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PubMed1977

Action of milk clotting enzymes on alphas-caseins from buffalo's and cow's milk.

alphaS-Caseins were isolated from buffalo's and cow's milk and hydrolyzed with rennet, bovine pepsin, microbial proteases from Mucor miebei, Mucor pusillus Lindt, and Endotbia parasitica. The rate of hydrolysis was followed by determining the unaltered alphaS-casein in the digest after acrylamide gel electrophoresis. The rate of hydrolysis of alphaS-casein from the two species with the different enzymes was comparable, being more rapid with microbial enzymes particularly Endotbia parasitica protease. However, the electrophoretic patterns of the degradation products of buffalo's and cow's alphaS-casein produced by microbial rennets were not identical.

Animals↗
PubMed1979

Antigenicity of casein enzymatic hydrolysate.

An enzymatic hydrolysate of bovine casein were studied for molecular size and antigenic properties. As determined by Sephadex G-25 gel filtration, polypeptide fractions having molecular weights greater than 1,000 were not detected in the soluble fraction of the casein hydrolysate. Antigenicity of the fraction was not detected by heterologous passive cutaneous anaphylaxis in guinea pig-rabbit antiserum system mediated by immunoglobulin G types of antibody (guinea pig passive cutaneous anaphylaxis) and its inhibition test. Furthermore, it was not detected by rat long latency homologous mediated by immunoglobulin E antibody and its inhibition test. To prepare anticasein immunoglobulin E serum for rat long latency homologous passive cutaneous anaphylaxis, immunization of rats was by single subcutaneous injection of casein with aluminum hydroxide. Antiserum with highest passive cutaneous anaphylaxis titer (1:64) against bovine casein was obtained by a dose of 2,000 micrograms of the protein at day 12.

Animals↗
PubMed1987

Variability in true protein, casein, nonprotein nitrogen, and proteolysis in high and low somatic cell milks.

Monthly variation in milk protein (total nitrogen X 6.38) and milk fat was determined for 115 farms over 2 yr. Yearly average milk protein and fat tests in each year were 3.16 and 3.62%, respectively. The mean regression coefficient for milk protein with respect to milk fat was .47 for the entire period. Twenty-four farms were selected and grouped high or low based on their previous 2-yr somatic cell history. Monthly milk samples for each farm were tested for direct microscopic somatic cell count, total nitrogen, noncasein nitrogen, and nonprotein nitrogen. No differences in monthly nonprotein nitrogen, true protein, and casein were found between groups. Casein as a percent of total nitrogen was significantly higher for the low somatic group for seven of the 12 mo studied but was significantly higher for 9 mo when expressed as a percent of true protein. The average increase in tyrosine value for incubated preserved milk was significantly higher for the high somatic cell milk, indicating higher proteolytic activity in high somatic cell milk. Electrophoretic analysis of high and low somatic cell milk indicated that there was substantial proteolytic breakdown of alpha S-casein and beta-casein by proteases associated with elevated somatic cell counts.

Animals↗
PubMed1988

Content of alpha S1-casein and coagulation properties in goat milk.

Samples of goat milk with low and high alpha S1-casein content collected from animals of Alpine and Saanen breeds in the same stage of lactation were compared for coagulation properties (coagulation time, rate of curd formation, curd firmness) and chemical composition (total solids, ash, total protein, total casein, whey protein, fat, Ca, P, pH). Milk with low alpha S1-casein had a faster coagulation time, whereas milk with high levels produced the firmer curd associated with a better chemical composition. Within high alpha S1-casein milk, comparison between breeds showed milk from the Alpine breed had significantly better coagulation properties than that from the Saanen breed. Milk composition accounted for 27% of the variation in coagulation time, 21% of variation in cured formation rate, and 54% of variation in curd firmness.

Animals↗
PubMed1988

Molecular cloning and expression of bovine kappa-casein in Escherichia coli.

A cDNA library was constructed using poly(A) +RNA from bovine mammary gland. This cDNA library of 6000 clones was screened employing colony hybridization using 32P-labelled oligonucleotide probes and restriction endonuclease mapping. The cDNA from the selected plasmid, pKR76, was sequenced using the dideoxy-chain termination method. The cDNA insert of pKR76 carries the full-length sequence, which codes for mature kappa-casein protein. The amino acid sequence deduced from the cDNA sequence fits the published amino acid sequence with three exceptions; the reported pyroglutamic acid at position 1, tyrosine at position 35, and aspartic acid at position 81 are, respectively, a glutamine, a histidine, and an asparagine in the clone containing pKR76. The MspI-, NlaIV-cleaved fragment (630 base pair) from the kappa-casein cDNA insert has been subcloned into expression vectors pUC18 and pKK233-2, which contain a lac promoter and a trc promoter, respectively. Escherichia coli cells carrying the recombinant expression plasmids were shown to produce kappa-casein protein having the expected mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and being recognized by specific antibodies raised against natural bovine kappa-casein.

Amino Acid Sequence↗
PubMed1990

Effects of dietary protein degradability and casein or amino acid infusions on production and plasma amino acids in dairy cows.

Responses to daily abomasal infusions of 400 g sodium caseinate, 400 g hydrolyzed casein, or 11.3 g L-methionine plus 30.1 g L-lysine were compared in eight Holstein cows fed diets with estimated ruminal protein degradabilities of 70 and 60.%. Basal diets contained corn silage and corn with either soybean meal or 66.7:33.3 soybean meal:corn gluten meal added. Infusion with Methionine plus lysine increased milk protein content when cows fed either diet but increased milk fat content and yield only when the soybean meal diet was fed. Sodium caseinate increased milk and milk protein production and decreased milk fat percentage. Concentration of total essential amino acids, branched chain amino acids, and urea cycle amino acids were increased by the infusion of both casein sources. Methionine-lysine infusion increased plasma lysine and taurine, a metabolite of methionine, suggesting that absorbed methionine was extensively metabolized. Results demonstrate an impact of both ruminal degradability of dietary protein and form of infused protein on amino acid nutrition of lactating daily cows.

Abomasum↗
PubMed1990

Effect of rumen-protected methionine and lysine on casein in milk when diets high in fat or concentrate are fed.

To examine the effect of supplying methionine and lysine on milk N composition, isoenergetic, isonitrogenous diets containing 50:50 with 3.9% added fat or 25:75 forage to concentrate with no added fat were fed with or without rumen-protected methionine and lysine to four primiparous and four multiparous early lactation (36 d in milk) Holstein cows in two 4 x 4 Latin squares. Diets contained 1.7 Mcal NE1 and were fed for ad libitum intake. Periods were 21 d. Rumen-protected methionine and lysine increased total N and casein N percentage with the 3.9% fat, but did not increase total N and casein N percentage with the diet without fat. Whey N percentage was greater with the no fat than with the 3.9% fat diet. Whey N percentage was not affected by adding amino acids. Nonprotein N percentage was greater for the diet with the 3.9% fat than with no fat. Proportions of casein N or whey N to total N were unaffected by treatments. Adding methionine and lysine to diets did not increase yields of total N and casein N. The 3.9% fat diet increased proportions of long-chain (C18:0 and C18:1) and decreased proportions of short- to medium-chain fatty acids (C8 to C16) in milk fat. Plasma nonesterified fatty acids and triglyceride concentrations were greater with the 3.9% fat as compared to the no fat diet. Methionine and lysine decreased plasma triglyceride concentrations with the 3.9% fat diet. Milk yields, DM intakes, and plasma glucose concentrations were unaffected by treatment.

Animal Feed↗
PubMed1991

Effects of differences in starch content of diets with whole cottonseed or rice bran on milk casein.

Forty lactating Holstein cows in early to midlactation were used in a randomized complete block design to measure the effects of the following diets on milk casein. Treatments were four complete rations fed for ad libitum intake consisting of 1) 60% concentrate, 10% alfalfa hay, and 30% corn silage; 2) 45% concentrate, 10% alfalfa hay, 30% corn silage, and 15% whole cottonseed; 3) 60% concentrate, 5% alfalfa hay, 20% corn silage, and 15% whole cottonseed; and 4) 45% concentrate, 10% alfalfa hay, 30% corn silage, and 15% rice bran. Least squares means for daily DM intake all were significantly different and were 3.51, 3.90, 3.28, and 3.74% BW, respectively. Cows fed diet 3 had higher arterial glucose and insulin and venous insulin. Least squares means were significantly different for milk yield, 30.1, 31.4, 28.4, and 31.6 kg/d; for milk protein, 3.30, 3.13, 3.48, and 3.12%; and for casein N, .376, .358, 3.73, and .330, respectively. However, milk protein and casein N yields were similar for all cows. The diet that contained the highest percentage of starch did not result in a significantly higher percentage of casein N in the milk but had the lowest milk production. Both whole cottonseed and rice bran, substituted for concentrate, depressed milk protein percentage.

Animal Feed↗
PubMed1991

Casein interference in bovine plasmin assays using a synthetic substrate.

Bovine plasmin (EC 3.4.21.7) activity on H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide was measured by determining the change in absorbance at 405 nm. Initial rates of reactions were estimated at all combinations of the following substrate concentrations [.4, 4, and 40 times the substrate concentration at one-half maximum velocity (Vmax) (Km)] and casein concentrations [.068, .68, and 6.8 times the inhibitor constant for competitive inhibition (KI)]. By nonlinear least squares fitting of the data to an equation that described reversible enzyme kinetics, steady state kinetic parameters, maximum velocity (Vmax), substrate concentration at one-half maximum velocity (Vmax) (Km), inhibitor constant for competitive inhibition (KI), and inhibitor constant for uncompetitive inhibition (KI) were estimated. Casein fit the equation as a competitive inhibitor of bovine plasmin. This enzyme has a catalytic constant (Kcat) of .0158 change in absorbance at 405 nm/min per nM, substrate concentration at one-half maximum velocity (Vmax) (Km) of .107 mM substrate, and inhibitor constant for competitive inhibition (KI) of .86 mg/ml of casein. Bovine plasmin activity can be measured directly in bovine milk without interference from casein.

Animals↗
PubMed1991

Insulin in bovine colostrum and milk: evolution throughout lactation and binding to caseins.

The changes in insulin concentration in bovine milk in the first period of lactation and its association with other milk proteins were studied. Highest concentration was found in the first milking (327 ng/ml). This concentration fell within the first 24 h postpartum to about 50% of its initial value. By d 3, the level was about 25%, and, on d 7, a stable concentration was reached at approximately 46 ng/ml (about 14% of its initial value). This concentration is about 100 times higher than that in serum, which suggests a specific mechanism of transfer from blood to milk. Colostral whey obtained by ultrafiltration or ultracentrifugation contains much less insulin than colostrum. When colostrum or milk was incubated with [125I]insulin and whey and casein fractions were separated by precipitation, it was observed that most insulin remained with the casein. However, when colostrum was incubated with [125I]insulin and subjected to gel filtration, most of the radioactivity corresponded to free insulin, indicating that insulin is associated with the precipitated casein but not with the casein micelles in solution.

Animals↗
PubMed1992

Variations and distributions of O-glycosidically linked sugar chains in bovine kappa-casein.

The variation and distribution of O-glycosidically linked sugar chains in kappa-casein from bovine mature milk were analyzed by HPLC, fast atom bombardment mass spectrometry, and 13C nuclear magnetic resonance. A monosaccharide alditol (N-acetylgalactosaminitol) and four oligosaccharide alditols [a neutral disaccharide (galactosyl-beta 1-3N-acetylgalactosaminitol), two acidic trisaccharides (straight chain: N-acetylneuraminyl alpha 2-3galactosyl-beta 1-3N-acetylgalactosaminitol and branch chain: galactosyl beta 1-3(N-acetylneuraminyl alpha 2-6)N-acetylgalactosaminitol), and an acidic tetrasaccharide(N-acetylneuraminyl alpha 2-3galactosyl-beta 1-3(N-acetylgalactosaminyl alpha 2-6)N-acetylgalactosaminitol] were identified as sugar chains linking on normal bovine kappa-casein. The most dominant sugar chain was an acidic tetrasaccharide. The four oligosaccharide chains were identical to those already found, but N-acetylgalactosamine was a newly identified sugar chain linking on kappa-casein. The distribution of monosaccharide, disaccharide, trisaccharide (straight), trisaccharide (branched), and tetrasaccharide chains were determined by HPLC to be .8, 6.3, 18.4, 18.5, and 56.0%, respectively (means of five kappa-caseins).

Animals↗
PubMed1992

Casein, actin, and tubulin expression during early involution in bovine and murine mammary tissue.

Hybridization methods and in vitro translation were used to examine the expression and functional condition of messenger RNA encoding caseins and cytoskeletal proteins in the mammary gland during early involution. In the mouse, steady state mRNA levels for alpha-, beta-, and gamma-caseins coordinately decreased to 20% of initial levels between 12 and 72 h after pup removal. In vitro translatability of mouse casein mRNA, as determined by immunoprecipitation, electrophoresis, and gel slice counting, revealed a pattern that closely paralleled mRNA expression. In contrast, bovine casein mRNA levels were only slightly reduced by 72 h postmilking, whereas in vitro translatability decreased by about one-half. Northern blot analysis of total mouse mammary RNA that were hybridized with probes to cytoskeletal proteins showed a gradual decrease of alpha-tubulin mRNA, but an increase in beta-actin mRNA during early involution. Two-dimensional gel analysis of in vitro translated products indicated a concordant increase in beta-gamma-actin. In the cow, beta-actin mRNA at 72 h of involution was equal to or greater than that during lactation. These results demonstrate the generally slower involution response in the cow and suggest that differing regulations are involved. Early events of cellular involution may be related to a reorganization of the cytoskeleton.

Actins↗
PubMed1993

Casein to whey protein ratio in rat and human milks: effects of maternal protein intake.

Maternal diet may affect milk composition quantitatively and qualitatively. The aim of this study was to assess the effects of different dietary protein quality and quantity on total milk protein concentration and on possible changes in casein:whey protein ratio as a result of differences in maternal nutritional status. Milk samples were obtained from Wistar rats fed either wheat gluten or supplemented casein at different percentages. A similar analytical scheme was applied to milk samples from lactating women belonging to different socioeconomic classes. Total milk protein in rat milk was related closely to protein quality and, to a lesser extent, to protein quantity, showing significant differences among treatment groups. Relative proportions between milk proteins were significantly affected by diet: casein: whey protein ratio was related positively to protein quality and quantity. In human milk, even though total protein content did not differ, the relative proportions between milk proteins were altered, but in a way opposite to that observed in rat milk: the whey protein:casein ratio was related positively to maternal protein intake. These modifications might influence the nutritive value or anti-infectious properties of the milk ingested by the neonate.

Animals↗
PubMed1993

Effect of infused volatile fatty acids and caseinate on milk composition and coagulation in dairy cows.

Milk protein secretion is changed by increasing the proportion of energy, mainly as propionic acid, or the availability of AA. Whether associative effects exist between energy nature and protein amounts is unknown. Therefore, ruminal isoenergetic infusions of low or high propionate mixtures were combined factorially with duodenal infusion of sodium caseinate or control. Four ruminally and duodenally fistulated Holstein cows were used. The diet was limited and consisted of 70% forage and 30% concentrate. Caseinate infusion increased milk yield and protein and casein contents and decreased milk fat content; curd yields and coagulation properties of milk were improved. The infusion of propionic acid caused a large increase in rumen propionate. Milk yield tended to decrease, and milk fat decreased, but protein, casein, and curd yields were unchanged; milk-coagulating properties were improved. No interaction existed between energy and protein amounts. Alteration of VFA had little effect on milk composition, but increasing the protein supply to the duodenum increased milk protein.

Animals↗
PubMed1993

Inhibition of plasmin by beta-lactoglobulin using casein and a synthetic substrate.

Bovine plasmin (EC 3.4.21.7) activity was measured on H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide and acid casein in the presence of native and heat-denatured beta-lactoglobulin (denatured at 100 degrees C for 15 min before being mixed with plasmin solutions). Native or denatured beta-lactoglobulin was then heated with plasmin at 60 degrees C for 15 min. Enzyme activity again was estimated after this mild heat treatment. Native and denatured beta-lactoglobulin inhibited the action of plasmin on H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide and casein. The mild heat treatment (60 degrees C for 15 min) caused stronger inhibition of the activity of plasmin against casein and the synthetic substrate. For H-D-valyl-L-leucyl-L-lysyl-4-nitroanilide, inhibition was competitive in unheated mixtures, but heating beta-lactoglobulin with plasmin changed inhibition type to mixed. This change suggests a heat-dependent interaction between plasmin and beta-lactoglobulin. Native beta-lactoglobulin was more inhibitory of plasmin's action against casein than was denatured beta-lactoglobulin. The converse was observed when plasmin activity was measured with the synthetic substrate.

Animals↗
PubMed1996

Alterations of the physical characteristics of milk from transgenic mice producing bovine kappa-casein.

kappa-Casein is the protein fraction of milk that allows formation of micelles and determines micelle size and function, thus affecting many of the physical characteristics of milk. Several lines of transgenic mice were generated bearing the B allele of the bovine kappa-CN gene under the control of the regulatory sequences of the caprine beta-CN gene that specifically directed expression of bovine kappa-CN to the lactating mammary tissue of these mice. High expression of bovine kappa-CN protein was observed in the lines studied; the total level of protein in milk was not significantly affected. A high degree of conservation in the amino acids involved in the predicted three-dimensional structure exists between murine and bovine kappa-CN. Milk from transgenic lines expressing high bovine kappa-CN had a significantly smaller micelle size than did control milk. Therefore, bovine kappa-CN appears to have effectively participated in assembly of murine casein micelles. There was no effect on the time of rennet coagulation, but the association was significant between the milk of transgenic lines and the production of a stronger curd in rennet-induced gels. We conclude that bovine kappa-CN is an appropriate candidate for transgenic technology that would increase the ratio of kappa-CN to the calcium-sensitive caseins, therefore affecting the physical properties of the colloidal casein suspension.

Amino Acid Sequence↗
PubMed1998

Micelle stability: kappa-casein structure and function.

The stability of the casein micelle is dependent on the presence of kappa-casein (CN) on the surface of the micelle where it functions as an interface between the hydrophobic caseins of the micelle interior and the aqueous environment. kappa-Casein is also involved in thiol-catalyzed disulfide interchange reactions with the whey proteins during heat treatments and, after rennet cleavage, in the facilitation of micelle coagulation. These functions of kappa-CN are regulated by the three-dimensional structure of the protein on the micelle surface. The usual means of determining structure are not available for kappa-CN because this protein is strongly self-associating and has never been crystallized. Instead, algorithms were used to predict selected secondary structures and circular dichroism spectroscopy on kappa-CN and the macropeptide released by chymosin. Three peptides were synthesized to cover the chymosin-sensitive site (His98-Lys111), the region in the macropeptide that could be helical (Pro130-Ile153), and the region between. Nuclear magnetic resonance spectroscopy showed that the peptide His98-Lys111 was probably a beta-strand with tight turns at each end. This hypothesis was confirmed by a study of the molecular dynamics showing that the C variant of kappa-CN interacted less strongly with chymosin; consequently, the slow renneting time of milk that contains this protein was explainable. Both circular dichroism and nuclear magnetic resonance indicated that the peptide Pro130-Ile153 was probably helical under normal physiological conditions. A preliminary study using nuclear magnetic resonance showed that the intervening peptide had no discernible secondary structure. Consequently, most of the beta-sheet structure of kappa-CN is likely in the para-kappa-CN region.

Amino Acid Sequence↗
PubMed1999

Significance of amount and form of dietary selenium on blood, milk, and casein selenium concentrations in grazing cows.

Organic selenized yeast enriched with selenoamino acids or inorganic sodium selenate (Na2SeO4) was administered per os three times weekly as a drench for 133 d to previously unsupplemented cows that were grazing low Se pastures. Treatment groups received the equivalent of 2 or 4 mg of Se/d of either supplement form. Control cows did not receive a drench. Samples of blood and milk were collected regularly throughout the trial. Selenium concentrations in blood, milk, casein, and liver and glutathione peroxidase activity in blood and liver are reported as responses per milligram of Se intake. Mean blood Se concentrations in treated cows increased steadily and, by d 133, were 4.7 to 8.8 times that in controls. Selenized yeast was 2 to 3 times more effective than was Na2SeO4, and low Se intakes were 27% more efficient per milligram of Se administered than were high Se intakes at increasing milk Se concentration. Casein Se content mirrored that of milk; among all treated and control cows and throughout the trial, the molar ratio of Se in casein as a percentage of the Se in whole milk was constant at 71 +/- 1.2%. The Se concentration in liver biopsies taken on d 133 was indicative of total Se intake during the trial and ranged from 920 to 3920 nmol of Se/kg of fresh weight. These results demonstrate the differing efficacy of organic and inorganic Se dietary supplements to increase dairy cow Se status and to enhance Se content of milk and casein.

Animals↗