[Classification of infant foods based on cow milk protein. Milk foods for mature born healthy infants in the first half-year of life].
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Germany, West↗
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Biochemical properties of peptides encrypted in bovine milk proteins.
Milk proteins are precursors of many different biologically active peptides. These peptides are inactive within the protein sequence, requiring enzymatic proteolysis for release of the bioactive fragment from the proteins precursor. It is evident that activated peptides originating from milk proteins should be taken into account as potential modulators of various regulatory processes in the body. Activated peptides are potential modulators of various regulatory processes in the living system: immuno-modulatory peptides stimulate the activities of cells of the immune system and several cytomodulatory peptides inhibit cancer cell growth, antimicrobial peptides kill sensitive microorganisms, angiotensin-I-converting enzyme (ACE)-inhibitory peptides exert an hypotensive effect, opioid peptides are opioid receptor ligands which can modulate absorption processes in the intestinal tract, mineral binding peptides may function as carriers for different minerals, especially calcium, antithrombotic peptides inhibit fibrinogen binding to a specific receptor region on the platelet surface and inhibit aggregation of platelets. Moreover, many milk-derived peptides reveal multifunctional properties, i.e. specific peptide sequences having two or more different biological activities have been reported. Bioactive peptides can interact with target sites (e.g. receptors, enzymes) at the luminal side of the intestinal tract, or they could be absorbed and reach any potential site of action in the system to elicit physiological effects. Bioactive peptides encrypted in bovine milk proteins can be produced on an industrial-scale and are claimed to be health enhancing components for functional foods, nutraceuticals and pharmaceutical preparations that are used to reduce risk of disease or to enhance certain physiological functions.
Angiotensin-Converting Enzyme Inhibitors↗
Evaluation of a colostrum supplement, with or without trypsin inhibitor, and an egg protein milk replacer for dairy calves.
Forty-eight Holstein bull calves were assigned to a 2 x 2 x 2 factorial arrangement in a completely randomized block design. Main effects were colostrum versus a serum-derived colostrum supplement, 0 versus 1 g of trypsin inhibitor added at the initial 2 feedings, and milk replacer containing 0 or 50% CP from whole egg. Calves were bled at 0, 6, 12, 18, and 24 h after birth for determination of serum immunoglobulin (Ig). G. Serum IgG concentrations were lower in calves consuming the colostrum supplement compared with calves consuming colostrum. Apparent efficiency of absorption of IgG was similar. Trypsin inhibitor did not affect IgG concentrations or absorption of IgG. Calves were fed either milk replacer for 28 to 35 d (preweaning phase) and weaned when they consumed 0.7 kg of starter grain for 2 consecutive days. The postweaning phase was from weaning to d 56. Feeding colostrum supplement resulted in higher fecal scores postweaning (1.90 vs. 1.58) and overall (1.85 vs. 1.65) and fewer days medicated preweaning (5.1 vs. 2.2 d) and postweaning (3.9 vs. 1.9 d) and overall (9.0 vs. 4.2 d). Calves were treated for upper respiratory tract infections and diarrhea. Dry matter intake and weaning age were not affected by treatment. Postweaning (1.69 vs. 1.2 kg) and overall (1.22 vs. 1.0 kg), calves that received colostrum and egg milk replacer consumed more dry matter and starter. Postweaning, calves fed colostrum and egg milk replacer had similar or greater body weight and gains compared with calves fed colostrum and milk protein milk replacer. Preweaning, feed efficiency was greater for calves fed colostrum (0.44 vs. 0.34), trypsin inhibitor (0.42 vs. 0.36), and milk protein milk replacer (0.48 vs. 0.30) compared with calves fed colostrum supplement, no trypsin inhibitor, and egg milk replacer, respectively. Trypsin inhibitor increased feed efficiency postweaning. Calves fed trypsin inhibitor and milk protein milk replacer were more efficient preweaning and overall than calves fed trypsin inhibitor and egg milk replacer. Results indicate that the blood derived colostrum supplement did not provide as much IgG as colostrum (4.55 g/L vs. 14.6 g/L, respectively), that feeding 1.0 g of trypsin inhibitor did not enhance serum IgG concentrations, and that the egg milk replacer-fed calves fed colostrum performed nearly as well as calves fed colostrum and the milk protein milk replacer.
Absorption↗
[Bioactive peptides derived from milk proteins].
Milk proteins are known for having a wide range of nutritional, functional and biological properties that make them important ingredients in functional or health promoting foods. These properties are partly attributed to bioactive peptides coded in the different milk proteins. Bioactive peptides are inactive within the protein sequence but may be released by the action of native proteolitic enzymes from milk, enzymes from lactic acid bacteria or from exogenous sources or may be produced during gastrointestinal digestion or processing of foods. Peptides derived from caseins and whey proteins were shown to present several bioactive properties such as opioid, antihypertensive, antimicrobial, immunodulatory, mineral carrier and antithrombotic. This overview presents a perspective of the importance of dairy proteins in the production of bioactive peptides and their biological activities, as well as the main analytical tecniques that have been used for the isolation and identification of these peptides.
Milk Proteins↗
Effect of milk protein genotypes on milk protein composition and its genetic parameter estimates.
The effects of kappa-casein (CN) and beta-lactoglobulin (LG) genotypes on milk protein concentration and composition were estimated for the US Holstein-Friesian population using a single-trait, mixed, linear animal model on 592 individual milk samples from 233 cows. Both milk protein genotypes had no statistically significant effect on the total milk protein concentration; however, substitution of the kappa-CN A allele additively increased the proportion of kappa-CN, and substitution of the beta-LG B allele additively increased the proportion of beta-LG in total milk protein. In response, proportions of the other milk proteins, mainly alpha S1-CN, were decreased. For proportions of alpha S1-CN, kappa-CN, and beta-LG in total milk protein, kappa-CN and beta-LG genotypes explain more than 50 and 25% of the heritability and repeatability estimates, respectively. We concluded that kappa-CN and beta-LG genotypes affect the phenotypic and genetic variation of milk protein composition but do not significantly affect milk protein concentration. A possible explanation for our conclusion is that altered gene sequences in the promoter region of kappa-CN B and beta-LG A, linked closely to the respective genotypes, favor the transcription or translation of their own protein at the expense of the synthesis of other milk proteins, in particular of alpha S1-CN.
Alleles↗
Nitrogen balance response in young men given one of two isolated soy proteins or milk proteins.
The protein nutritional value of two isolated soy proteins was compared with that of dried skim milk proteins in healthy young men. Eight subjects received one of the isolated soy proteins and six subjects received the dried skim milk as the test protein source. Each protein was tested at intakes of 0.35, 0.45, 0.55 and 0.65 g protein (N X 6.25) per kilogram per day during 10-day diet periods separated by break periods of 3 days and a 1-day protein-free period. Nitrogen balances were determined for the final 5 days of each experimental diet period. From regression analysis of nitrogen intake minus nitrogen output data, intakes of each protein source to meet mean nitrogen requirements were 124, 146 and 144 mg N/kg per day for the two isolated soy proteins and skim milk protein, respectively. It is concluded that well-processed isolated soy proteins are indistinguishable from milk as a protein source for maintenance of short-term N balance in adult human nutrition.
Adolescent↗
Blood antigen, serum protein, and milk protein gene frequencies and genetic interrelationships in Holstein cattle.
Gene frequencies at ten blood group loci, one serum protein locus, and four milk protein loci were determined for the Holstein-Friesian breed in the United States. The sample consisted of 8630 cows in 51 herds from 10 states. Because of the close linkage among casein subloci and the concimitant rarity of crossover-recombinant groups, casein gene combination or haplotype frequencies were determined also. As one means of comparison of systems, indices of homozygosity and number of effective alleles were calculated. These indices were proposed also to be useful tools for monitoring changes in genetic variability of breeds. Genotypes within codominant systems and phenotypes associated with paired-system combinations generally were not randomly occurring. Paired system phenotypes within the sire sample corresponded much more closely to expectations of randomness.
Alleles↗
[State of milk protein contained in milk-protein-rich powders and medicinal preparations; an appeal for verification of the value or worthlessness of milk-protein admixture].
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Animals↗
Plant proteins in milk replacers for rearing buffalo calves. I. Effect of replacing half of the milk proteins by plant proteins on the preweaning performance of buffalo calves.
In an experiment, 12 female and 8 male buffalo calves aged 3 to 4 weeks with an average of 65.2 kg live body weight were divided into 4 equal groups. Group 1 received dried skim milk plus non-milk fat. In groups 2, 3, and 4, 50% of the milk protein were replaced by American soybean flour, Egyptian soya meal, or corn glutine. Scouring occurred in all groups during the first three weeks. Death losses occurred in group 2 (2 calves) and 4 (1 calf). During the first three experimental weeks the calves consumed on average 828, 868, 847, 696 g dry matter (DM) as liquids. The average daily gain (ADG) was 229, 215, 252, 48 g/d, respectively. The energy consumption reached 4.1, 4.6, 3.8, 16.6 TDN/kg ADG. During the second period, the calves consumed 1.57, 1.45, 1.55, 1.65 kg DM as liquid and solid feedstuff. Up to a live body weight of 90 kg they had a daily increase of 695, 611, 593, 600 g. The energy used amounted to 1.98, 2.08, 2.28, 2.40 TDN/kg ADG. The apparent digestibility of the crude protein was 95, 92, 91, 92% during the first period and 81, 77, 76, 73% during the second period.
Animal Feed↗
Plant protein in milk replacers for rearing buffalo calves. II. Effect of replacing 75% of the milk proteins by plant proteins on the preweaning performance of buffalo calves.
In an experiment, 9 female and 6 male buffalo calves at the age of 3 to 4 weeks were divided into 3 groups. The animals were given milk replacers in which 75% of the dried skim milk protein had been replaced by American soybean flour (ASP), Egyptian soya meal (ESP), or corn glutine (GP). Scouring occurred in all groups during the first 3 weeks of the experiment, continuing up to the fourth week in groups ESP and GP. In groups ESP and GP one calf each died. During the first 3 weeks of the experiment, the calves consumed on average 747, 631, 787 g dry matter (DM) as liquids. They achieved live weight gains of 314, 83, -286 g/d, with significant differences between the groups. The digestibility of the crude protein was 73, 74, 70%. During the second period--up to 70 or 62.5 kg live body weight--only groups ASP and ESP were investigated. The calves consumed 1.64 or 1.66 kg DM/d as liquid and dry feedstuff. The average daily weight gain was 3.87 or 3.50 TDN/kg ADG. During this period, the crude protein was digested by 76 or 73%.
Animal Feed↗
[Comparative studies on premature infant nutrition with human milk, lactose protein milk, lactose fat milk and acid 2/3 milk].
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Female↗
Antibody response to milk proteins in patients with milk-protein intolerance documented by challenge.
To evaluate the role of specific antibody response to milk proteins in patients with milk-protein intolerance, allergen-specific IGE, IgG, and IgG4 to these proteins were measured by ELISA. Bovine casein, gamma globulin (GG), beta-lactoglobulin, and lactalbumin were the milk proteins used. Antibody production to these proteins were analyzed in 18 patients who underwent milk-protein challenges (eight positive and 10 negative) and in five normal children used in the analysis. ELISA results for specific IgE, IgG, and IgG4 to these specific proteins demonstrated no statistically different response to the four milk proteins among the three patient groups by multivariate analysis. When the specific antibody results from the positive challenge group, the negative challenge group, and the normal group were combined, the IgE and IgG4 to GG and the IgG to casein were significantly higher (p less than 0.01) than the corresponding specific antibody to the other proteins tested. The IgG or IgG4 to GG would differentiate the positive from the negative challenge group (p less than 0.05) but were not significantly different from the normal control group. Contrary to previously published studies, these results indicate IgG specific for the milk proteins are not increased in patients with milk-protein intolerance. The data also support the concept that IgE and IgG4 are not elevated in these patients. Therefore, there appears to be no pathogenic role for these specific immunoglobulins in milk-protein intolerance.
Antibody Formation↗
Effect of psychrotrophic bacteria from raw milk on milk proteins and stability of milk proteins to ultrahigh temperature treatment.
The effects of psychrotroph growth in raw milk on proteins of mils and on the response of milk proteins to heat treatments with ultrahigh temperature were studied. Ten gram-negative psychrotrophs isolated from raw milk readily attacked raw milk proteins. Kappa- and beta-casein were most susceptible although some of the isolates also attacked the whey proteins. Detectable proteolysis did not require large psychrotroph populations. A 10 to 20% decrease in kappa-casein during 2 days at 5 C accompanied growth of one isolate to a population of only 10,000/ml. Growth of psychrotrophs in raw milk predisposed the proteins to deleterious effects of ultrahigh temperature treatments. Ultrahigh temperature treatment by direct steam injection had little effect on raw milk caseins and decreased alpha-lactalbumin and beta-lactoglobulin by 21% and 34%, respectively. Milk that had undergone proteolysis exhibited decreased detectable kappa-, beta-, and alphas-caseins and increased loss of beta-lactoglobulin as a result of ultrahigh temperature treatment. Milk suffering extensive kappa-casein degradation coagulated during ultrahigh temperature treatment. Coagulation during or shortly after heating increased with severity of heat treatment and size of psychrotroph population.
Animals↗
Associations between milk protein polymorphisms and milk production traits.
Associations between milk protein genotypes and milk production traits were estimated from 6803 first lactation records. Exact tests of associated hypotheses and unbiased estimates of genotype effects were from an animal model. Milk protein genotype effects were estimated using a model in which each milk protein gene was analyzed separately (single-gene analysis) and a model in which all milk protein genes were analyzed simultaneously (multigene analysis). The results of the two models indicate that some effects ascribed to certain milk protein genes in the single-gene analysis are not effects of the milk protein gene itself but of linked genes. Results from this study and from literature indicate that the kappa-casein gene or a very closely linked gene affects protein percentage, and the beta-lactoglobulin gene or a very closely linked gene affects fat percentage. Furthermore, effects of beta-casein genotypes on milk production, fat percentage, and protein yield were significant, and beta-lactoglobulin genotypes had significant effects on milk production and protein yield. It is less clear whether those effects are due to effects of milk protein genes themselves or to effects of linked genes.
Animals↗
Growth and metabolic responses in low-birth-weight infants fed human milk fortified with human milk protein or with a bovine milk protein preparation.
Unfortified human milk does not normally provide enough protein to secure maximal growth in low-body-weight (LBW) infants. Due to the practical difficulties in obtaining human milk protein (HMP), a bovine milk protein preparation (BMP) was designed by computer calculation to contain as close as possible the amino acid composition of the nutritionally available human milk proteins. Twenty-one AGA, LBW infants (BW of 1,180 to 1,600 g, GA of 27 to 33 weeks) were randomly assigned to be fed HM enriched either with HMP (9 infants) or BMP (12 infants). When full volume intake (170 ml/kg/day) was reached, the protein intakes were 3.6 +/- 0.5 and 3.3 +/- 0.3 g/kg/day, respectively, in the two diet groups. During the study period of 24 days, the infants achieved intrauterine or better weight gains: 32.9 +/- 3.3 g/day (17.7 +/- 1.9 g/kg/day) in the HMP group and 34.7 +/- 7.3 g/day (18.3 +/- 3.5 g/kg/day) in the BMP group. Serum urea nitrogen, acid-base status, and albumin values were normal and similar in both groups of infants. Plasma concentrations of total essential and total amino acids at the end of the study were 3,999 and 1,539 mumol/L and 3,899 and 1,422 mumol/L in the HMP and the BMP groups, respectively. The concentrations of all individual plasma amino acids were similar in both feeding groups. These results show that feeding human milk fortified with a modified bovine milk protein preparation produces satisfactory growth and a plasma amino acid profile similar to that found in LBW infants fed exclusively human milk protein at similar intakes.
Acid-Base Equilibrium↗
Prolactin signalling to milk protein secretion but not to gene expression depends on the integrity of the Golgi region.
Prolactin added to the incubation medium of lactating mammary epithelial cells is transported from the basal to the apical region of cells through the Golgi region and concomitantly stimulates arachidonic acid release and protein milk secretion. We report that when PRL is added after disorganisation of the Golgi apparatus by brefeldin A treatment, prolactin signalling to expression of genes for milk proteins and prolactin endocytosis are not affected. However, prolactin transport to the apical region of cells (transcytosis), as well as prolactin-induced arachidonic acid release and subsequent stimulation of the secretion of caseins, which are located in a post-Golgi compartment, are inhibited. This inhibition was not a consequence of damage to the secretory machinery, as under the same conditions, protein secretion could be stimulated by the addition of arachidonic acid to the incubation medium. Thus, it is possible to discriminate between prolactin-induced actions that are dependent (signalling to milk protein secretion) or independent (signalling to milk gene expression) on the integrity of the Golgi apparatus. These results suggest that these two biological actions may be transduced via distinct intracellular pathways, and support the hypothesis that prolactin signals may be emitted at various cellular sites.
Animals↗
Compared with casein or total milk protein, digestion of milk soluble proteins is too rapid to sustain the anabolic postprandial amino acid requirement.
BACKGROUND: The in vivo quality of milk protein fractions has seldom been studied in humans. OBJECTIVE: Our objective was to compare the postprandial utilization of dietary nitrogen from 3 [(15)N]-labeled milk products: micellar caseins (MC), milk soluble protein isolate (MSPI), and total milk protein (TMP). DESIGN: The macronutrient intakes of 23 healthy volunteers were standardized for 1 wk, after which time the subjects ingested a meal containing MC (n = 8), MSPI (n = 7), or TMP (n = 8). [(15)N] was measured for an 8-h period in plasma amino acids, proteins, and urea and in urinary urea. RESULTS: The transfer of dietary nitrogen to urea occurred earlier after MSPI ingestion than after MC and TMP ingestion, and concentrations remained high for 8 h, concomitantly with higher but transient hyperaminoacidemia and a higher incorporation of dietary nitrogen into plasma amino acids. In contrast, deamination, postprandial hyperaminoacidemia, and the incorporation of dietary nitrogen into plasma amino acids were lower in the MC and TMP groups. Finally, total postprandial deamination values were 18.5 +/- 2.9%, 21.1 +/- 2.8%, and 28.2 +/- 2.9% of ingested nitrogen in the TMP, MC, and MSPI groups, respectively. CONCLUSIONS: Our results confirm the major role of kinetics in dietary nitrogen postprandial utilization and highlight the paradox of MSPI, which, despite its high Protein Digestibility Corrected Amino Acid Score, ensures a rate of amino acid delivery that is too rapid to sustain the anabolic requirement during the postprandial period. Milk proteins had the best nutritional quality, which suggested a synergistic effect between soluble proteins and caseins.
Adult↗
PEANUT PROTEIN AND MILK PROTEIN BLENDS IN THE TREATMENT OF KWASHIORKOR.
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Arachis↗