The effects of low and high frequency ultrasound on the production of volatile compounds along with their derivation and corresponding off-flavours in milk and milk products are discussed in this review. The review will simultaneously discuss possible mechanisms of applied ultrasound and their respective chemical and physical effects on milk components in relation to the production of volatile compounds. Ultrasound offers potential benefits in dairy applications over conventional heat treatment processes. Physical effects enhance the positive alteration of the physicochemical properties of milk proteins and fat. However, chemical effects propagated by free radical generation cause redox oxidations which in turn produce undesirable volatile compounds such as aldehydes, ketones, acids, esters, alcohols and sulphur, producing off-flavours. The extent of volatile compounds produced depends on ultrasonic processing conditions such as sonication time, temperature and frequency. Low frequency ultrasound limits free radical formation and results in few volatile compounds, while high ultrasonic frequency induces greater level of free radical formation. Furthermore, the compositional variations in terms of milk proteins and fat within the milk systems influence the production of volatile compounds. These factors could be controlled and optimized to reduce the production of undesirable volatiles, eliminate off-flavours, and promote the application of ultrasound technology in the dairy field.

Colostrum consists of a number of biologically active proteins and peptides that influence physiological function and development of a neonate. The present study investigated the biological activity of peptides released from first day bovine colostrum through in vitro and in vivo enzymatic digestion. This was assessed for proliferative activity using a human intestinal epithelial cell line, T84. Digestion of the protein fraction of bovine colostrum in vitro was conducted with the enzymes pepsin, chymosin and trypsin. Pepsin and chymosin digests yielded protein fractions with proliferative activity similar to that observed with undigested colostrum and the positive control foetal calf serum (FCS). In contrast trypsin digestion significantly (P<0·05) decreased colostral proliferative activity when co-cultured with cells when compared with undigested colostrum. The proliferative activity of undigested colostrum protein and abomasal whey protein digesta significantly increased (P<0·05) epithelial cell proliferation in comparison to a synthetic peptide mix. Bovine colostrum protein digested in vivo was collected from different regions of the gastrointestinal tract (GIT) in newborn calves fed either once (n=3 calves) or three times at 12-h intervals (n=3 calves). Digesta collected from the distal duodenum, jejunum and colon of calves fed once, significantly (P<0·05) stimulated cell proliferation in comparison with comparable samples collected from calves fed multiple times. These peptide enriched fractions are likely to yield candidate peptides with potential application for gastrointestinal repair in mammalian species.

CVD are the leading cause of death worldwide. Hypertension, a major controllable risk factor of CVD, is intimately associated with vascular dysfunction, a defect which is also now recognised to be a major, modifiable risk factor for the development of CVD. The purpose of the present review was to critically evaluate the evidence for the effects of milk proteins and their associated peptides on blood pressure (BP) and vascular dysfunction. After a detailed literature search, the number of human trials evaluating the antihypertensive effects of casein-derived peptides (excluding isoleucine-proline-proline and valine-proline-proline) was found to be limited; the studies were preliminary with substantial methodological limitations. Likewise, the data from human trials that examined the effects of whey protein and peptides were also scarce and inconsistent. To date, only one study has conducted a comparative investigation on the relative effects of the two main intact milk proteins on BP and vascular function. While both milk proteins were shown to reduce BP, only whey protein improved measures of arterial stiffness. In contrast, a growing number of human trials have produced evidence to support beneficial effects of both milk proteins and peptides on vascular health. However, comparison of the relative outcomes from these trials is difficult owing to variation in the forms of assessment and measures of vascular function. In conclusion, there is an accumulating body of evidence to support positive effects of milk proteins in improving and/or maintaining cardiovascular health. However, the variable quality of the studies that produced this evidence, and the lack of robust, randomised controlled intervention trials, undermines the formulation of firm conclusions on the potential benefits of milk proteins and peptides on vascular health.

Curcumin is a bioactive polyphenolic compound extracted from turmeric with known anti-inflammatory properties, and its hydrophobic nature restricts its solubility and its bioaccessibility. Solubility may be improved upon binding of curcumin to native or treatment-modified casein micelles. The present work demonstrated that high hydrostatic pressure treatment of skim milk increases the binding of curcumin to caseins. The association of curcumin to casein micelles was assessed using fluorescence spectroscopy, either directly or by tryptophan quenching. The amount of curcumin associated with the milk proteins increased in pressure-treated milk, and a further improvement in the amount of bound curcumin was observed upon pressure treatment of a milk/curcumin mixture. However, in this case, some of the curcumin dissociated during storage, contrarily to what was observed for untreated milk. From a molecular standpoint, the data presented here indicate that structural modifications induced by high-pressure treatment and known to affect the structure of milk proteins result in a rearrangement of the amino acid residues in close proximity to the protein-associated curcumin.

The polymorphism of six milk protein loci in five Cuban breeds was investigated by means of DNA analysis by combined techniques of PCR and amplification created restriction sites (ACRS), the method of allele-specific oligonucleotides (ASO), and restriction fragment length polymorphism (RFLP). Allele frequencies of loci CASA1, CASAB, CASA2, CASK, LAA and LGB were estimated in the five breeds (N = 324), the number of individuals per population being: Siboney de Cuba (SC = 85), Cuban Creole (CC = 60) Cuban Zebu (ZC = 61), Cuba Mambí (MC = 60) and Taíno of Cuba (TC = 58). Hardy–Weinberg equilibrium was estimated for each locus in each population, showing that all the populations have at least one locus deviated from this condition of equilibrium and always through heterozygote excess. Alleles CASA1C and LAAA were identified in the CC and CT breeds, showing the presence of Bos indicus genes in these populations. An increase of heterozygosis is observed in these populations, and genotype frequencies in each population allow differentiation of these from those which originated them.

The first months of life correspond to a key period in human life where dramatic physiological changes (establishment of microbiota, development of the immune system, etc.) occur. In order to better control these changes it is necessary to understand the behaviour of food in the gastrointestinal tract of the newborn. Infant formula is the only food for the newborn when breast-feeding is impossible. The kinetics of digestion of milk proteins and the nature of the peptides liberated in the small intestine throughout infant formula digestion have never been extensively investigated so far and were therefore studied using the piglet as a model of the newborn child. Piglets were fed infant formula by an automatic delivery system during 28 d, and slaughtered 30, 90 and 210 min after the last meal. Contents of stomach, proximal and median jejunum and ileum were collected and characterised. The extent of β-lactoglobulin (β-lg), α-lactalbumin (α-la) and casein proteolysis was monitored by inhibition ELISA, SDS-PAGE, immunoblotting and MS. At 30 min after the last meal, caseins were shown to be extensively hydrolysed in the stomach. Nevertheless, peptides originating mainly from β-caseins (from 509 to 2510 Da) were identified in the jejunum and ileum of the piglets. β-Lg partially resisted gastric digestion but completely disappeared in the stomach after 210 min. α-La had a similar behaviour to that of β-lg. Two large peptides (4276 and 2674 Da) generated from β-lg were present in the ileum after 30 and 210 min and only one (2674 Da) after 90 min.

An inverse relationship between Ca intake and BMI has been found in several studies. It has been suggested that Ca affects adipocyte metabolism via suppressing 1,25-dihydroxycholecalciferol (1,25(OH)2-D3) and decreases fat absorption. We studied the effect of Ca and milk proteins (whey and casein) on body weight in C57Bl/6J mice. Male mice, age 9 weeks, were divided into three groups (ten mice per group) receiving modified high-fat (60 % of energy) diets. Two groups received a high-Ca diet (1·8 % calcium carbonate (CaCO3)), with casein or whey protein (18 % of energy), and one group received a low-Ca diet (0·4 % CaCO3) with casein for 21 weeks. Food intake was measured daily and body weight twice per week. Body fat content (by dual-energy X-ray absorptiometry) of all mice and faecal Ca and fat excretion of seven mice/group were measured twice during the study. Final body weight (44·1 (sem 1·1) g) and body fat content (41·6 (sem 0·6) %) were significantly lower (P < 0·05) in the high-Ca whey group than in the low-Ca casein group (48·1 (sem 0·8) g and 44·9 (sem 0·8) %). Body weight and body fat content of the high-Ca casein group did not differ significantly from the low-Ca casein group even though serum 1,25(OH)2-D3 levels were significantly lower (P < 0·001) in both high-Ca groups than in the low-Ca casein group. Thus changes in serum 1,25(OH)2-D3 do not seem to affect body weight in this animal model. There was a significant difference in fat excretion between the high-Ca whey and low-Ca casein groups (3·9 (sem 0·9) % in the high-Ca whey v. 1·4 (sem 0·2) % in the low-Ca casein group; P < 0·05), which may partly explain the effect on body weight.

Four multiparous Holstein cows, each equipped with a duodenal cannula and an ultrasonic mammary blood flow probe, were assigned to a 4×4 Latin square to measure the effects of duodenal infusions of Leu (0, 40, 80 and 120 g/d) on lactational responses and mammary metabolism of nutrients. Cows were fed a diet of 67·0% corn silage, 5·3% grass hay, 14·2% peas, 7·8% maize starch, 1·0% each of molasses, urea, and sodium bicarbonate and 2·4% minerals and vitamins. Requirements of the remaining 9 essential amino acids were met by infusing into the duodenum 323 g/d of a mixture of amino acids including, Ile, Val, Met, Lys, Trp, Phe, His, Thr, Arg, Tyr and Glu. Milk protein content and yield were highest with 40 g/d of Leu and then progressively declined. Milk fat content and yield were significantly decreased over the entire range of Leu infusions. Arterial concentrations of Leu increased linearly and corresponding mammary arterio-venous differences increased to a plateau with 80 g/d of Leu. As Leu infusions increased, extraction rates of Leu decreased linearly, whereas those of Ile, Val, Lys, Arg, Thr and Tyr were significantly increased. Leu was taken up by the mammary gland according to milk output with 0 and 40 g/d of Leu infused and then largely in excess. Based on responses of protein yield and mammary uptake to milk output ratio, Leu concentration in total amino acids absorbed in the small intestine needs to be close to 8·9% for optimal milk protein synthesis.

The relative proportion of caseins to total protein is a parameter that can be used to control the protein quality in standardised milk, an increasing tendency in dairy industries. 31P-NMR was used to analyse the casein content of milk, by the quantitation of the area under the resonances belonging to SerP, and using methylenediphosphonic acid as internal standard. This procedure yielded good results, as similar values of caseins were obtained from N Kjeldahl and NMR analysis for slightly heated milk samples. Heating at 95 °C for 15 min did not alter the casein content results. Casein content of raw, pasteurised and UHT milks (25·6±1·4, 26·4±1·8, 25·5±1·6 g casein/l milk, respectively), obtained by NMR, were not significantly different, giving an average of 25·8±1·6 g casein/l for bulk liquid milk. This work concluded that 31P-NMR could be used as an alternative method to determine casein in raw, pasteurised, dry and UHT milks.

Two groups of 15 multiparous cows in mid-lactation were used in a Latin square design experiment with 4-week experimental periods. The genetic milk protein concentration level was high in the first group and low in the second. Each group of cows was given in a random order three feeding levels that covered 85, 100 and 115% of energy requirements and 90, 110 and 125% of nitrogen requirements, respectively. In both groups, increasing level of feeding induced a significant increase in milk yield (+2·4 kg/d between lowest and highest levels) and in protein concentration (+1·7 g/kg). The proportion of paracasein in total proteins was not altered by either genetics or nutrition. The proportion of casein in total proteins was slightly increased by 0·5 percentage points (P<0·05) with the intermediate level of feeding. Plasmin and plasminogen activities were not significantly modified by the genetic milk concentration level. Plasmin activity significantly increased with nutrient supplementation, but only in animals of low genetic potential (+21% between low and high levels, P<0·01). Casein composition was not significantly altered by the genetics or level of nutrition. Over the whole range of individual measurements taken (n = 90), the relationships between casein or paracasein and total protein concentrations were linear and very narrow (R2 = 0·92 and 0·95, respectively). The proportion of casein or paracasein in total proteins significantly decreased as plasmin activity increased.

Studies on camels' milk, whether with respect to concentration or bioavailability of trace elements from this milk, are limited and warrant further investigation. The object of this study was to analyse the concentration and distribution of zinc, copper, selenium, manganese and iron in camel milk compared to those in human milk, cows' milk and infant formula under similar experimental conditions. Camels' milk and cows' milk were collected from local farms, human milk samples were obtained from healthy donors in Kuwait and infant formula was purchased locally. Milk fractionation was performed by ultra-centrifugation and gel-column chromatography. The concentration of trace elements was analysed by atomic absorption spectrometry and that of protein was determined spectrophotometrically. The concentration of manganese and iron in camels' milk was remarkably higher (7–20-fold and 4–10-fold, respectively) than in human milk, cows' milk and infant formula. The zinc content of camels' milk was higher than that of human milk but slightly lower than in cows' milk and infant formula. The concentration of copper in camels' milk was similar to that of cows' milk but lower than in human milk and infant formula. The selenium content of camels' milk was comparable to those of other types of milk. Approximately 50–80% of zinc, copper and manganese in camels' milk were associated with the casein fraction, similar to that of cows' milk. The majority of selenium and iron in camels' milk was in association with the low molecular weight fraction. It is recommended that camels' milk be considered as a potential source of manganese, selenium and iron, perhaps not only for infants, but also for other groups suspected of mild deficiency of these elements. Further investigations are required to confirm this proposal.

Milk and yoghurt proteins were 15N-labelled in order to measure the flow rate of exogenous N during digestion in the human intestine. After fasting overnight, sixteen healthy volunteers, each with a naso-jejunal tube, ingested either [15N]milk (n 7) or [15N]yoghurt (n 9). Jejunal samples were collected every 20 min for 4 h. A significant stimulation of endogenous N secretion was observed during the 20–60 min period after yoghurt ingestion and the 20–40 min period after milk ingestion. The endogenous N flows over a 4 h period did not differ between the groups (44·3 (SEM 6·5) mmol for milk and 63·5 (SEM 5·9) mmol for yoghurt). The flow rates of exogenous N indicated a delayed gastric emptying of the yoghurt N compared with N from milk. The jejunal non-protein N (NPN) flow rate increased significantly after milk and yoghurt ingestion due to an increase in the exogenous NPN flow rate. The NPN fraction of exogenous N ranged between 40 and 80%. The net gastro-jejunal absorption of exogenous N did not differ significantly between milk (56·7 (SEM 8·5)%) and yoghurt (50·9 (SEM 7)%). The high level of exogenous N hydrolysis is in accordance with the good digestibility of milk products. Fermentation modifies only the gastric emptying rate of N and does not affect the level of diet hydrolysis, the endogenous N stimulation or the digestibility rate.

The variation of protein fractions in the milk of indigenous Greek goats fCapra prisca) during the milking period was studied. Total nitrogen (TN), non-casein or soluble nitrogen (SN), rennet whey nitrogen (WN), non-protein nitrogen (NPN) were determined and from these analyses crude protein (CP), true protein (TP), casein (Cas) rennet casein or coagulable protein (Coag P) were calculated. The NPN component is lost during the cheese process whereas Cas and Coag P are important constituents of the cheese itself. The ratios NPNICP, CaslTP and Coag PITP throughout milking, were for the groups A and B 0·0646 and 0·0648 (s.e.d. = 0·00025), 0·846 and 0·845 (s.e.d. = 0·0141) and 0·916 and 0·904 (s.e.d. = 0·0112), respectively, suggesting a high level of suitability for conversion of milk into cheese.