Composition of milk fat from cows selected for milk fat globule size and offered either fresh pasture or a corn silage-based diet

The objective of this study was to examine the synthesis and composition of milk produced by dairy cows that secrete either small milk fat globules (SMFG) or large milk fat globules (LMFG), and to study their response to diets known to alter milk composition. Four groups of 3 multiparous dairy cows were assigned to 2 isoenergetic feeding treatments: a corn silage treatment supplemented with soybean meal, and fresh pasture supplemented with cereal concentrate. The 4 groups comprised 2 groups of 3 dairy cows that produced SMFG (3.44 μm) and 2 groups of 3 dairy cows that produced LMFG (4.53 μm). The SMFG dairy cows produced higher yields of milk, protein, and calcium. Nevertheless, their milk had lower fat and protein contents. Both SMFG and LMFG cows secreted similar amounts of milk fat; therefore, higher globule membrane contents in milk fat were observed in SMFG cows. Higher calcium mineralization of the casein micelles in SMFG cows suggests that it may be possible to improve cheese-making properties even if the lower protein content may lead to lower cheese yields. The SMFG cows secrete milk fat with a higher concentration of monounsaturated fatty acids and a lower concentration of short-chain fatty acids. They also have a higher C18:1/C18:0 ratio than LMFG cows. This suggests that SMFG cows have more significant fatty acid elongation and desaturation. The pasture treatment led to an increase in milk and protein yields because of increased energy intake. It also resulted in lower milk fat yield and fat and protein contents. The pasture treatment led to a decrease in milk fat globule size and, as expected, an increase in monounsaturated and polyunsaturated fatty acid contents. However, it induced a decrease in the protein content, and in calcium mineralization of casein micelles, which suggests that this type of milk would be less suitable for making cheese. This study also shows that there is no correlation between the cows, based on milk fat globule size and diet. These results open up possibilities for improving milk fat quality based on milk fat globule size, and composition. The mechanisms involved in milk fat globule secretion are still to be determined.     

Seasonal variations in composition,properties, and heat-induced changes in bovine milk in a seasonal calving system

We determined seasonal variations in the composition and characteristics of bovine milk, as well as heat-induced changes in the physicochemical properties of the milk, in a typical seasonal-calving New Zealand herd over 2 full milking seasons. Fat, protein, and lactose contents varied consistently during the year in patterns similar to those of the lactation cycle. Seasonality also had significant effects on milk calcium, ionic calcium, fat globule size, buffering capacity, and ethanol stability, but not on casein micelle size. The ratio of casein to total protein did not vary significantly over the season, but late-season milk had the highest content of glycosylated κ-casein (G-κ-CN) and the lowest content of α-lactalbumin in both years. We observed significant between-year effects on protein, total calcium, ionic calcium, pH, and casein:total protein ratio, which might have resulted from different somatic cell counts in the 2 years. Compared with heating at 90°C for 6 min, UHT treatment (140°C for 5 s) induced greater dissociation of κ-casein, a similar extent of whey protein denaturation, a lower extent of whey protein–casein micelle association, and a larger increase in casein micelle size. Indeed, UHT treatment might have triggered significant dissociation of G-κ-CN, resulting in aggregation among the casein micelles and increased apparent mean casein micelle diameter. Seasonality had significant effects on the partitioning of G-κ-CN between the micelle and the serum phase, the extent of whey protein–casein micelle association under both heating conditions, and the casein micelle size of the UHT milk.     

Supramolecular structure of the casein micelle

The supramolecular structure of colloidal casein micelles in milk was investigated by using a sample preparation protocol based on adsorption of proteins onto a poly-l-lysine and parlodion-coated copper grid, staining of proteins and calcium phosphate by uranyl oxalate, instantaneous freezing, and drying under a high vacuum. High-resolution transmission electron microscopy stereo-images were obtained showing the interior structure of casein micelles. On the basis of our interpretation of these images, an interlocked lattice model was developed in which both casein-calcium phosphate aggregates and casein polymer chains act together to maintain casein micelle integrity. The caseins form linear and branched chains (2 to 5 proteins long) interlocked by the casein-stabilized calcium phosphate nanoclusters. This model suggests that stabilization of calcium phosphate nanoclusters by phosphoserine domains of α_s1-, α_s2-, or β-casein, or their combination, would orient their hydrophobic domains outward, allowing interaction and binding to other casein molecules. Other interactions between the caseins, such as calcium bridging, could also occur and further stabilize the supramolecule. The combination of having an interlocked lattice structure and multiple interactions results in an open, sponge-like colloidal supramolecule that is resistant to spatial changes and disintegration. Hydrophobic interactions between caseins surrounding a calcium phosphate nanocluster would prevent complete dissociation of casein micelles when the calcium phosphate nanoclusters are solubilized. Likewise, calcium bridging and other electrostatic interactions between caseins would prevent dissociation of the casein micelles into casein-calcium phosphate nanocluster aggregates when milk is cooled or urea is added to milk, and hydrophobic interactions are reduced. The appearance of both polymer chains and small aggregate particles during milk synthesis would also be expected based on this interlocked lattice model of casein micelles, and its supramolecule structure thus exhibits the principles of self-aggregation, interdependence, and diversity observed in nature.     

Effects of mineral salts and calcium chelating agents on the gelation of renneted skim milk

The effects of adding CaCl2, orthophosphate, citrate, EDTA, or a mixture of these, to reconstituted skim milk (90 g of solids/kg solution) on the gelation of renneted milk were mediated by changes in Ca2+ activity and the casein micelle. At pH 6.65, the addition of citrate or EDTA, which removed more than 33% of the original colloidal calcium phosphate with the accompanying release of 20% casein from the micelle, completely inhibited gelation. Reformation of the depleted colloidal calcium phosphate and casein in the micelle, by the addition of CaCl2, removed this inhibition. When the minimum requirements for colloidal calcium phosphate and casein in the micelle were met, the coagulation time decreased with increasing Ca2+ activity, leveling off at high Ca2+ activity. The storage modulus of renneted gels, measured at 3 h, increased with increasing colloidal calcium phosphate content of micelles up to a level at which it was approximately 130% of the original colloidal calcium phosphate in the micelles. Further increases in colloidal calcium phosphate by the addition of CaCl2, orthophosphate, or mixtures of these, which did not change the proportion of casein in the micelle, decreased the storage modulus. The gelation of the renneted milk was influenced by Ca2+ activity, the amounts of colloidal calcium phosphate, and casein within the micelle, with the effects of colloidal calcium phosphate and casein within the micelle clearly dominating the storage modulus. These results are consistent with the model of Horne (Int. Dairy J. 8:171-177, 1998) which postulates that, following cleavage of the stabilizing K-casein hairs by rennet, the properties of the rennet gel are determined by the balance between the electrostatic and hydrophobic forces between casein micelles.     

Changes in the surface protein of the fat globules during ultra-high pressure homogenisation and conventional treatments of milk

Disruption of fat globules upon homogenisation provokes a reduction of their size and a concomitant increase in their specific surface area. In order to overcome this phenomenon, the milk fat globule membrane (MFGM) adsorbs non-native MFGM proteins. The aim of the present study was to examine the effects of UHPH conditions (temperature and pressure) on the milk fat globule and the surface proteins by comparison with conventional treatments applied in the dairy industry. Transmission electron microscopy and SDS-PAGE revealed major differences. In UHPH-treated milk, casein micelles were found to be adsorbed on the MFGM in a lesser extent than in conventional homogenisation–pasteurisation. However, greater adsorption of directly bonded casein molecules, released by UHPH through the partial disruption of casein micelles, was observed especially at high UHPH pressures. Adsorption of whey proteins on the MFGM of conventionally homogenised–pasteurised milk was mainly through intermolecular disulfide bonds with MFGM material, whereas in UHPH-treated milk, disulfide bonding with both indirectly and directly adsorbed caseins was also involved.     

The use of sedimentation field flow fractionation and photon correlation spectroscopy in the characterization of casein micelles

Sedimentation Field Flow Fractionation (SdFFF) was combined with Photon Correlation Spectroscopy (PCS), to characterize changes in the structure of the colloidal particles of reconstituted skim milk of diameter >50 nm (aggregates of casein and calcium phosphate known as casein micelles) with the changes in partitioning (with the addition of salt) of calcium (Ca), inorganic phosphate (Pi) and casein between the serum and colloidal phases of the milk. The number weighted particle size distributions are determined. These are well represented by a log-normal distribution. Methods are presented for estimating the relative contributions of scattering and absorbance to the SdFFF detector signal and for taking both into account when analysing SdFFF data. The values found for the effective density of the casein micelles were in good agreement with the literature and ranged from (1.06-1.08 g cm(-3)) according to the composition of micelles. The changes in the scattering intensity as determined by PCS correlated with the changes in the particle composition. Although the concentrations of colloidal calcium phosphate (CCP) (1.1-3.5 g/kg milk) and micellar casein (18.1-27.2 g/kg milk) varied considerably only small changes in the size distribution of particles >50 nm diameter were observed except for milk to which 30 mmol Pi+10 mmol Ca/kg milk had been added where the particle size distribution shows a swelling of the particles consistent with a lower than expected value for the particle density. These observations suggest that the micelles have the ability to both lose (depleted micelles) and accommodate (enriched micelles) more casein, calcium and inorganic phosphate in their interior, thus confirming the model of the micelles which postulates an open structure allowing freedom of movement of casein and small ions.     

Does homogenization affect the human health properties of cow's milk?

During the processing of marketed milk, homogenization reduces fat droplet size and alters interface composition by adsorption of casein micelles mainly, and whey proteins. The structural consequences depend on the sequence of the homogenization and heat treatments. Regarding human health, homogenized milk seems more digestible than untreated milk. Homogenization favors milk allergy and intolerance in animals but no difference appears between homogenized and untreated milk in allergic children and lactose-intolerant or milk-hypersensitive adults. Controversies appear regarding the atherogenic or beneficial bioactivity of some casein peptides and milk fat globule membrane proteins, which might be enhanced by homogenization. In children prone to type I diabetes, early cow's milk consumption would be a risk but no link was observed in the general population and the effect of homogenization has not been studied. In the current context of obesity and allergy outbreaks, the impact of homogenization and other technological processes on the health properties of milk remains to be clarified.     

Composition and Structure of Fat Globule Surface Layers in Recombined Milk

Protein coverage, composition and structure of surface layers of fat globules in recombined milk were determined. Average protein load was ～6 mg/m² fat surface. Both casein and whey proteins were present in the fat globule surface layer, with casein adsorbed in preference to whey proteins and α_s (α_sl+α_s2)-casein adsorbed in preference to β-casein. Transmission electron microscopy showed that the surface layer of fat globule was made up of casein micelles, fragments of casein micelles and a thin layer of protein, possibly whey proteins. Experiments with surface layers that had been dispersed in EDTA showed that the extent of dissociation of caseins followed the order: β-casein > α_s-casein ≦ K-casein, suggesting that most of the K-casein was probably associated directly with the fat surface.     

Mineral and casein equilibria in milk: effects of added salts and calcium-chelating agents

We have investigated the effects of adding a range of mineral salts and calcium-chelating agents on the distribution of casein and minerals between the non-pelleted and pelleted phases of milk obtained upon centrifugation at 78000 g for 90 min. Adding CaCl2 or mixtures of NaH2PO4 and Na2HPO4 to reconstituted skim milk (90 g milk solids/kg) at pH 6.65 increased both pelleted casein and pelleted calcium phosphate. Opposite effects were obtained by adding citrate or EDTA. The change in pelleted calcium phosphate was not simply related to casein release from the micelle. Upon adding 5 mmol EDTA/kg milk, 20% of the pelleted Ca, 22% of the pelleted phosphate and 5% of the micellar casein were removed. Increasing the concentration of EDTA to 10 mmol/kg milk decreased the pelleted Ca by 44% and the pelleted phosphate by 46%, and caused 30% of the micellar casein to be released. The effects of adding phosphate, citrate or EDTA at pH 6.65, followed by the addition of CaCl2, demonstrated the reversibility of the dissolution and formation of the micellar calcium phosphate. There were limits to this reversibility that were related to the amount of colloidal calcium phosphate removed from the casein micelles. Adding CaCl2 to milk containing > or = 20 mmol EDTA or > or = 30 mmol citrate/kg milk did not result in complete reformation of casein micelles. Light-scattering experiments confirmed that the dissolution of moderate amounts of colloidal calcium phosphate had little effect on micellar size and were reversible, while the dissolution of larger amounts of colloidal calcium phosphate resulted in large reductions in micellar size and was irreversible.     

Interactive effects of casein micelle size and calcium and citrate content on rennet‐induced coagulation in bovine milk

Interactive effects of casein micelle size and milk calcium and citrate content on rennet‐induced coagulation were investigated. Milk samples containing small (SM) and large (LM) micelles, obtained from individual Holstein cows, were modified by addition of calcium and/or citrate and milk coagulation properties were evaluated in a full factorial design. The results showed that LM milk had a higher relative proportion of casein, coagulated faster, and resulted in a stronger gel than SM milk. Addition of calcium slightly decreased casein micelle size, while addition of citrate slightly increased micelle size. Calcium addition resulted in a shorter coagulation time and the strongest gels, while citrate addition increased the coagulation time and resulted in the weakest gels. Addition of calcium and citrate in combination resulted in intermediate coagulation properties. The interactive effect of micelle size and citrate was significant for gel strength. Microstructural differences between the milk gels were consistent with the rheological properties, for example, the micrographs revealed that a more homogeneous network was formed when calcium was added, resulting in a stronger gel. A more inhomogeneous network structure was formed when citrate was added, resulting in a weaker gel. Thus, variations in casein micelle size and in calcium and citrate content influence rennet‐induced coagulation in bovine milk. The calcium and citrate contents in Swedish milk have changed over time, whereby calcium content has increased and citrate content has decreased. In practical cheese making, calcium is added to cheese milk, most likely altering the role of inherent citrate and possibly influencing casein micelle size. The observed interaction effect between casein micelle size and citrate in this study, suggests that larger micelles with moderate citrate level will result in firmer gels, whereas a higher citrate content reduced gel strength more in case of large than SM. Since firmer gels are likely to retain more protein and fat than less firmer gels, this interaction effect could have implications in practical cheese production.     

High pressure-induced denaturation of alpha-lactalbumin and beta-lactoglobulin in bovine milk and whey: a possible mechanism

In this study, high pressure (HP)-induced denaturation of alpha-lactalbumin (alpha-la) and beta-lactoglobulin (beta-lg) in dairy systems was examined. In both milk and whey, beta-lg was less baroresistant than alpha-la; both proteins were considerably more resistant to HP-induced denaturation in whey than in milk. HP-induced denaturation of alpha-la and beta-lg increased with increasing proportion of milk in mixtures of milk and whey. Addition of a sulphydryl-oxidising agent, KlO3, to milk or whey increased HP-induced denaturation of beta-lg, but reduced the denaturation of alpha-la. Denaturation of both alpha-la and beta-lg was prevented by adding a sulphydryl-blocking agent, N-ethylmaleimide, to milk or whey prior to HP treatment, highlighting the crucial role of sulphydryl-disulphide interchange reactions in HP-induced denaturation of alpha-la and beta-lg. Removal of colloidal calcium phosphate from milk also reduced HP-induced denaturation of alpha-la and beta-lg significantly. The higher level of HP-induced denaturation of alpha-la and beta-lg in milk than in whey may be the result of the abscence of the casein micelles and colloidal calcium phosphate from whey, which facilitate HP-induced denaturation of alpha-la and beta-lg in milk.     

Microfiltration of butter serum upon casein micelle destabilization

The gross composition of butter serum, the aqueous phase of butter, is comparable to that of buttermilk, except that it has a higher content of material derived from the milk fat globule membrane (MFGM). As such, butter serum is a good source for further purification of MFGM material. The purified fraction could be of interest for its emulsifying and nutritional properties. The effect of sodium citrate and ethanol on the dissociation of butter serum casein micelles, and their effect on casein retention upon tangential microfiltration were investigated. Optimal conditions of casein micelle dissociation were assessed by using an experimental design (response surface full central composite orthogonal design) with temperature and ethanol or sodium citrate concentration as design variables and the Hunter L* value as response variable. For both dissociating agents, a highly significant reduced quadratic model was fit to the data. Microfiltration tests were performed on pure butter serum, and on butter serum in the presence of sodium citrate, under optimal dissociation conditions (50°C, 80 mM). A cellulose acetate membrane with a pore size of 0.15 μm was used. From the filtration curves and fouling coefficients it was clear that the addition of sodium citrate improved the permeation flux, and minimized fouling. All fractions were analyzed for dry matter, protein, lactose, lipid, and polar lipid contents. The protein fraction was further characterized by sodium dodecyl sulfate-PAGE. It was shown that sodium citrate greatly enhanced casein transmission through the membrane, but at the expense of substantial losses of polar lipids.     

Reformation of casein particles from alkaline-disrupted casein micelles

In this study, the properties of casein particles reformed from alkaline disrupted casein micelles were studied. For this purpose, micelles were disrupted completely by increasing milk pH to 10.0, and subsequently reformed by decreasing milk pH to 6.6. Reformed casein particles were smaller than native micelles and had a slightly lower zeta-potential. Levels of ionic and serum calcium, as well as rennet coagulation time did not differ between milk containing native micelles or reformed casein particles. Ethanol stability and heat stability, >pH 7.0, were lower for reformed casein particles than native micelles. Differences in heat stability, ethanol stability and zeta-potential can be explained in terms of the influence of increased concentrations of sodium and chloride ions in milk containing reformed casein particles. Hence, these results indicate that, if performed in a controlled manner, casein particles with properties closely similar to those of native micelles can be reformed from alkaline disrupted casein micelles.     

Milk lipoprotein lipase distribution in the major fractions of bovine milk

Raw, bovine bulk tank milk and milks from selected cows were separated by ultracentrifugation into four major fractions: casein, sloughed membrane material, serum, and milk fat globule membrane. Milk lipoprotein lipase activity was measured by the pH stat method and protein determinations were made by the Lowry procedure for each of the four fractions in order to calculate specific activity (units per milligram of protein). In six farm-cooled bulk milk samples stored less than or equal to 24 h, casein had a significantly higher milk lipoprotein lipase total activity, 35.66 units/ml of milk, than all of the fractions. Serum had the next highest activity with 11.69 units/ml of milk. Fluff and milk fat globule membrane had activities of .80 and .41 units/ml of milk, respectively. The specific activity of the fluff was 3.3 milk lipoprotein lipase units/mg of protein, which was significantly higher than the casein and serum fractions in pooled milk. Milks from five cows in midlactation were assayed individually for milk lipoprotein lipase activity and protein content immediately after milking and after 12, 24, 48 and 72 h of cold (4 degrees C) storage. Fresh warm milk was characterized by the absence of fluff. Casein had the highest mean activity (29.91 units/ml), followed by serum (10.25 units/ml) and milk fat globule membrane (.26 units/ml) in the warm milk from the individual cows. Upon cooling to 4 degrees C, significant increases in enzyme activity in the fluff and milk fat globule membrane fractions were observed at 12 h.(ABSTRACT TRUNCATED AT 250 WORDS)     

Cold ultrafiltered or microfiltered milk retentates: A systematic comparison of the effects of compositional differences on their gelation functionality

The colloidal stability of casein micelles suspensions prepared using ultrafiltration (UF) and microfiltration (MF) was studied by testing acid- and rennet-induced destabilization. Skim milk and 4× (based on volume reduction) concentrates were obtained by processing under similar conditions, at temperatures below 10°C. Concentrates were subjected to different levels of diafiltration (DF), resulting in samples with comparable casein volume fractions but different amounts of proteins and ions in the serum phase. The novelty of the work is the systematic comparison of MF and UF concentrates of similar history. More specifically, concentrates similar in ionic composition but with or without serum proteins were compared, to evaluate whether whey proteins and β-casein depletion from the micelles will play a role in the processing properties, or whether these are affected solely by the ionic balance. Microfiltered micelles' apparent diameter decreased by about 50 nm during the specific hydrolysis of κ-casein by chymosin, whereas those in skim milk control showed a decrease of about half that size. All concentrates subjected to extensive DF showed smaller hydrodynamic diameters, with reductions of ∼18 and 13 nm for MF and UF, respectively. Highly diafiltered UF retentates showed a delayed onset of rennet-induced gelation, due to low colloidal calcium, compared with other samples. Low-diafiltered samples showed weak storage modulus (∼1 Pa) after 60 min of onset of gelation. In addition, onset pH increased with diafiltration to ∼5.8 for UF and ∼6 for MF in high-diafiltered samples. These results clearly demonstrated that the functional properties of casein micelles change during membrane concentration, and this cannot be solely attributed to changes in ionic equilibrium.     

The effect of hexametaphosphate addition during milk powder manufacture on the properties of reconstituted skim milk

Skim milk powders with various levels of sodium hexametaphosphate (NaHMP) were prepared. Reconstituted skim milk samples were prepared from these powders. NaHMP slightly reduced the pH, markedly reduced the serum and ionic calcium and markedly increased the serum phase orthophosphate levels of the milks. This shift in the mineral equilibrium resulted in a drastic reduction in casein micelle integrity, with a marked dissociation of casein from the micelles. κ-Casein was the predominant casein dissociated, although significant levels of α_S-casein and β-casein were also transferred to the serum phase. This dissociation of the casein micelles caused a marked decrease in size and scattering properties of the casein micelles. In addition, a small decrease in the zeta potential of the casein micelles in the milk was observed. Heat treatment of the milks with added NaHMP induced further dissociation of κ-casein, although much of the α_S-casein and β-casein re-associated with the micelles.     

Effect of NaCl on some physico-chemical properties of concentrated bovine milk

The influence of added NaCl (75–850 mmol L⁻¹) on some physicochemical properties of 2× or 3× concentrated milk (18 or 27%, w/v, total solids, respectively) was investigated. Adding NaCl did not influence average casein micelle size, but reduced the net-negative charge on the casein micelles and milk pH. The level of soluble and ionic calcium was increased by addition of NaCl, but the level of soluble inorganic phosphorus was not influenced. Addition of NaCl shifted the maximum in the pH–heat coagulation time (HCT) profile of 2× or 3× concentrated milk to a higher pH value and certain concentrations increased the maximum HCT, probably due to the fact that NaCl reduced the extent of heat-induced dissociation of κ-casein. Added NaCl reduced the ethanol stability, with the extent of this effect increasing with the concentration of NaCl. The key-mechanism though which added NaCl induces changes in the physico-chemical stability of casein micelles appears to be through changes in the charge on the casein micelles.     

Proteolytic activity in UHT-sterilized milk.

The proteolytic activity in UHT-sterilized milk of a proteinase-containing fraction, prepared from the milk, is reported. The proteinase fraction was isolated from casein micelles as described by Reimerdes & Klostermeyer (1974). The fraction was added to UHT milks and the proteolysis in the samples, measured as the liberation of non-protein nitrogen, compared with that in control samples without added proteinases. The increase in proteolytic activity and deterioration in samples containing added proteinases indicates that an enzyme process occurred in UHT-sterilized milk which could influence gel formation.     

Distribution of plasminogen and plasmin in fractions of bovine milk.

The relative amounts of immunoreactive plasminogen and active plasmin in different fractions of bovine milk were examined. Raw milk was centrifuged to separate skim, cream, and a somatic cell pellet. Skim milk was centrifuged to separate milk serum and casein micelles. Milk fat globule membranes were isolated from the cream fraction of bovine milk. Proteins from somatic cells were isolated following sonication of the cells. Western blot analysis showed the presence of several forms of plasminogen in bovine milk. The predominant forms of plasminogen identified following electrophoresis under nonreducing conditions were proteins with approximate molecular weights of 88,000, 152,000, and 160,000. The predominant forms of plasminogen identified after electrophoresis under reducing conditions were two proteins with approximate molecular weights of 88,000 and 50,000. The highest amount (82% of the total plasminogen), as determined by an ELISA, was associated with the casein fraction. Lower plasminogen concentrations were associated with the serum, cream fractions, and milk fat globule membranes. The SDS-PAGE of the cream and milk fat globule membranes indicated that some casein was present in both fractions. Thus, the low plasminogen concentrations in these fractions may be associated with the caseins there. No immunoreactive plasminogen was present in the somatic cells. Active plasmin was present in the same milk fractions in which plasminogen was detected: casein, serum, and cream.     

Behaviour of homogenized fat globules during the spray drying of whole milk

The changes in milk fat globule size and fat globule surface proteins of both low-preheated and high-preheated concentrated milks, which were homogenized at low or high pressure prior to spray drying using a disc atomization drier, were examined. The average fat globule size (d₃₂) of the spray-dried milk powders was smaller than that of the corresponding concentrates, but a small proportion of very large globules (4–80 μm) was also formed during spray drying. As a consequence, total surface protein (mg protein g⁻¹ fat) increased due to the adsorption of casein micelles at the fat globule surface during spray drying. Confocal micrographs of the powders showed some apparent spreading of the fat on the surface of the powder particles, particularly when the concentrates were homogenized at low pressure. These results indicate disruption of the milk fat globules during spray drying, which consequently causes changes in the fat globule surface protein layer.