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PubMed2003

Effect of controlled kappa-casein hydrolysis on rheological properties of acid milk gels.

An experimental method based on the controlled chymosin-induced kappa-casein hydrolysis of milk was proposed to modify micellar reactivity. Milk samples with a degree of kappa-casein hydrolysis of 19, 35, and 51% were obtained. The physicochemical properties of partially converted casein micelles were determined. The net negative charge of casein micelles was reduced with increasing degree of kappa-casein hydrolysis and a small but significant decrease in hydrodynamic diameter and micellar hydration were noted. Dynamic low amplitude oscillatory rheology was used to monitor the rheological properties of acid milk gels (GDL) made with partially chymosin-hydrolyzed milks in comparison with those of strictly acid and rennet gels. An increase in the gelation pH value was observed with increasing the degree of kappa-casein hydrolysis. The moduli values (G' and G'') reached 2 h after the point of gel were, for all degrees of hydrolysis tested, significantly higher than those of strictly rennet and acid gels. Comparison of changes in delta G'/delta t with time indicated differences in gel formation that could be related to the increased values of G' obtained for acid gel made with chymosin-treated milk. At a given time after gelation (2 h), increasing the degree of kappa-casein hydrolysis in milk led also to an increase in the loss tangent and the serum holding capacity of acid milk gels suggesting a correlation between these two parameters.

Animals↗
PubMed2003

Gelation mechanism of milk as influenced by temperature and pH; studied by the use of transglutaminase cross-linked casein micelles.

Casein micelles in milk are colloidal particles consisting of four different caseins and calcium phosphate, each of which can be exchanged with the serum phase. The distribution of caseins and calcium between the serum and micellar phase is pH and temperature dependent. Furthermore, upon acidification casein micelles lose their colloidal stability and start to aggregate and gel. In this paper, we studied two methods of acid-induced gelation, i.e., 1) acidification of milk at temperatures of 20 to 50 degrees C and 2) decreasing the pH at 20 degrees C to just above the gelation pH and subsequently inducing gelation by increasing the temperature. These two routes are called T-pH and pH-T, respectively. The gelation kinetics and the properties of the final gels obtained are affected by the gelation route applied. The pH-T milks gel at higher pH and lower temperature and the gels formed are stronger and show less susceptibility to syneresis. By using intramicellar cross-linked casein micelles, in which release of serum caseins is prevented, we demonstrated that unheated milk serum caseins play a key role in gelation kinetics and characteristics of the final gels formed. This mechanism is presented in a model and is relevant for optimizing and controlling industrial processes in the dairy industry, such as pasteurization of acidified milk products.

Animals↗
PubMed2004

Fat digestion in veal calves fed milk replacers low or high in calcium and containing either casein or soy protein isolate.

The hypothesis tested was that the inhibitory effect of dietary soy protein versus casein on fat digestion in veal calves would be smaller when diets were fed with high instead of low calcium content. Male calves, 1 wk of age, were fed 1 of 4 experimental milk replacers in a 2 x 2 factorial design. There were 19 animals per dietary group. The milk replacers contained either casein or soy protein isolate as variable protein source and were either low or high in calcium. Body weight gain was not significantly affected by the experimental diets. Soy protein isolate versus casein significantly reduced apparent fat digestibility. High versus low calcium intake also depressed fat digestion. The protein effect was smaller (2.9% units) for the high than the low calcium diets (3.6% units), but the interaction did not reach statistical significance. Soy protein isolate versus casein raised fecal bile acid excretion and so did high versus low calcium intake. The difference in bile acid excretion between the soy and casein containing diets was significantly greater for the high than low calcium diets. The absorption of phosphorus, calcium, and magnesium was higher for the casein diets than for the soy-containing diets. This study shows for the first time that soy protein isolate versus casein depressed fat digestion and raised fecal bile acid excretion in veal calves.

Animals↗
PubMed2005

Casein haplotype structure in five Italian goat breeds.

The aim of this work was to investigate the genetic structure of the casein gene cluster in 5 Italian goat breeds and to evaluate the haplotype variability within and among populations. A total of 430 goats from Vallesana, Roccaverano, Jonica, Garganica, and Maltese breeds were genotyped at alphas1-casein (CSN1S1), alphas2-casein, (CSN1S2), beta-casein (CSN2), and kappa-casein (CSN3) loci using several genomic techniques and milk protein analysis. Casein haplotype frequencies were estimated for each breed. Principal component analysis was carried out to highlight the relationship among breeds. Allele and haplotype distributions indicated considerable differences among breeds. The haplotype CSN1S1*F- CSN1S2*F-CSN3*D occurred in all breeds with frequencies >0.100 and was the most common haplotype in the Southern breeds. A high frequency of CSN1S1*0-CSN1S2*C-CSN3*A haplotype was found in Vallesana population (0.162). Principal component analysis clearly separated the Northern and Southern breeds by the first component. The variability of the caprine casein loci and variety of resulting haplotypes should be exploited in the future using specific breeding programs aiming to preserve biodiversity and to select goat genetic lines for specific protein production.

Animals↗
PubMed2005

Effects of bovine somatotropin on beta-casein mRNA levels in mammary tissue of lactating cows.

Bovine somatotropin (bST) increases milk production in lactating cows through its effect on nutrient partition and maintenance of mammary cell function. A positive relationship between bST treatment and abundance of beta-casein mRNA in mammary tissues from lactating cows was hypothesized. In mammary tissue isolated from 14 midlactation Holstein cows, beta-casein mRNA was 35.4% higher among 7 cows receiving continuous bST infusions at 29 mg/d for 63 d compared with tissue from 7 untreated control cows. To investigate whether increased beta-casein mRNA resulted from a direct effect of bST on the mammary gland, explants of mammary tissue from other lactating cows that had not received bST were incubated with bST and prolactin in 2 experiments. Mammary explant cultures taken from 2 lactating cows that had not been milked for 48 h were supplemented with either prolactin or bST. Both prolactin and bST stimulated higher levels of beta-casein mRNA in the mammary explants compared with their non-supplemented counterparts. Explant cultures from 4 additional lactating cows were prepared from rear quarter mammary tissue subjected to milking intervals of 6 h for right rear quarters or 20 h for left rear quarters. Both bST- and prolactin-mediated increases in beta-casein mRNA were dependent on milking intervals. That is, levels of beta-casein mRNA were increased by bST or prolactin supplementation in explants isolated from the mammary quarters biopsied 20 h after milking but not for those biopsied at 6 h after milking. Results are consistent with a potential role for bST in up-regulating or sparing beta-casein mRNA levels in lactating bovine mammary tissue in a manner similar to prolactin.

Animals↗
PubMed2005

Effects of emulsifying salts on the turbidity and calcium-phosphate-protein interactions in casein micelles.

Influence of emulsifying salts (ES) on some physical properties of casein micelles was investigated. A reconstituted milk protein concentrate (MPC) solution (5% wt/wt) was used as the protein source and the effects of ES [0 to 2.0% (wt/wt)] were estimated by measuring turbidity, acid-base titration curves and amount of casein-bound Ca and inorganic P (P(i)). Various ES, trisodium citrate (TSC), or sodium phosphates (ortho-, pyro-, or hexameta-) were added to MPC solution, and all samples were adjusted to pH 5.8. Acid-base buffering curves were used to observe changes in the amount and type of insoluble Ca phosphates. An increase in the concentration of TSC added to MPC solution decreased turbidity, buffering at pH approximately 5 (contributed by colloidal Ca phosphate), and amount of casein-bound Ca and P(i). Addition of up to 0.7% disodium orthophosphate (DSP) did not significantly influence turbidity, buffering curves, or amount of casein-bound Ca and P(i). When higher concentrations (i.e., > or =1.0%) of DSP were added, there was a slow decrease in turbidity. With increasing concentration of added tetrasodium pyrophosphate (TSPP), turbidity and buffering at pH approximately 5 decreased, and amount of casein-bound Ca and P(i) increased. When small concentrations (i.e., 0.1%) of sodium hexameta-phosphate were added, effects were similar to those when TSPP were added but when higher concentrations (i.e., > or =0.5%) were added, the buffering peak shifted to a higher pH value, and amount of casein-bound Ca and P(i) decreased. These results suggested that each type of ES influenced casein micelles by different mechanisms.

Animals↗
PubMed2006

Stability of casein micelles cross-linked by transglutaminase.

In this study, caseins micelles were internally cross-linked using the enzyme transglutaminase (TGase). The integrity of the micelles was examined on solubilization of micellar calcium phosphate (MCP) or on disruption of hydrophobic interactions and breakage of hydrogen bonds. The level of monomeric caseins, determined electrophoretically, decreased with increasing time of incubation with TGase at 30 degrees C; after incubation for 24 h, no monomeric beta- or kappa-caseins were detected, whereas only a small level of monomeric alphaS1-casein remained, suggesting near complete intramicellar cross-linking. The ability of casein micelles to maintain structural integrity on disruption of hydrophobic interactions (using urea, sodium dodecyl sulfate, or heating in the presence of ethanol), solubilization of MCP (using the calcium-chelating agent trisodium citrate) or high-pressure treatment was estimated by measurement of the L*-value of milk; i.e., the amount of back-scattered light. The amount of light scattered by casein micelles in noncross-linked milk was reduced by >95% on complete disruption of hydrophobic interactions or complete solubilization of MCP; treatment of milk with TGase increased the stability of casein micelles against disruption by all methods studied and stability increased progressively with incubation time. After 24 h of cross-linking, reductions in the extent of light scattering were still apparent in the presence of high levels of dissociating agents, possibly through citrate-induced removal of MCP nanoclusters from the micelles, or urea- or sodium dodecyl sulfate-induced increases in solvent refractive index, which reduce the extent of light-scattering.

Animals↗
PubMed2007

Evidence for fibril-like structure in bovine casein micelles.

The addition of Congo red (CR) dye to diluted raw skim milk resulted in a red shift indicative of the presence of fibril-like structures. Thioflavin T (ThT) is another dye that very specifically binds to protein fibrils, and when added to undiluted raw skim milk, the classic 485 nm fluorescence peak of a ThT-fibril complex was observed. Repeating these experiments with various raw milk components showed that the CR red shift and ThT fluorescence peak were due to the presence of casein micelles, and to a lesser extent, sodium caseinate. Fluorescent peaks were also observed when ThT was added to solutions of purified alpha(S)- and kappa-casein, but not beta-casein, in 0.5 M HEPES buffer (pH = 6.8). The addition of 25 mM Ca(2+) had no effect on beta-casein fluorescence, and significantly reduced the kappacasein peak. However, adding 25 mM Ca(2+) to alpha(S)-casein produced a turbid solution and a 6-fold increase in fluorescence, indicating that the aggregates formed contain fibril-like structure. Casein micelle images obtained by transmission electron microscopy showed the presence of short (7 to 10 nm) fibers cross-linked by dense aggregate junction zones. The observed fibers closely resemble protofibrils, intermediate structures that are observed during the formation of amyloid fibrils.

Animals↗
PubMed1976

Review: Casein micelle structure; an examination of models.

The casein micelle system of bovine milk is unique in that protein aggregates of similar spherical shape but extreme variability of size are formed by the self-assembly of three major nonidentical subunits. The monomeric subunits appear to be approximately the same size and shape with similar amphiphilic natures, the chief difference in properties being in the carbohydrate-containing kappa-casein which acts to stabilize the system against precipitation by calcium ion. Micelle models with kappa-casein exclusively in the interior lack a stabilization mechanism and can be eliminated. Statistical considerations of a chain polymer model also lead to its rejection. Electron microscopy reveals spherical submicellar aggregates which at present can be accounted for by only three models. Of these three, the experimental data are predicted only by one in which, alphas 1-, beta-, and kappa-casein subunits are associated into spherical soap micelle-like particles with the kappa-casein segregated into one portion, giving these submicelles an amphiphilic nature. The alphas 1- and beta-caseins are hydrophobic while the kappa-casein portion of the submicelle surface is hydrophilic. Of particular interest is the ability of this micelle model to explain the formation of a minimum micelle which is larger than a submicellar particle.

Amino Acid Sequence↗
PubMed1977

Phosphorylation of casein by the lactating mammary gland: a review.

The lactating mammary gland synthesizes and secretes large amounts of phosphoproteins that mainly are associated with the casein fraction of milk. The free amino acids and inorganic phosphate of blood serve as building materials for casein, and the final product appears in milk as a colloidal-sized particle, the casein micelle. According to our present concept, the biosynthesis of casein occurs in two steps: synthesis of the polypeptide chain, followed by phosphate addition. Phosphate groups are transferred to the nascent casein by a protein kinase localized in the Golgi apparatus. The enzyme uses adenosine 5'-triphosphate as the phosphate donor and requires divalent cations. Neighboring amino acids may be important in determining which serine residues in casein are phosphorylated. This review discusses historical and current research on the phosphorylation of casein.

Animals↗
PubMed1983

Effect of carbohydrate limitation on degradation and utilization of casein by mixed rumen bacteria.

Mixed rumen bacteria were incubated in media containing salts, ammonia, vitamins, volatile fatty acids, sulfide, and casein. When initial cell density was 1.0 absorbance unit and mixed carbohydrates (glucose, sucrose, maltose, cellobiose, and soluble starch) were provided at 0, 40, 80, and 160 mg/liter per h, cell growth was limited by carbohydrates, average bacterial growth rate was slow (less than .07/h), and types of bacteria did not appear to change during 7 h. Growth was small if casein was the sole source of energy. Addition of casein to incubations fed carbohydrates caused cell yield to double. Casein hydrolysis was accompanied by marked accumulation of peptides that were metabolized slowly by rumen bacteria. High pressure liquid chromatography indicated that the peptide pool was composed primarily of four fractions. Carbohydrate availability or bacterial growth had little influence on proteolysis or peptide accumulation. Ammonia production was always inversely proportional to rate of carbohydrate feeding. Nitrogen-15 labeling studies indicated that 66% of the cell nitrogen was derived directly from casein at all rates of carbohydrate addition. If average bacterial growth rate was approximately .07/h, little casein entered the ammonia pool even though large amounts of peptide or casein remained undegraded.

Ammonia↗
PubMed1986

Effects of intake and postruminal casein infusion on performance and concentrations of hormones in plasma of lactating cows.

Four Holstein cows were utilized in a Latin square design with a factorial arrangement of treatments to examine the interaction between effects of dry matter intake (107 vs. 78% of energy requirements) and postruminal infusions (water vs. 395 g/d casein) on lactational performance, utilization of nitrogen and energy, and plasma concentrations of hormones. Yields of milk and milk protein were decreased by feed restriction and increased by casein infusion with no treatment interactions. Restricting feed intake decreased total nitrogen intake by 143 g/d and resulted in smaller quantities of fecal, absorbed, urinary, milk, and retained nitrogen compared with cows fed ad libitum. Casein infusion increased total nitrogen intake (55 g/d), absorbed nitrogen (54 g/d), urinary nitrogen excretion (28 g/d), and milk nitrogen (13 g/d). Casein by dry matter intake interactions were not significant for nitrogen utilization. Restricting feed intake increased plasma growth hormone and decreased concentrations of insulin and triiodothyronine. Glucagon, prolactin, and thyroxine were not affected by intake. Casein infusion did not affect growth hormone, insulin, prolactin, triiodothyronine, or thyroxine. Increased milk and milk protein yields obtained with casein infusion were apparently not mediated through changes in circulating concentrations of these hormones; however, plasma glucagon was increased by casein infusions.

Animals↗
PubMed1991

Identification of kappa-casein genotype in Holstein sires: a comparison between analysis of milk samples from daughters and direct analysis of semen samples from sires by polymerase chain reaction.

Two different methods were used to determine kappa-casein genotypes of Holstein sires. In the earlier procedure, genotypes of sires were deduced by analyzing frequency distribution data of kappa-casein variants obtained through typing of milk samples from daughters by electrophoresis. The second method involved direct analysis of DNA obtained from semen samples of the sires. The polymerase chain reaction was used to amplify a 99-bp region from the kappa-casein gene that contains nucleotide substitutions that are diagnostic of variants A and B. Identity of the amplified product was confirmed by sequencing. Results obtained by both methods of genotyping were similar. For the 42 sires that were analyzed by both methods, the distribution of kappa-casein genotypes were 31 AA, 11 AB, and 0 BB. The frequency of B allele for kappa-casein in the sire population studied was lower than in larger Holstein cow populations. Due to the high demand for kappa-casein B milk by the dairy industry, it might be advantageous to increase this allele in the dairy cattle population by identifying sires with homozygous kappa-casein B and using them more frequently as service sires.

Alleles↗
PubMed1991

Quantification of alpha s1-casein in goat milk from French-Alpine and Anglo-Nubian breeds using reversed-phase high performance liquid chromatography.

Samples of isoelectrically precipitated goat casein from the milks of French-Alpine and Anglo-Nubian breeds were separated into four components in a single run by reversed-phase HPLC. The proportion of alpha s1-casein thus resolved was determined quantitatively. The method uses a reversed-phase C-4 column and a linear gradient from 30 to 50% acetonitrile in 30 min with trifluoroacetic acid constant at .1%. Sodium dodecyl sulfate-PAGE was carried out to establish the identity of the isolated components. By a comparison with previously published results for caprine and bovine milk caseins, the four peaks were identified as kappa-, alpha s2-, alpha s1-, and beta-casein. Quantitative variations in the chromatographically resolved alpha s1-casein fraction of goat milk were evident. Some individual goat milks contained high levels of alpha s1-casein (2.70 g/L), but others contained significantly low levels (.12 g/L). There was no statistical difference in the overall means between breeds in alpha s1-casein composition, but cluster analysis statistics showed three distinct categories of alpha s1-producers: high, medium, and low. Interestingly, 6 of 15 French-Alpine goats and only one Anglo-Nubian goat fell into the "low" producer category (.38 +/- .2 g/L). Thus, expression of the alpha s1-component may be genetically regulated but may not be a breed-specific trait.

Animals↗
PubMed1989

Effects of addition of sulfur-containing amino acids and glycine to soybean protein and casein on serum cholesterol levels of rats.

The effects of the supplementation of methionine (Met), cystine (Cys), and glycine (Gly) to soybean protein or casein on serum and liver lipid levels were studied in rats. Rats were fed cholesterol-free diets containing 25% soybean protein or casein supplemented with 0.75% Met, 2.5% Gly, or a combination of these two for 4 weeks. The addition of Met to soybean protein caused a significant increase in serum cholesterol and this was slightly ameliorated when Gly was given simultaneously. In rats fed casein diets, serum cholesterol tended to decrease when Gly, or Met and Gly were added. A simultaneous supplementation of Met and Gly to casein resulted in a reduction of hepatic cholesterol. Cystine added at the 0.6% level did not cause demonstrable changes in lipid concentrations except for a drop in serum triglyceride of the casein group. When 2.0% Gly was added to cholesterol-enriched diets containing 20% protein, serum cholesterol decreased significantly only when the protein source was casein and the level attained was comparable to that observed in rats fed soybean protein. Liver cholesterol was also markedly decreased by the addition of Gly to casein. The results suggest a possible role of Gly in the regulation of serum cholesterol levels by dietary protein.

Animals↗
PubMed1990

Nutritional and physiological effects of casein modified by glucose, diacetyl, or hexanal.

Casein was modified by glucose, diacetyl, or hexanal at 50 degrees C, RH 75% for 1, 7, or 11 days. The chemical changes and digestibility in vitro of these nondialyzable caseins were investigated. The effects of these nondialyzable caseins supplemented with lost amino acids, on rats were studied by pair-feeding for 2 months. It was observed that internal organs such as liver, spleen, kidney, stomach, small intestine, cecum, colon and rectum were mostly unchanged. Biochemical values such as hematocrit, cholesterol, triglyceride, GPT, and GOT were also unchanged. However, the quantity of leucocytes was increased and serum glucose was decreased by feeding rats with modified caseins. Significant decrease in weight gain of rats fed with modified casein was observed, and the rate of decrease depended on the degree of modification of casein by carbonyl compounds. From these results, we supported the suggestion that some inhibitory or antinutritional compounds might be formed during the modification of casein by carbonyl compounds.

Aldehydes↗
PubMed1998

Effects of soy protein isolate (SPI) and casein on the postprandial lipemia in normolipidemic men.

To elucidate the effects of soybean protein and casein on postprandial lipemia, oral fat load tests were performed before and 3 weeks after the administration of soy protein isolate (SPI) and casein supplement to normolipidemic men. Eleven normolipidemic male subjects on otherwise identical controlled diets were assigned to either a 20 g/d soy protein isolate (SPI) dietary supplement or a casein dietary supplement for three weeks in a crossover design. Fat load tests with 40 g/m2 of bovine milk fat were carried out before and after 3 weeks on the experimental dietary supplements. Fasting plasma concentrations of lipids and apolipoproteins were not significantly different from baseline levels before or after the administration of SPI or casein supplemented diets. Neither SPI nor casein supplement affected the fasting plasma concentrations of lipids and apolipoproteins. The areas under the incremental curve (AUIC) of triglyceride (TG) and remnant-like particles triglyceride (RLP-TG) after both experimental diets were not significantly different from those before the experimental diets. However, the AUIC of remnant-like particles cholesterol (RLP-C) showed a tendency (p = 0.07) to decrease after administration of the diet supplemented with SPI than before the diet. The AUIC of RLP-C was significantly (p < 0.05) lower after the diet supplemented with SPI than after administration of the diet supplemented with casein. These results suggest that 3 weeks of 20 g/d SPI dietary supplement favorably affects the postprandial remnant lipoprotein response as compared to the casein dietary supplement.

Adult↗
PubMed1992

Absorption of oligo-L-[35S]methionine after feeding of a low casein or a low soybean protein isolate diet in rats.

We studied the absorptive properties of oligo-L-methionine (OM), which is an enzymatically synthesized and slowly digestible peptide. Previously, we demonstrated that when OM was added to a low casein diet, the improvement of the body weight gain was higher than when OM was added to a low soybean protein isolate (SPI) diet and we suggested that the difference in the supplementary effect of OM depends on its absorptive rate. In the present study, the OM absorption estimated by the portovenous difference in radioactivity derived from 35S-labeled OM was higher in the casein diet than in the SPI diet in early stages of feeding after fasting. Absorbed OM was quantified by subtracting the radioactivity of [35S]OM remaining in the whole gut from the ingested [35S]OM, 90 and 180 min after feeding casein and SPI diets containing 3% [35S]OM. We also estimated the absorptive efficiencies by subtracting the amount of radioactivity remaining in the intestines from the amount of [35S]OM emptied from the stomach as percentages of the emptied OM. Both the amount of absorbed OM and absorptive efficiencies of OM were higher in the casein group than in the SPI group, and the higher absorptive efficiency in the casein group indicates a higher digestibility for OM when rats are fed a 3% OM diet after fasting. The digestibility of [35S]OM measured by fecal excretion of radioactivity of OM during normal feedings for diets containing 0.3% [35S] OM for 7 days was about 80% in the casein group and 60% in the SPI group. We conclude that the different supplementary effects of OM in the low casein and SPI diets depend on the difference in OM digestibility. The difference in the digestibility of OM may partly depend on the faster absorption rate of OM in the early stages of feeding.

Animals↗