including exosomes, oligosaccharides, and bacteria, which possibly act as biological signals and modulate the intestinal environment and immune status in piglets and later in life. Evaluation of these nutritional and non-nutritional components in porcine milk will help better understand the nutritional and biological function of porcine colostrum and milk. Furthermore, some important functions of the porcine mammary gland have been reported in recent published literature. These preliminary studies hypothesized how glucose, amino acids, and fatty acids are transported from maternal blood to the porcine mammary gland for milk synthesis. Therefore, we summarized recent reports on sow milk composition and porcine mammary gland function in this review, with particular emphasis on macronutrient transfer and synthesis mechanisms, which might offer a possible approach for regulation of milk synthesis in the future.
Comparison of composition and whey protein fractions of human, camel, donkey, goat and cow milk
The aim of this study was to compare the physicochemical parameters of milk samples of five different species: cow, goat, donkey, camel and human. Also the analysis of whey protein profile in different milk samples was performed by anion-exchange fast protein liquid chromatography (FPLC) while polyacrylamide gel electrophoresis was used to identify a single fraction. Camel milk was the most acid (pH 6.460±0.005) and the richest in total proteins (3.41±0.31 %) and ash (0.750±0.102 %), whereas donkey milk had a neutral pH (7.03±0.02) and characterised by low proteins (1.12±0.40 %) and fat (0.97±0.03 %) content, being very close to human milk. Proteomic analysis of cow, goat, donkey, camel and human milk highlighted significant interspecies differences. Camel milk was similar to human milk in lacking of β-lactoglobulin and richness of α-lactalbumin. The knowledge gained from the proteomic comparison of the milk samples analysed within this study might be of relevance, both, in terms of...