Tryptophan intake influences infants' sleep latency.

Formula-fed infants have depressed plasma tryptophan concentration relative to human milk-fed infants. Because tryptophan alters sleep-waking patterns in adults, a study was designed to determine whether additional dietary tryptophan could elevate plasma tryptophan concentrations of formula-fed infants to concentrations characteristic of human milk feeding and whether differences in plasma tryptophan or the ratio of plama tryptophan to the sum of the other plasma large neutral amino acids (tryptophan:LNAA) were of behavioral significance. Infants were fed a formula (13 g protein/L; whey:casein, 34:66) containing either 0, 294, 588 or 882 mumol/L of added tryptophan. Infants fed human milk or commercial formula (15 g protein/L; whey:casein, 18:82) were included for comparison. In formula-fed groups, plasma tryptophan was directly related to tryptophan intake (r = 0.46, P less than 0.0005). Infants fed commercial formula or the formula without added tryptophan had lower (P less than 0.001) plasma tryptophan compared with infants fed human milk. Only the infants fed the highest tryptophan formula had significantly higher plasma tryptophan:LNAA ratios than the other experimental groups, and these ratios were similar to those of infants fed human milk. The plasma tryptophan:LNAA ratios, not plasma tryptophan concentrations, were predictive of differences in the infants' sleep latency; infants fed formula containing the highest tryptophan had sleep latencies of 18.7 min, significantly shorter (P less than 0.05) than those of infants fed formulas containing less added tryptophan (27.7 min). Feeding infants formulas differing in tryptophan concentration produced differences in sleep latency, which could influence neurobehavioral developments.(ABSTRACT TRUNCATED AT 250 WORDS)     

The importance of alpha-lactalbumin in infant nutrition

The ideal "humanization" of milk substitutes should include the creation of an amino acid pattern closely resembling that of human milk. Because the mixture of proteins in human milk is particularly rich in tryptophan and cysteine and low in methionine, this pattern is difficult to achieve with commercially available proteins. Even whey-predominant formulas only approximate human milk. Human milk has a high concentration of whey protein (70% of total protein). Of this, alpha-lactalbumin, a component of the lactase synthetase complex, accounts for 41% of the whey and 28% of the total protein. Only 3% of the protein in bovine milk is alpha-lactalbumin. Human and bovine alpha-lactalbumin share a 72% amino acid sequence homology. Both proteins contain (wt/wt) 6% tryptophan and 5% cysteine but only 0.9% methionine. Thus the differences in the amino acid compositions of bovine and human milks are largely attributable to differences in their alpha-lactalbumin contents. Commercial availability of bovine alpha-lactalbumin would allow the construction of infant formulas with amino acid compositions that are very close to that of human milk. alpha-Lactalbumin would also be a valuable constituent of diets for patients whose protein intake must be restricted.     

Phenylalanine kinetics differ between formula-fed and human milk-fed preterm infants

Infants fed casein-dominant formulas have higher plasma phenylalanine and tyrosine concentrations than those fed mother's milk. Conversely, elevated plasma threonine concentrations are observed in infants fed whey-dominant formulas. We recently showed that formula-fed preterm infants have a lower capacity to degrade threonine than do preterm infants fed mother's milk. We hypothesized that these same infants (n = 18) would differ in their catabolism of phenylalanine in response to phenylalanine loads provided by formulas with increasing casein content of formulas (whey:casein 60:40, 40:60, and 20:80) compared with preterm infants fed mother's milk. Plasma phenylalanine concentrations significantly rose (49, 46, 79 micromol . L(-1) for whey:casein 60:40, 40:60, and 20:80, respectively, pooled SD 8, P < 0.05); and plasma phenylalanine concentrations in infants fed mother's milk were low (40 +/- 4 micromol . L(-1)). Using [1-(13)C]phenylalanine tracer and (13)CO(2) production in breath we found that although there was a significant positive relation between phenylalanine oxidation and phenylalanine intake in formula-fed infants (r(2) = 0.43, P = 0.03), these infants were not able to increase their oxidation of phenylalanine enough to prevent a significant rise in plasma phenylalanine when fed the 20:80 formula. Compared to infants fed mother's milk, formula-fed infants had significantly lower phenylalanine oxidation (39.1 vs. 30.7% of phenylalanine intake, respectively, P < 0.05). We conclude that one of the mechanisms for the differences in plasma amino acid concentration between formula-fed and mother's milk-fed preterm infants may be in vivo down-regulated catabolism of 2 important essential amino acids (phenylalanine in addition to threonine) in formula-fed preterm infants.     

Effects of alpha-lactalbumin-enriched formula containing different concentrations of glycomacropeptide on infant nutrition

BACKGROUND: Formula-fed infants have growth and plasma amino acid patterns different from those of breastfed infants. OBJECTIVE: alpha-Lactalbumin is a major protein in human milk, and the addition of bovine alpha-lactalbumin to infant formula has been proposed to modify the plasma amino acid pattern of the recipient infant, possibly allowing a reduction in the protein content of the formula, which may affect growth. DESIGN: We compared breastfed infants and infants fed standard formula or alpha-lactalbumin-enriched formulas (25% of protein) with glycomacropeptide accounting for 15% or 10% of the protein. The protein content of each formula was 13.1 g/L. Ninety-six infants aged 6 +/- 2 wk were recruited. Anthropometric measures were recorded, and interviews were conducted at enrollment and monthly until 6 mo of age. Blood samples were collected at enrollment and at 4 and 6 mo. RESULTS: Formula intake did not differ between groups, and weight gain in the alpha-lactalbumin-enriched formula groups were similar to that of the breastfed infants. The standard formula group gained significantly more weight than did the breastfed infants. All formula-fed infants had significantly higher plasma concentrations of most essential amino acids at 4 and 6 mo than did the breastfed infants, and serum urea nitrogen was also higher in the formula-fed infants. Insulin and leptin concentrations did not differ between groups. CONCLUSIONS: Compared with standard formula-fed infants, infants fed formula with a modified protein composition had growth patterns more similar to those of breastfed infants. All formula-fed groups had plasma amino acid concentrations similar to or higher than those of breastfed infants. This indicates that the protein content of alpha-lactalbumin-enriched formula can be further reduced, which should be evaluated.     

Casein content of human milk

Three methods for estimating the casein content of human milk were tested; isoelectric precipitation with washing and correction for co-precipitating proteins, sedimentation by ultracentrifugation, and indirect analysis (ie analyzing for the content of the major whey proteins and subtracting these from the total protein content). Gel electrophoresis and amino acid analysis were used to confirm some of the results. The casein content (mg/ml) of mature human milk (n = 9) was 2.33 +/- 1.69 by isoelectric precipitation, 1.80 +/- 0.48 by sedimentation and 2.96 +/- 1.08 by the indirect approach. A probable partition of nitrogen in breast milk would be casein N: whey protein N: non-protein N of 20:50:30; ie the correct ratio of casein nitrogen: whey nitrogen is approximately 20:80. Analysis of trace elements and minerals demonstrates that of total Ca 10%, Mg 5%, Zn 28%, Cu 17%, and Fe 27% is bound to casein when prepared by ultracentrifugation while isoelectric precipitation causes a redistribution of some of these elements. Since the protein ratio of human milk is considered a guideline when manufacturing infant formulas, these findings should be considered with regard to infant nutrition.     

Glycomacropeptide and alpha-lactalbumin supplementation of infant formula affects growth and nutritional status in infant rhesus monkeys

BACKGROUND: Advances in dairy technology make it possible to enrich infant formula with specific bovine milk components that may enhance nutrient status. Glycomacropeptide, a carbohydrate-rich casein peptide, may increase absorption of calcium, iron, or zinc. alpha-Lactalbumin, a major breast-milk protein, may contribute to a balanced amino acid pattern and increase calcium and zinc absorption. OBJECTIVE: We determined the effects of glycomacropeptide- and alpha-lactalbumin-supplemented infant formula on growth; trace mineral status; iron, zinc, and calcium absorption; and plasma amino acid, blood urea nitrogen, and plasma insulin concentrations. DESIGN: Infant rhesus monkeys (n = 5 infants per group) were breastfed or fed control or alpha-lactalbumin- or glycomacropeptide-supplemented formula from birth to 4 mo of age. Hematologic measures and growth were assessed monthly. Mineral absorption was measured with radioisotopes and whole body counting. RESULTS: Infants fed glycomacropeptide had higher food intake than did other formula-fed infants. Infants fed glycomacropeptide or control formula had higher hematocrit values than did infants that were breastfed or fed alpha-lactalbumin. Infants fed glycomacropeptide or control formula had higher plasma zinc and zinc absorption than did breastfed infants. Where differences were observed, breastfed infants and infants fed alpha-lactalbumin had similar plasma essential amino acid and insulin profiles, which were different from those of infants fed glycomacropeptide or control formula. CONCLUSIONS: Glycomacropeptide- or alpha-lactalbumin-supplemented formula has no adverse effects on nutritional status in infant monkeys. Glycomacropeptide supplementation increases zinc absorption, which may permit the reduction of formula zinc concentrations, and alpha-lactalbumin supplementation promotes a plasma amino acid pattern similar to that of breastfed infant monkeys.     

Protein evaluation in growing rats of breast milk and breast milk substitutes with special reference to the content of non-protein nitrogen.

The levels of individual proteins and other nitrogen containing substances differ considerably between cow's milk and human milk. Therefore, during manufacture of infant formulas, attempts are made to simulate the protein composition of human milk. However, the composition and nutritional characteristics of human milk protein are incompletely known. In this paper, the protein quality of breast milk protein with and without the non-protein-nitrogen (NPN) substances present in human milk was studied with growing rats and compared to two formulas, one "adapted" commercial infant formula and a suggested further modified, possibly improved, infant formula. Detailed examinations of protein and amino acid composition of the test diets are given. Breast milk protein with added NPN substances showed a lower protein quality than all other test proteins. Breast milk protein without NPN substances and the protein of the suggested infant formula were of similar quality while the protein of the commercial adapted formula was significantly better than all other test proteins. The use of rat growth assays in the evaluation of protein quality of infant formulas is discussed.     

Effects of pH variation and NaCl on in vitro digestibility of cow's milk proteins in commercially available infant formulas

Allergenicity and antigenicity of food proteins are generally dependent on their heat-stability and resistance to digestive enzymes. Using the methods of SDS-PAGE and immunoblots, we assessed peptic-digestibility of major milk proteins (casein, beta-lactoglobulin and alpha-lactalbumin) in commercially available infant formulas in acidic pH range (pH 1.5 to 4.0), and we also investigated the effect of NaCl on peptic-digestibility of cow's milk proteins at pH 2.0. The profile of peptic-digestion of casein was similar at pH range from 1.5 to 3.5 where the intact protein of casein rapidly disappeared, whereas slow digestibility of the protein was found at pH 4.0. Beta-lactoglobulin and alpha-lactalbumin were digested at pH range from 1.5 to 2.5 and were almost entirely resistant to peptic digestion at over pH 3.0. In the presence of NaCl at pH 2.0, casein showed a good digestibility by pepsin similar to that in the absence of NaCl, in contrast to beta-lactoglobulin and alpha-lactalbumin both having their peptic-digestibility decreased in the presence of 0.2 M NaCl. As the state of the stomach in new born infants shows low amounts of secretary pepsin and out of optimum pH of peptic activity, low digestibility of beta-lactoglobulin and alpha-lactalbumin in cow's milk based infant formulas at over pH 3.0 is supposed to be responsible for their allergenicity.     

Unequal distribution of a stable isotopic calcium tracer between casein and whey fractions of infant formulas, human milk and cow's milk

Measurement of calcium absorption with tracers assumes a complete equilibration of tracer with milk calcium. In this study, the equilibration of tracer between the micellar casein and soluble fractions (primarily whey) of infant formulas, human milk and cow's milk was measured in vitro using milk samples enriched with 42Ca and analyzed by thermal ionization mass spectrometry. Incomplete equilibration of tracer occurred with the micellar casein fraction of all milks. The least equilibration with micellar casein was found with premature infant formula, for which the ratio of slopes of the equilibration lines (whey/casein) was 8.5/1. These differences may be due to Ca-casein binding in cow's milk-based formulas. The effects of the lack of tracer equilibration in vivo cannot be determined. However, unequal bioavailability of casein- vs. whey-bound Ca may exist.     

Amino acid composition determined using multiple hydrolysis times for three goat milk formulations

The amino acid composition of goat milk formulations with varying protein and carbohydrate concentrations were determined. Proteins in goat milk infant formula, goat milk growing-up formula and goat whole milk powder were hydrolysed using multiple hydrolysis time intervals. A least-squares non-linear regression model was used to predict the free and protein bound amino acid concentrations. The amino acid composition of goat infant formula was compared with human milk reference values. There was good agreement between the multiple hydrolysis and single 24-h hydrolysis methods for approximately one-half of the amino acids. Tryptophan, aspartic acid, threonine, tyrosine, isoleucine, valine, serine and alanine contents were underestimated by 10.6, 5.6, 5.6, 4.7, 4.4, 3.7, 3.7 and 3.6%, respectively, by the single 24-h hydrolysis. The study provides accurate reference data on the amino acid composition of goat milk powders. Goat milk infant formula has amino acids in amounts similar to human milk reference values, when expressed on a per-energy basis.     

Reduction in the antigenicity of whey proteins by heat treatment: a possible strategy for producing a hypoallergenic infant milk formula

Residual antigenic protein in heat-denatured cow's milk whey and in two commercial infant milk formulas was determined using enzyme-linked immunosorbent assays specific for beta-lactoglobulin, alpha-lactalbumin, bovine serum albumin, bovine IgG1 and alpha-casein. This immunochemical assessment of antigenicity was related to the capacity of the preparations to sensitize immunologically when fed to guinea-pigs for 2 weeks. Antibody production was measured and the susceptibility of the animals to systemic anaphylaxis was assessed by injecting them intravenously with heated or unheated milk proteins. Whey protein that had been heated at 100 degrees or 115 degrees for 30 min was extensively denatured and, in contrast to pasteurized whey, failed to sensitize guinea-pigs for anaphylaxis. Antibody production was undetected or very low. The proteins in SMA powder and SMA Gold Cap liquid concentrate were less denatured and animals given these formulas prepared according to the maker's instructions produced relatively high levels of antibodies to beta-lactoglobulin and alpha-casein and a majority developed anaphylaxis when injected intravenously with these products. As well as failing to sensitize, whey that had received severe heat treatment did not, in most cases, elicit anaphylaxis when injected into animals that had been sensitized with unheated milk. Discrimination between antibodies of the IgG1 and IgG2 subclasses specific for beta-lactoglobulin showed that IgG1, the principal anaphylactic antibody in guinea-pigs, was preferentially depressed in animals drinking heat-denatured milk preparations. The results suggest that heat denaturation of whey protein may be a logical and simple strategy for producing a hypoallergenic baby milk. Nevertheless, the value of experiments in guinea-pigs for predicting results in man is uncertain and the proposal awaits assessment in clinical trials.     

Amino acid composition determined using multiple hydrolysis times for three goat milk formulations

The amino acid composition of goat milk formulations with varying protein and carbohydrate concentrations were determined. Proteins in goat milk infant formula, goat milk growing-up formula and goat whole milk powder were hydrolysed using multiple hydrolysis time intervals. A least-squares non-linear regression model was used to predict the free and protein bound amino acid concentrations. The amino acid composition of goat infant formula was compared with human milk reference values. There was good agreement between the multiple hydrolysis and single 24-h hydrolysis methods for approximately one-half of the amino acids. Tryptophan, aspartic acid, threonine, tyrosine, isoleucine, valine, serine and alanine contents were underestimated by 10.6, 5.6, 5.6, 4.7, 4.4, 3.7, 3.7 and 3.6%, respectively, by the single 24-h hydrolysis. The study provides accurate reference data on the amino acid composition of goat milk powders. Goat milk infant formula has amino acids in amounts similar to human milk reference values, when expressed on a per-energy basis.     

Substitution of casein by beta-casein or of whey protein isolate by alpha-lactalbumin does not affect mineral balance in growing rats

Bovine milk protein fractions that enable modification of the protein composition and amino acid profile of infant formulas to mimic those of human milk have recently become available. To determine the effects on protein quality and mineral bioavailability of replacing casein by beta-casein and of whey protein isolate by alpha-lactalbumin, 4 groups of growing rats were fed for 3 wk diets containing 10% protein as 1) casein (control); 2) beta-casein; 3) casein:whey (40:60); or 4) beta-casein:alpha-lactalbumin (40:60). Protein quality, determined as protein efficiency ratio (PER), net protein utilization (NPU), biological value (BV) and protein digestibility (PD), as well as body weight gain, were higher (P < 0.05) with consumption of the whey-adapted diets [casein:whey (40:60); beta-casein:alpha-lactalbumin (40:60)] compared with the casein diets (casein; beta-casein); however, there were no differences between the 2 casein diets or between the 2 whey-adapted diets. Apparent absorption of minerals (Ca, P, Fe, Zn) from the whey-adapted diets was higher than that from the casein diets (P < 0.05); but again, no differences were observed when casein or whey protein isolate were replaced by beta-casein or alpha-lactalbumin, respectively. Thus, substitution of casein by beta-casein or of whey protein isolate by alpha-lactalbumin does not affect protein quality or mineral bioavailability as determined in growing rats.     

Specialized formulas and feedings for infants with malabsorption or formula intolerance

The composition of specialized formulas for infants who experience malabsorption or formula intolerance is described in detail. The limited studies of efficacy, as well as a rationale for selecting an appropriate formula for infants with malabsorption or formula intolerance, are discussed. Infants with symptoms of diarrhea or emesis may have intolerance to milk lactose or milk protein. Soy formulas contain no lactose or cow's milk and should be the first choice of an alternative feeding because of cost and convenience. Some infants may be intolerant of soy as well as cow's milk protein. They benefit from formula containing neither cow's milk nor soy protein or from a specially processed milk-based formula containing hydrolyzed casein. A carbohydrate-free formula to which the desired type of carbohydrate is added may be helpful in the diagnosis and treatment of disaccharidase deficiencies and monosaccharide intolerances. Infants with extensive intestinal resections or intractable diarrhea may require specialized infant formulas with qualitative/quantitative modifications of fat, carbohydrate, and protein. Formulas with medium-chain triglycerides may be useful for infants with steatorrhea. "Preterm" formulas or milk from the infant's mother are preferred for preterm infants, since such feedings promote improved fat and carbohydrate absorption and better meet the infant's nutrient requirements.     

Concentration and distribution of sialic acid in human milk and infant formulas

BACKGROUND: In animal studies, sialic acid supplementation is associated with increases of gangliosides in the brain and improved learning ability. Only limited data are available on the sialic acid content of human milk and infant formulas. OBJECTIVE: We compared the concentrations of oligosaccharide-bound, protein-bound, and free sialic acid in milk from mothers of full-term and preterm infants and in a range of infant formulas. DESIGN: The milk from 20 and 14 mothers of full-term and preterm infants (mean gestational age: 31 +/- 3 wk), respectively, was collected at 4 stages of lactation (colostrum, transition, 1 mo, and 3 mo) and compared with 21 different infant formulas. RESULTS: Total sialic acid concentrations were highest in colostrum (x +/- SEM: 5.04 +/- 0.21 mmol/L in full term) and decreased by nearly 80% over the next 3 mo. Human milk from mothers of preterm infants contained 13-23% more sialic acid than did milk from mothers of full-term infants at 3 of the 4 lactation stages (P < 0.02). The sialic acid content of most formulas was <25% of that found in mature human milk (P < 0.01). Most of the sialic acid in the formulas ( approximately 70%) was bound to glycoproteins, whereas in human milk most sialic acid was bound to free oligosaccharides. CONCLUSIONS: Human milk, including milk from mothers of preterm infants, is a rich source of oligosaccharide-bound sialic acid, which contrasts with the relatively small amounts found in infant formulas. The nutritional significance of sialic acid is presently unknown, but it is plausible that it is a conditional nutrient that contributes to sialic acid accretion in the brain.     

Liquid concentrates are lower in bioavailable tryptophan than powdered infant formulas, and tryptophan supplementation of formulas increases brain tryptophan and serotonin in rats.

The bioavailability of tryptophan in powdered and/or liquid concentrate forms of milk-based infant formulas was determined by studying rat growth response by using a slope ratio method (food conversion efficiency: weight gain/food consumed vs. tryptophan consumed). A gelatin basal diet formulated to be adequate in all nutrients, except tryptophan (0.03%), for rat growth was supplemented with graded levels of crystalline L-tryptophan (0.02, 0. 04, 0.06, 0.08, 0.10, 0.12 and 0.14%, standard diets) or infant formulas providing 0.04 and 0.08% supplemental tryptophan (test diets). These diets were fed to weanling rats for 2 wk. Tryptophan bioavailabilities of various formulas varied from 83 to 95%, with some of the liquid concentrates having the lowest values. The levels of bioavailable tryptophan in the liquid concentrate forms (9.7-12.6 mg/g protein) and the powdered forms (11.1-13.1 mg/g protein) were considerably lower than those of human milk (17-19 mg/g protein). Supplementation of the liquid concentrates with graded levels of L-tryptophan (0.1, 0.5 and 1.0%) had no effect on protein quality indices, based on rat growth, but resulted in a dose-related increase in the concentrations of tryptophan in the plasma and brain and of serotonin and 5-hydroxyindole-3-acetic acid in the brains of rats. This study supports further research to investigate the influence of tryptophan supplementation of infant formulas, to more closely simulate tryptophan composition of human milk, on tryptophan metabolites and their potential related effects on sleep latency and neurobehavioral developments in infants.     

Nutritional evaluation of protein hydrolysate formulas in healthy term infants: plasma amino acids,hematology, and trace elements

BACKGROUND: Protein hydrolysate formulas are used for infants with food allergy. Most studies of such formulas focus on their effect on allergy and rarely evaluate their capacity to provide normal nutritional status. OBJECTIVE: We compared plasma aminograms, serum urea nitrogen, and trace element status in breastfed infants, infants fed hydrolysate formulas, and infants fed milk formula. DESIGN: From 6 wk to 6 mo of age, infants were breastfed or fed regular milk formula (RF), 1 of 2 casein-hydrolysate formulas (CH-1 or CH-2), or whey-hydrolysate formula (WH). Anthropometric measures were taken monthly, and blood samples were collected at 6 wk and 6 mo. Plasma amino acids, serum urea nitrogen, hematologic indexes, plasma zinc, and plasma copper were analyzed. RESULTS: There were no significant differences in hemoglobin, serum transferrin receptor, copper, or zinc among groups. Serum ferritin was significantly lower in infants fed the CH formulas than in the other groups. Infants fed CH-2 had significantly higher serum urea nitrogen than did all other groups. Plasma threonine, valine, phenylalanine, methionine, and tryptophan were significantly higher in the hydrolysate formula groups than in the breastfed group. Plasma tyrosine was significantly lower in infants fed the CH formulas than in the breastfed group, whereas arginine was significantly higher in the WH group than in all other groups. Plasma proline was lower, whereas threonine and tryptophan were higher, in the WH group than in the CH groups. CONCLUSIONS: The iron status of infants fed CH formula was lower than that of all other groups. The amounts of amino acids provided by hydrolysate formulas appear excessive compared with regular formula, which is reflected by high serum urea nitrogen (CH-2) and high plasma amino acid concentrations. A reduced and more balanced amino acid content of hydrolysate formulas may be beneficial.     

Manganese binding proteins in human and cow's milk

Manganese nutrition in the neonatal period is poorly understood, due in part to a lack of information on the amount of manganese in infant foods and its bioavailability. Since the molecular localization of an element in foods is one determinant of its subsequent bioavailability, we have studied the binding of manganese in human and cow's milk. An extrinsic label of 54Mn was shown to equilibrate isotopically with native manganese in milks and formulas. Milk samples were separated into fat, casein and whey by ultracentrifugation. In human milk, the major part (71%) of manganese was found in whey, 11% in casein and 18% in the lipid fraction. In contrast, in cow's milk, 32% of total manganese was in whey, 67% in casein and 1% in lipid. Within the human whey fraction, most of the manganese was bound to lactoferrin, while in cow's whey, manganese was mostly complexed to ligands with molecular weights less than 200. The distribution of manganese in formulas was closer to that of human milk than of cow's milk. The bioavailability of manganese associated with lactoferrin, casein and low molecular weight complexes needs to be assessed.     

Iron absorption in humans as influenced by bovine milk proteins

The effect of the two major bovine milk protein fractions on the dialyzability of iron in vitro under simulated gastrointestinal conditions and on the absorption of Fe by humans was studied. Liquid-formula meals were prepared from hydrolyzed maize starch, corn oil, and either spray-dried egg white or a milk-protein product. In meals containing egg white, 3.32% of the Fe was dialyzable. The substitution of casein and whey protein products reduced the dialyzable fraction to 0.19-0.56% and 0.86-1.60%, respectively. Percentage Fe absorption was also reduced by the substitution of casein or whey protein for egg white. Mean absorption values fell from 6.67 to 3.65% and 2.53 to 0.98%, respectively. When the intact milk-protein products were replaced by enzyme- or acid-hydrolyzed preparations, the dialyzable fraction increased markedly and in proportion to the extent of hydrolysis. A similar but much smaller effect on absorption was observed. These studies suggest that bovine casein and whey proteins are responsible at least in part for the poor bioavailability of the Fe in some infant formulas.     

Free amino acid content in standard infant formulas: comparison with human milk

OBJECTIVE: To compare the concentration of non-protein nitrogen (NPN) and free amino acids (FAA) in powdered and liquid commercial formulas with that in human milk. METHODS: The non-protein nitrogen and FAAs in pooled breast milk was compared with that in 11 protein-modified starting infant formulas (seven powdered, four liquid whey-predominant formulas) and one powdered soy-formula. Human milk was collected at the end of each feeding (hindmilk) over 24 hours in a group of 40 healthy lactating women after delivery of full-term infants at age one month. RESULTS: In human milk glutamic acid plus glutamine and taurine were the prevalent amino acids, accounting for around 50% total FAA. In the analysed formulas the total FAA fraction was 10% or even less than in human milk, mostly represented by taurine, while methionine was high in soy formula. The sum of glutamic acid and glutamine in all the formulas was much lower than in human milk. CONCLUSIONS: Breastfed infants are supplied with FAA, mainly glutamic acid and glutamine, compared to formula-fed counterparts. The different FAA intake might be the origin of some functional differences at the enteral level between breast- and formula-fed infants.