Academic literature on the topic 'Alpha-lactalbumin milk protein'

This review covers modern possibilities of modeling breast milk unique properties to produce infant milk formulas. The main approach of such modelling is to advance the protein composition in the formula to the spectrum of breast milk proteins, primarily α-lactalbumin. This protein has multi-directional protective properties; the organism synthesizes the antibacterial and immunomodulating peptide complex HAMLET (Human Alpha-lactalbumin Made LEthal to Tumor cells, complex of α-lactalbumin and oleic acid) on its basis. The amino acid composition of α-lactalbumin provides mild neuroprotective effect due to sufficient level of tryptophan. Non-protein components of the produced formulas (carbohydrate and fat included) enhance their protective qualities and ensure the prevention of delayed health disorders. This review provides information about the innovative baby food product containing ?-lactalbumin and other bioactive components like those in breast milk.

A variety of proteins contributes greatly to the unique nutritional and functional quality of dairy cow milk. Particularly, milk casein content and composition have substantial influence on the processing capabilities. In the present study, milk of 23 multiparous Holstein-Friesian cows, grouped as high- (3.49 ± 0.05%; n = 11) and low-protein (3.03 ± 0.05%; n = 12) cows, was sampled approximately weekly during the first 155 days of lactation to determine the course of relative milk protein composition (α-lactalbumin; β-lactoglobulin; α-, β-, and κ-casein). Furthermore, feed restrictions by 30% of dry matter intake in early and mid-lactation as well as experimental tissue biopsies were conducted to observe their effect on milk protein composition. Milk protein composition was relatively stable and displayed similar concentration patterns throughout the experimental period between both groups. Mean relative concentrations of α-, β-, κ-casein, α-lactalbumin, and β-lactoglobulin were 34.2, 31.4, 16.0, 2.1, and 9.7% of total protein, respectively. Feed restrictions did not alter milk protein composition, whereas the season influenced α- and β-casein as well as α-lactalbumin. Further, effects were observed in both groups at times of unfamiliar stressful situations caused by taking liver or muscle biopsies. As a result, the relative concentration of β-casein increased. Therefore, acute stress factors may lead to a deviation in milk protein composition and should be avoided.  

We have generated transgenic mice carrying the entire guinea-pig alpha-lactalbumin gene. Lactating transgenic mice expressed high levels of correctly initiated and processed guinea-pig alpha-lactalbumin mRNA in the secretory epithelium of their mammary glands, and secreted guinea-pig alpha-lactalbumin in their milk. Transcripts were detectable after 7 days of pregnancy, indicating that the transgene was under correct hormonal control. Whereas no or negligible transcription was detectable in all other tissues tested, high levels of transcripts were found in the skin of lactating transgenic mice. Guinea-pig alpha-lactalbumin protein was undetectable in the skin, however. In situ hybridization analysis showed that expression was localized to the undifferentiated cells in the basal layer of the sebaceous glands. Further studies revealed high levels of endogenous beta-casein mRNA in normal lactating mouse skin, demonstrating that the transcription of milk protein genes in lactating mouse skin is a normal event, and is not peculiar to the transgene. This surprising finding highlights the developmental relationship of the mammary gland to other specialized structures of the skin, supports a role for epithelial-extracellular matrix interactions in the regulation of milk protein gene expression in vivo, and identifies the skin as a particularly accessible model system in which to study the regulation of milk protein gene expression. In addition, the guinea-pig alpha-lactalbumin gene will be a source of regulatory sequences with which to direct heterologous gene expression to the sebaceous glands of transgenic mice.

Two concentrates, one protein-rich and one based on cereals, were combined with two silages with a crude protein content of 17 and 13% of dry matter (DM), respectively to give four different diets for dairy cows. Milk content of caseins (α_S1-, α_S2-, β-, and κ-casein) and whey proteins (α-lactalbumin (α-LA) and β-lactoglobulin (β-LG)) and the fatty acid profile of milk were analyzed before the start and on four occasions during the experiment. Milk analyses showed that diet had no influence on the protein profile of the milk. However, a significant increase of α-linolenic acid, 13 and 39%, was obtained on the high protein concentrate feed and on the silage higher in crude protein, respectively. Cows on the protein-rich concentrate diet increased the proportion of conjugated linoleic acid by 53%. Linoleic acid was not affected by the diet.  

Objective: The aim of this work was to study the biochemical characteristics of coconut milk and its antigenic effect on the Balb/c mice immunized with α-lactalbumin protein, as well as its consequences on the structure of the intestinal epithelium.Methods: To achieve the objective of the study, an electrophoresis was realised on a polyacrylamide gel to determine various proteins contained in coconut milk. In addition, Lowry’s method was used to determine the amount of proteins in the formula. The antigenicity of coconut milk in sera was also studied using the Enzyme-Linked Immunosorbent Assay (ELISA) method. For the histological study, 21 w-old mice Balb/c were used and distributed in three groups of 7 mice each. Group 1, received a standard feed with no treatment (Negative control), group 2 and 3 received respectively a standard feed (Positive control) and coconut milk for a period of 28 d after being immunized with α- lactalbumin.Results: Analysis of the data revealed that the rate of proteins of cow’s milk is higher than that of the coconut milk ( p0.01). However, after carrying out the electrophoresis analysis, the coconut milk showed the absence of intact proteins. The anti α-Lactalbumin IgG titers significantly increased in positive control groups that received coconut milk (p<0.0001). Moreover, there was an increase of the intestinal villi height of mice fed with coconut milk, in the structure level of their intestinal epithelium compared to the negative control group.Conclusion: The findings of the study provide the evidence that coconut milk is a possible alternative to the cow’s milk formula in case of allergy.

As studies by Russian and foreign scientists show, the breed and the cows genotype affects on their productivity and milk quality. In connection with this, the purpose of this research was to study the milk productivity and milk quality of the Tatarstan type Kholmogory cows with different complex genotypes on the milk protein genes, namely, alpha S1-casein, beta-casein, kappa-casein, beta-lactoglobulin, alpha-lactalbumin. The genotypes on the milk protein genes were determined by DNA analysis methods. Determination of quantitative and qualitative indicators of milk was carried out by control milking and on a milk analyzer «LAKTAN1–4». Better raw milk, that is, with the greatest amount of nutrients, such as milk fat and protein, was milk from cows with complex genotypes of milk proteins ВВ/АВ/АВ/АВ/АА, ВВ/АВ/АВ/АВ/АВ, ВВ/АВ/АВ/АВ/ВВ. In practical terms, it is possible to get more quality dairy products from such raw materials.

Milk is a food of high nutritional value processed by heat treatment. Heat treatment of milk is a technological process designed to inhibit the growth of microorganisms and extend the shelf life of products. The heating process directly affects the molecular structure of whey proteins by the process of denaturation. It leads to the formation of a whey protein–casein polymer complex. Based on these facts, milk heat-treatment conditions should be controlled during milk processing. This work focuses on describing the whey protein denaturation process and formation of the complex of whey protein with casein. The effect of heat treatment on individual milk protein fractions alpha-casein (α-cas), beta-casein (β-cas), kappa-casein (κ-cas), beta-lactoglobulin (β-lg) and alpha-lactalbumin (α-la) was studied by SDS-PAGE. Formation of the whey protein–casein polymer complex increased significantly (p < 0.05) on increasing the temperature and duration of the heat treatment.

Frozen storage is necessary to preserve expressed human milk for critically ill and very preterm infants. Milk pasteurization is essential for donor milk given to this special population. Due to these storage and processing conditions, subtle changes occur in milk nutrients. These changes may have clinical implications. Potentially, bioactive complexes of unknown significance could be found in human milk given to preterm infants. One such complex, a cytotoxic α-lactalbumin-oleic acid complex named “HAMLET,” (Human Alpha-Lactalbumin Made Lethal to Tumor cells) is a folding variant of alpha-lactalbumin that is bound to oleic acid. This complex, isolated from human milk casein, has specific toxicity to both carcinogenic cell lines and immature non-transformed cells. Both HAMLET and free oleic acid trigger similar apoptotic mechanisms in tissue and stimulate inflammation via the NF-κB and MAPK p38 signaling pathways. This protein-lipid complex could potentially trigger various inflammatory pathways with unknown consequences, especially in immature intestinal tissues. The very preterm population is dependent on human milk as a medicinal and broadly bioactive nutriment. Therefore, HAMLET’s possible presence and bioactive role in milk should be addressed in neonatal research. Through a pediatric lens, HAMLET’s discovery, formation and bioactive benefits will be reviewed.

Human milk is rich in nutritional factors, such as alpha-lactalbumin (α-Lac), and important for neonatal development, but nutrient supplementation may be required for optimal growth. Using a pig model, we hypothesized that α-Lac-enriched whey protein concentrate (WPC) supplementation improves neonatal development. Cesarean-delivered preterm pigs were fed either dilute bovine milk (REF) or REF milk supplemented with WPC with normal (STANDARD-ALPHA) or high (HIGH-ALPHA) α-Lac. Clinical, gut, immune and cognitive endpoints (open field, T-maze) were assessed and tissues collected at Day 19. The growth of STANDARD-ALPHA and HIGH-ALPHA were higher than REF (31 vs. 19 g/kg/d). Most organ weights, gut, immunity and brain variables were similar between WPC groups. HIGH-ALPHA had a higher bone mineral content, colon microbial diversity and an abundance of specific bacteria and microbial metabolites, and tended to show a faster food transit time (p = 0.07). Relative to REF, WPC pigs showed higher relative organ weights, blood amino acids, blood neutrophil function, and microbial metabolites, but lower brush-border enzyme activities and plasma cortisol. Cognition outcomes did not differ among the groups. In conclusion, WPC supplementation of milk improved some growth, gut and immunity parameters in preterm pigs. However, increasing the α-Lac content beyond human milk levels had limited effects on the immature gut and developing brain.

This study was conducted to evaluate changes in composition of whey proteins of Czech White Short-haired goat and East Friesian ewe milk and their comparison throughout lactation. Some differences in composition between ewe and goat milk were found. The results showed that the mean total protein (%), whey protein (g/100 g), and &beta;-lactoglobulin (&beta;-Lg, g/100 g) contents of goat milk were 2.75, 0.433, and 0.119 respectively and of ewe milk 6.36, 1.11, and 0.732 respectively. The contents of total protein as well as acid whey proteins in goat milk were nearly constant throughout the lactation period and fluctuated around the mean value while the contents of total protein as well as acid whey proteins in ovine milk were dependent on the period of lactation. The total protein content in ovine milk continuously increased during the lactation period. A higher content of ovine acid whey proteins was noticed at the beginning and in the final period of lactation. The average ratio of whey to total protein was 15.8  2.61% in goat milk and 17.4  2.68% in ewe milk and ranged from 13.0 to 20.4% in goat and from 14.0 to 20.8% in ewe milk. The total contents of two major whey proteins. &alpha;-lactalbumin and &beta;-lactoglobulin (&alpha;-La + &beta;-Lg = AG), averaged 87% of total whey protein, 92% in ovine milk. The main component of acid whey proteins in goat milk was &alpha;-La while in ovine milk the main component of acid whey proteins was &beta;-Lg, however, at the end of the lactation period the content of &beta;-Lg for both kinds of milk increased steeply, and the &beta;-Lg/&alpha;-La ratio reached a maximum value of 1.94 in goat milk and of 9.74 in ewe milk. In addition, goat milk contains a similar amino acid profile to ewe milk but the amino acid pattern in whey proteins differs from that in milk. Total essential amino acids were approximately 40% of the total amino acids in goat and ewe milk as well as in goat and ewe whey. &nbsp; &nbsp;

Thesis (Ph. D.)--University of Wisconsin--Madison, 1991.
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Le lait écrémé est utilisé depuis plus d’un demi-siècle comme diluant protecteur des spermatozoïdes de mammifères. Depuis quelques années, il existe une demande grandissante pour des diluants exempts de produits d’origine animale. Toutefois, le mécanisme par lequel le lait protège les spermatozoïdes n’est pas connu, ce qui rend difficile de lui trouver un substitut. Les protéines majeures du plasma séminal de taureau, les protéines « Binder of SPerm » (BSP), sont néfastes lors de la conservation de la semence. Les spermatozoïdes sont en contact avec une grande concentration de protéines BSP qui stimulent une extraction continuelle de cholestérol/phospholipides de leur membrane plasmique. Les lipoprotéines de faible densité (LDL) du jaune d’oeuf, un autre composé utilisé dans les diluants, empêcheraient les protéines BSP de se lier à la membrane des spermatozoïdes de taureaux et de stimuler un efflux des lipides membranaires, ce qui les protégerait durant la conservation. Notre hypothèse était que les protéines du lait protègent les spermatozoïdes durant la conservation en séquestrant les protéines BSP. Premièrement, nous avons démontré par filtration sur gel qu’il y a une interaction entre les protéines BSP bovines et les protéines du lait. Le lait écrémé a été fractionné en trois fractions : F1 (alpha-lactalbumine, bêta-lactoglobuline et caséine kappa), F2 (toutes les protéines du lait) et F3 (sels, sucres et petits peptides). Les protéines BSP1 et BSP5 ont une affinité plus grande pour F1 que BSP3, tandis que toutes les protéines BSP ont une affinité pour F2. Le titrage calorimétrique isotherme a permis de confirmer l’interaction entre les protéines BSP et les protéines du lait. L’association entre la protéine BSP1 bovine et les micelles de caséines est caractérisée par une constante d’affinité (Ka) de 3.5 × 10^5 M-1 et un paramètre stoichiométrique (n) de 4,5 BSP1 pour une caséine. L’association entre la protéine BSP1 bovine et l’alpha-lactalbumine (une protéine du sérum principale), est caractérisée par un Ka de 2.4 × 10^5 M-1 et une valeur “n” de 0,8. Ces résultats indiquent que le lait protège les spermatozoïdes bovins en séquestrant les protéines BSP grâce à une interaction protéine : protéine, tandis que le jaune d’oeuf les protège grâce à une interaction protéine : lipoprotéine. Deuxièmement, nous avons démontré par filtration sur gel que les protéines homologues aux BSP bovines retrouvées dans le plasma séminal de porc, d’étalon et de bélier ont une affinité avec les protéines du lait, ce qui suggère que le mécanisme de protection des spermatozoïdes par le lait pourrait être le même chez ces espèces. Troisièmement, nous avons caractérisé l’interaction entre BSP1 bovine et les LDL du jaune d’oeuf qui a un Ka de 3.4 ± 0.4 × 10^6 M-1 et une valeur de « n » de 104 BSP1 pour une particule de LDL, indiquant qu’il existe des différences entre le mécanisme de protection des spermatozoïdes par le lait et le jaune d’oeuf. Nous croyons que les résultats présentés dans cette thèse aideront à créer de nouveaux diluants ne contenant pas de produits d’origine animale afin de cryoconserver les spermatozoïdes des mammifères.
Skim milk is being used as a protective agent for mammalian semen conservation over half a century. Recently, there has been increased interest in developing extenders free of animal products. However, it is difficult to find suitable component in order to replace milk as an extender, because the mechanisms by which milk protect sperm against cooling and freezing damages during the storage is unknown. The Binder of SPerm (BSP) proteins are the major proteins of bull seminal plasma and they are harmful during sperm storage. In fact, sperm would be in contact with a large quantity of BSP proteins that induce a continuous cholesterol and phospholipids efflux from the sperm membrane during storage. When bull sperm is diluted with an extender containing egg yolk, another compound frequently used in extender, the low-density lipoproteins (LDL) present in the egg yolk prevent the binding of the BSP proteins to the sperm membrane, thus, preventing the lipid efflux from the sperm membrane induced by the BSP proteins. Our hypothesis was that milk proteins would protect sperm during storage by binding BSP proteins. First, we demonstrated by gel filtration that bovine BSP proteins could bind the milk proteins. Skim milk was fractionated into three fractions: F1 (alpha-lactalbumin and beta- lactoglobulin, the major whey proteins and kappa-casein), F2 (mainly caseins and all other milk proteins in small amounts) and F3 (salts, sugars and small peptides). Bovine BSP1 and BSP5 have more affinity for F1 as compared to BSP3 and all the BSP proteins have affinity for F2. We confirmed the interaction between bovine BSP proteins and milk proteins by isothermal titration calorimetry. The binding of BSP1 to casein micelles is characterized by an affinity constant (Ka) of 3.5 × 10^5 M-1 and of a stoichiometric parameter for the association (n) of 4.5 BSP1 per casein. The association between BSP1 and alpha-lactalbumin (one of the major whey proteins) is characterized by a Ka of 2.4 × 10^5 M-1 and a “n” value of 0.8. These results support our contention that milk can protect sperm by preventing the BSP proteins’ binding to the sperm membrane attributable to a protein : protein interaction, while egg yolk sperm protection is attributable to a protein : lipoprotein interaction. Second, our studies showed that the homologous BSP proteins found in the boar, stallion and ram seminal plasma can bind the milk proteins. These results indicate that the mechanism of sperm protection by milk in these species should be similar to the one in bovine species. Third, we characterized the interaction between bovine BSP1 protein and LDL from hen’s egg yolk. The binding was characterized by a Ka of 3.4 ± 0.4 × 10^6 M-1 and a « n » value of 104 BSP1 per LDL particle. Our results indicated that there is difference between the mechanism of sperm protection by milk and egg yolk. We believe that the results presented in this thesis may help to create new extenders free of animal product for mammal sperm preservation in liquid or frozen state.