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PubMed2005

Human IgE binding to the glycosidic moiety of bovine kappa-casein.

IgE ability for recognizing milk proteins was assayed in the serum of an adult atopic patient who outgrew cow milk allergy in early childhood. A number of protein species included in casein from bovine milk were detected by human IgE in immunoblotting experiments. Comparing these results with those obtained from an analysis using antibody preparations specifically directed toward the different casein fractions, IgE-reactive bands were identified as isoforms of kappa-casein. IgE-reactive protein was not present in neither bovine cheese, regardless of cheese-making technology and time ripening, nor milk from any other dairy animal, such as ewe, goat, and water buffalo. Chemical deglycosylation of protein bands immobilized onto nitrocellulose proved that the glycosidic moiety of bovine kappa-casein was principally involved in IgE recognition.

Animals↗

PubMed2005

Interactions of vitamin D3 with bovine beta-lactoglobulin A and beta-casein.

It is of nutritional significance to fortify processed dairy products (e.g., cheese, yogurt, and ice cream) with vitamin D3; however, the inherent complexity of these foods may influence the stability and bioavailability of this nutrient. In the present study, the interactions of vitamin D3 with beta-lactoglobulin A and beta-casein were investigated under various environmental conditions (i.e., pH and ionic strength) using fluorescence and circular dichroism spectroscopic techniques. The results indicated that vitamin D3 was bound to both beta-lactoglobulin A and beta-casein depending on the solution conditions. The apparent dissociation constants ranged from 0.02 to 0.29 microM for beta-lactoglobulin A, whereas the beta-casein apparent dissociation constants ranged from 0.06 to 0.26 microM. The apparent mole ratios were also comparable, i.e., 0.51-2.04 and 1.16-2.05 mol of vitamin D3 were bound per mole of beta-lactoglobulin A and beta-casein, respectively. It was concluded that these interactions may strongly influence vitamin D3 stability and, hence, bioavailability in processed dairy products.

Animals↗

PubMed2006

Control of heat-induced aggregation of whey proteins using casein.

The ability of alphas1/beta-casein and micellar casein to protect whey proteins from heat-induced aggregation/precipitation reactions and therefore control their functional behavior was examined. Complete suppression (>99%) of heat-induced aggregation of 0.5% (w/w) whey protein isolate (pH 6.0, 85 degrees C, 10 min) was achieved at a ratio of 1:0.1 (w/w) of whey protein isolate (WPI) to alphas1/beta-casein, giving an effective molar ratio of 1:0.15, at 50% whey protein denaturation. However, in the presence of 100 mM NaCl, heating of the WPI/alphas1/beta-casein dispersions to 85 degrees C for 10 min resulted in precipitation between pH 6 and 5.35. WPI heated with micellar casein in simulated milk ultrafiltrate was stable to precipitation at pH>5.4. Protein particle size and turbidity significantly (P<or=0.05) increased from an initial diameter of 165.5 nm in the unheated mixture to 272 nm following heating at 85 degrees C for 10 min at pH 6. Whey protein denaturation was significantly (P<or=0.05) promoted when heated in the presence of micellar casein, but whey protein aggregation was controlled down to pH 5.4. The protective behavior of alphas1/beta-casein and micellar casein differed in that the former inhibited denatured whey protein aggregation, whereas the latter system promoted denaturation but controlled aggregation.

Caseins↗

PubMed2006

Study of the effect of soy proteins on the acid-induced gelation of casein micelles.

The objective of this research was to understand whether addition of soy protein to milk protein affects the properties of acid-induced casein gels. Different samples were prepared by suspending casein micelles pellets in milk serum containing soy proteins or whey proteins as well as mixtures of the two proteins. Glucono-delta-lactone was added, and the changes in apparent size (in diluted systems) as well as the viscoelastic properties of the mixtures were measured. Size exclusion chromatography was also carried out to characterize the soluble phase of the various mixtures before and after heating. Soy protein affected the gelation of the mixtures; however, not to the same extent as whey proteins, which dominated formation of the network in soy-whey-casein systems. It was concluded that, up to a critical ratio of soy/whey proteins, soy proteins can be incorporated in the mix without a significant change in structure of the casein gels.

Caseins↗

PubMed2006

Conjugation of sodium caseinate and gum arabic catalyzed by transglutaminase.

Conjugation of the milk protein sodium caseinate and a protein-containing polysaccharide, gum arabic, was achieved through the use of the cross-linking enzyme transglutaminase. The extent of conjugation was monitored by size exclusion separation coupled with a multiangle laser light scattering detector. The elution times of gum arabic solutions incubated with transglutaminase were unchanged over time, whereas incubation of sodium caseinate with transglutaminase resulted in shorter elution times as reaction time increased, indicating the formation of cross-linked caseinate polymers. However, when mixtures of caseinate and gum arabic were incubated with transglutaminase, the elution times were decreased markedly, indicating conjugation between the protein and polysaccharide. The molecular masses of the conjugates increased from approximately 950 to 1600 kDa. This method of protein-polysaccharide conjugation offers noticeable advantages over previously used methods, and the conjugates produced may exhibit unique functional properties.

Caseins↗

PubMed2000

Orthokinetic flocculation of caseinate-stabilized emulsions: influence of calcium concentration, shear rate, and protein content.

Calcium-induced flocculation of caseinate-stabilized soybean oil-in-water emulsions in conditions of Couette flow was studied. A concentrated emulsion (20% oil, 0.5-2.0% sodium caseinate in 20 mM imidazole, pH 7) was diluted 20 times in buffer containing concentrations of CaCl(2) between 9 and 17 mM and sheared at rates between 335 and 1340 s(-)(1). The average particle size (d(43)), measured by integrated light scattering, increased in a sigmoidal manner with shearing time. An increased shear rate resulted in an increased flocculation rate, because of the increased number of collisions between particles, but a decreased value of the maximum d(43), because higher shear rates increasingly disrupted the flocs. The flocculation rate was increased by increasing the calcium concentration, indicating an increased collision efficiency. The orthokinetic stability of the emulsions was increased with increased protein content, and it is postulated that the increased surface coverage and hydrodynamic thickness of the adsorbed protein layer increased steric repulsion between droplets, so that higher calcium concentrations were necessary to induce sufficient conformational change of the proteins to allow flocculation. At high caseinate concentrations, calcium may also induce precipitation of unadsorbed caseins from the serum to the oil-water interface, thereby increasing steric repulsion and hence increasing orthokinetic stability.

Calcium↗

PubMed2000

Characterization of commercial and experimental sodium caseinates by multiangle laser light scattering and size-exclusion chromatography.

A range of sodium caseinate samples were characterized by a multiangle laser light scattering (MALLS) system or by the use of MALLS as an on-line detector with size-exclusion chromatography (SEC). Sodium caseinate solutions, analyzed using a MALLS system alone, gave weight-average molar mass (M(w)) values in the range 1200-4700 kDa and z-average root-mean-square radius (R(g)) values ranged from approximately 50 to 120 nm. When these solutions were ultracentrifuged at 90000g for 1 h, a cloudy top layer was formed; the subnatant was carefully removed and analyzed by SEC-MALLS. The M(w) values were found to be in the range approximately 30-575 kDa, and R(g) values ranged from approximately 22 to 49 nm. During SEC, the MALLS system detected some very large-sized material that eluted close to the void volume; this material was hardly detected by the concentration detectors, i.e., ultra-violet (UV) and differential refractive index (DRI). The intensity of the light scattering (LS) signal from this very large sized material was greatly reduced in the subnatant. SEC of sodium caseinate samples revealed two main peaks with M(w) of approximately 420-750 kDa and 39-69 kDa, respectively. The R(g) values were very large for a protein molecule, and initial calculations suggested that the shape of caseinate molecules was likely to be highly elongated.

Caseins↗

PubMed2000

Zinc transport in Caco-2 cells and zinc balance in rats: influence of the heat treatment of a casein-glucose-fructose mixture.

The effects of the heat treatment of casein in the presence of glucose-fructose on Zn bioavailability were studied. Changes in Zn speciation were compared after in vitro digestion of heated (HC) and unheated mixture (C) alone and as part of the diet. The uptake and transport of digested soluble Zn was investigated in Caco-2 cells grown in bicameral chambers; balance studies were done in rats fed diets containing the different samples. After in vitro digestion, the precipitated Zn was significantly higher in HC than in C. In assays with Caco-2 cells, the amount of Zn transferred from the apical to the basolateral chamber was significantly greater when the culture medium contained raw or heated casein. However, because a larger proportion of Zn was precipitated by in vitro digestion, Zn utilization was less efficient in the presence of casein. In biological experiments, food efficiency of the heated casein-glucose-fructose diet was lower, and feeding this diet increased the urinary Zn excretion and lowered Zn absorption and retention. The effects of browning products generated during food processing should be taken into account, especially in diets containing marginally adequate levels of Zn, to prevent possible deficiency.

Animals↗

PubMed2005

Interactions between denatured milk serum proteins and casein micelles studied by diffusing wave spectroscopy.

The acid-induced aggregation of casein micelles from milk, in the presence of different whey protein preparations from heated and unheated milk, has been studied using diffusing wave spectroscopy (DWS). In particular, the study focused on the turbidity (or l*) parameter obtainable from DWS, which can give information on the interactions between particles in aggregating systems. The experiments provided evidence that the presence of small, soluble, whey protein/kappa-casein aggregates derived from heated milk gave rise to interactions with both heated and unheated casein micelles over a pH range of 5.6 down to 5.2. Comparison of heated and unheated milks, together with milks whose sera had been exchanged, showed that direct interactions were indeed occurring, even between untreated casein micelles and soluble whey protein complexes. Comparison of the behavior of the whey protein aggregates in emulsion preparations where they could not interact with the large particles confirmed that the effect was specific to the presence of casein micelles and could not arise simply from the aggregation of the whey proteins themselves.

Caseins↗

PubMed1998

Effect of inclusion of cashew globulin (Anacardium occidentale) to a casein diet on lipid parameters in rats.

The effect of inclusion of cashew globulin to a casein diet on lipid metabolism was studied in rats fed diets with two levels of cashew globulin meal. Inclusion of cashew globulin to a casein diet produced lower levels of total cholesterol, triacylglycerol and phospholipids in the serum and tissues and lower levels of serum lipoprotein cholesterol. There was decreased cholesterogenesis in the liver as evidenced by decreased activity of HMG CoA reductase and decreased release of lipoproteins into circulation. Rats fed cashew globulin along with casein also showed higher activity of LPL in the heart and adipose tissue and higher activity of LCAT. Increased hepatic diversion of cholesterol to bile acid synthesis and increased excretion of bile acids and sterols were also observed in these groups. Activity of glucose-6-phosphate dehydrogenase and malic enzyme was decreased in rats fed cashew globulin along with casein. This study demonstrates that cashew globulins included in the diet of rats are able to alter lipid metabolism which results in lower levels of lipid parameters in the serum and tissues.

Adipose Tissue↗

PubMed1999

A hybrid bovine beta-casein/bGH gene directs transgene expression to the lung and mammary gland of transgenic mice.

We investigated spatial and temporal expression of bGH controlled by two different sizes (1.8 kb and 15 kb) of 5'-flanking sequences of the bovine beta-casein in transgenic mice. In the 1.8-kb promoter-containing mice, bGH expression was specifically confined to lung and mammary gland at lactation. While mammary gland expression was highly variable depending on the lines, lung expression was relatively constant with a high level in most lines. Moreover, this dual-tissue specificity of bGH expression was consistently retained in all of the 15 kb-promoter-containing mice, although a low ectopic expression was sometimes detected in salivary gland or brain. During mammary gland development in the 1.8-kb promoter-containing mice was mammary gland expression first detected at lactation, following the bovine rather than murine pattern of beta-casein expression. In contrast, lung expression was almost constant regardless of mammary gland developmental state or sex. Therefore, it can be concluded that a combination of the bovine beta-casein promoter and bGH gene directs a distinct dual-tissue specific bGH expression with different regulatory mechanisms between mammary gland and lung and as little as 1.8-kb promoter is sufficient for the proper regulation of the bovine beta-casein gene in mammary gland.

Animals↗

PubMed1997

Effect of ethanol on nuclear casein kinase II activity in brain.

Casein kinase II (CK II) plays an important role in serine/threonine dependent protein phosphorylation. In brain it is associated with long term potentiation besides its involvement in DNA, RNA and protein metabolism. Ethanol has been shown to induce cognitive impairment and affects DNA, RNA and protein metabolism at various steps. Since CK II is central in all these events, which are specifically affected by ethanol, the role of nuclear CK II is investigated in the present study. Total nuclear casein kinase activity was unaffected while heparin sensitive nuclear casein kinase II activity showed a 30% decrease in the brain from chronic alcohol fed rats. Cytosolic CK II activity was also unaffected. Immunological detection by western analysis using CK II antibodies showed no alteration in the quantity of enzyme. The decrease in nuclear casein kinase II might be responsible for ethanol induced cognitive impairment in the brain.

Animals↗

PubMed1979

Initiation and processing in vitro of the primary translation products of guinea-pig caseins.

1. Guinea-pig caseins synthesized in a mRNA-directed wheat-germ cell-free protein-synthesizing system represent the primary translation products, even though they appear to be of lower molecular weight when analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis in parallel with caseins isolated from guinea-pig milk. 2. Identification of the N-terminal dipeptide of the primary translational product of caseins A, B and C and alpha-lactalbumin showed that all shared a common sequence, which was identified as either Met-Arg or Met-Lys. 3. Procedures utilizing methionyl-tRNAfMet or methionyl-tRNAMet in the presence or absence of microsomal membranes during translation provide a rapid method of distinguishing between N-terminal processing of peptides synthesized in vitro and other post-translational modifications (glycosylation, phosphorylation), which also result in a change in mobility of peptides when analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 4. The results demonstrate that guinea-pig caseins, in common with most other secretory proteins, are synthesized with transient N-terminal 'signal'-peptide extensions, which are cleaved during synthesis in the presence of microsomal membranes.

Animals↗

PubMed1981

Differential expression of alpha-lactalbumin and casein genes during the onset of lactation in the guinea-pig mammary gland.

1. The expression of alpha-lactalbumin and casein genes was examined in guinea-pig mammary tissue taken from animals both pre- and post-partum. 2. Analysis of total RNA by RNA excess hybridization with sequence-specific complementary DNA probes demonstrated that alpha-lactalbumin mRNA was present late in pregnancy, and that maximum concentrations were present at parturition. Casein gene transcripts were absent late in pregnancy (62 days), but by parturition were present at concentrations identical to those found at all time points examined throughout lactation. 3. Studies using mammary explants in organ culture showed that tissue from pregnant animals, or animals at parturition, synthesized and secreted only alpha-lactalbumin. After parturition, at the onset of casein synthesis, differential rates of secretion of alpha-lactalbumin and the caseins were observed. 4. The results are discussed in terms of the multiple intracellular mechanisms involved in the regulation of milk protein gene expression in the guinea-pig mammary gland.

Animals↗

PubMed1982

Characterization of the translation products of the major mRNA species from rabbit lactating mammary glands and construction of bacterial recombinants containing casein and alpha-lactalbumin complementary DNA.

Total cytoplasmic polyadenylated RNA from lactating rabbit mammary glands was analysed on methylmercury hydroxide-agarose gels. The size of the most abundant mRNA species ranged between 0.5 and 5.0 kb (kilobases), with major bands at 0.55, 0.84, 0.92, 1.18 and 2.4 kb and discrete minor bands of 1.5, 1.7, 3.0 and 3.9 kb. Translation in vitro of total mRNA with [3H]leucine or [35S]methionine as precursor yielded four major bands with apparent Mr values of 16 000, 25 000, 26 000 and 29 000. The four protein bands were identified by immunoprecipitation by using specific antisera as alpha-lactalbumin and x-, kappa- and alpha-caseins, respectively. Labelling with (35S]cysteine followed by immunoprecipitation with anti-transferrin or anti-alpha-lactalbumin sera allowed the identification of two whey proteins. Translated transferrin was resolved as an 80 000-dalton band and alpha-lactalbumin appeared as a 16 000-dalton protein. A library of recombinant plasmids containing cDNA (complementary DNA) sequences representing cytoplasmic polyadenylated RNA was used to isolate clones for the major rabbit caseins and alpha-lactalbumin. A preliminary characterization of these cDNA clones was achieved by colony hybridization with enriched RNA fractions as probes. Positive clones were identified by use of hybrid-promoted translation in vitro and immunoprecipitation of the translation products. The corresponding mRNA species were further identified by hybridizing RNA blots with radioactively labelled cDNA clones. We present the restriction map of alpha-casein and kappa-casein cDNA clones.

Animals↗

PubMed1982

Isolation and characterization of beta- and gamma-caseins from horse milk.

Three groups of casein components were isolated from horse milk. Group I is almost insoluble at acid and neutral pH, and is rather heterogeneous on alkaline gels with or without sodium dodecyl sulphate. Group II shows strong similarity to beta-casein from other species, as concluded from its amino acid composition and its N- and C-terminal sequences. This group consists of five electrophoretically distinguishable forms, all containing ester phosphate groups but no carbohydrate. Group III is composed of C-terminal fragments of the beta-like (group II) fraction and probably arises from the action of a plasmin-like enzyme present in horse milk. It does not contain phosphate or carbohydrate. Homology of this group with bovine gamma-caseins is demonstrated. Both beta- and gamma-like caseins are more soluble at 4 degrees C than at room temperature.

Acid Phosphatase↗

PubMed1993

Characterization of two novel casein transcripts in rabbit mammary gland.

Two clones were isolated from a cDNA library corresponding to mRNAs which accumulate in mid-lactating (14 day) rabbit mammary gland and characterized by DNA sequencing. The two clones sequenced corresponded to two novel casein transcripts (pBRM5 and pBRM42). Relative mRNA abundances for the two clones were assessed by dot-blot analysis. Phylogenetic analysis and comparison of both pBRM5 and pBRM42 with other members of the casein family revealed that the rabbit may be unique among mammals in expressing two alpha s2-casein genes. The presence of two alpha s2-casein genes in the rabbit may be the result of a relatively recent intergenic duplication event.

Amino Acid Sequence↗

PubMed1996

Ability of a beta-casein phosphopeptide to modulate the precipitation of calcium phosphate by forming amorphous dicalcium phosphate nanoclusters.

The ability of casein in the form of colloidal-sized casein micelles to modulate the phase separation of calcium phosphate during milk secretion is adapted to produce nanometre-sized particles of calcium phosphate stabilized by a casein phosphopeptide (nanoclusters). The nanoclusters were prepared from an undersaturated solution of salts and the peptide by raising the pH homogeneously from about 5.5 to 6.7 with urea plus urease. Chemical analysis and IR spectroscopy showed that they comprise an amorphous dicalcium phosophate bound to the phosphopeptide. Multinuclear NMR spectroscopy of the cluster solutions showed that the small ions and free peptide in the solution were in a state of dynamic exchange with the nanoclusters. The peptide is linked to the calcium phosphate through its sequence of phosphorylated residues, but, in a proportion of adsorbed conformational states, the termini retain the conformational freedom of the unbound peptide. The ability of casein to form nanoclusters in milk suggests a more general mechanism for avoiding pathological calcification and regulating calcium flow in tissues and biological fluids exposed to or containing high concentrations of calcium.

Adsorption↗