Over 3 years, 4 groups of heifers and 6 groups of cows calving in the autumn were used in a study of electronically controlled compound feed dispensers. For each group the treatments consisted of access or no access to the dispensers (selector feeders) arranged factorially with 2 levels of compound feed in the milking parlour. These were applied in weeks 3–15 of lactation. A basal diet including high quality silage was fed ad lib. communally to each group. The mean intake of compound from the dispensers was 5·6 kg/d, but there was considerable variation from animal to animal. The dispensers were visited at all times of the day and notably during the night. There was no bullying around the feeders. Milk yield was greater with the higher level of parlour feeding, and with access to the feed dispenser at the lower, but not the higher level of parlour feeding. Liveweight change benefited from additional compound feed supplied by either method.

Bulk milk cell counts obtained by a Coulter Milk Cell Counter were shown to be falsely elevated because of the formation of non-cellular particles (NCP). The NCP, which were detected by the use of a particle size analyser, were removed if the milk samples were heated to 55 °C for 15 min before the addition of formalin. A survey of bulk milk supplies in New South Wales showed that NCP occurred in milk from 2 % of farms, the counts being falsely elevated by about 200000 cells/ml. Surveys of milking equipment of farms where the bulk milk had shown this phenomenon demonstrated a relationship between the use of centrifugal milk pumps and the presence of NCP with a much lower prevalence in herds where spit chamber releasers were used. These particles were not air bubbles since air was removed from the milk by heating to 60 °C for 5 min, vacuum at 65 mmHg for 15 minor 0·5% v/voctan-2-ol; only the heat treatment removed the NCP.

Mice were fasted during pregnancy or early lactation and the effects on mammary development and milk yield studied on d 13 and d 18 of pregnancy and on d 7 of lactation. Fasting during pregnancy reduced body weight and mammary weight on d 13 of pregnancy but not on d 18. Mammary concentrations and total contents of DNA and RNA ([DNA], [RNA], DNAt, RNAt) were increased or unchanged on d 13 but significantly decreased on d 18. Fasting had no effect on fetal number or weight at either stage of pregnancy. Fasting on d 1 of lactation reduced mammary weight, DNAt and RNAt (but not [DNA] or [RNA]) and the incorporation of tritiated thymidine into DNA on d 2 of lactation. Mammary gland weight and composition on d 7 of lactation were not significantly affected by fasting for 24 h on d 1 of lactation or for 40 h on d 11–13 of pregnancy, except that DNAt was decreased slightly by the latter treatment.

Milk yield (litter weight gain) was depressed markedly during fasting on d 1 of lactation, but thereafter recovered so that it was the same as controls between d 3 and 13 of lactation; after d 13 it fell once more. A 40 h fast on d 11–13 of pregnancy had no effect on milk yield. Thus, although normal mammary development was inhibited by starvation, the gland was subsequently able to compensate so that milk yield was not reduced.

Proteolysis was measured quantitatively in normal bulk milk, either raw, pasteurized or heated (95 °C, 15 min). During incubation at 37 °C for 24 h, about 0·7 mM of peptide bonds were split in raw milk, and 1·8 mM after activation of the zymogen with urokinase. The same values were observed in pasteurized milk, and no significant activity was present in heated milk. When compared with a commercial plasmin preparation, these levels correspond to about 1·4 and 3·6μg/ml of plasmin respectively. Most of this activity was separated in the micellar fraction, and it was suppressed by addition of soyabean trypsin inhibitor (SBTI). The remaining activity in the serum phase was not inhibited by SBTI and gave a rather non-specific breakdown with few well-defined casein fragments being produced. Upon further incubation, after the first 24 h, the activity increased, indicating that activation of the zymogen (plasminogen) occurred spontaneously. The rate of this activation was independent of the addition of more plasminogen and was higher in pasteurized than in raw milk. In pasteurized milk, all the native milk proteinase was in the form of the zymogen at the time of secretion. β-Casein was the preferred substrate for the milk proteinase (plasmin) and produced γ-caseins and proteose-peptone components 5 and 8-fast; other fragments were clearly visible on polyacrylamide gel electrophoresis, and included degradation products of αs1-casein. The formation of all these fragments was enhanced by addition of urokinase alone, or of plasminogen and urokinase, or by increasing the incubation time. They were also produced by incubating the micellar fraction alone, but not the serum fraction. Additional fragments were produced when porcine plasmin was added presumably due to differences in specificity between the porcine and bovine enzymes or to contaminating enzymes. Proteolysis induced by additions of plasminogen alone, or of plasminogen plus urokinase, was closer to that observed for the native milk proteinase, and must be recommended for future work in which it is desired to enhance the level of proteinase without altering breakdown patterns, unless a very pure bovine plasmin is available.

Proteolytic activity in mastitic skim-milk was often 5–10 fold higher than in normal milk, its level being related to somatic cell count but not precisely correlated with it. In milks with the highest levels of activity plasmin accounted for about one third of the total proteinase. A further third was sedimented with the micellar fraction together with the plasmin, but unlike plasmin, was not inhibited by addition of soyabean trypsin inhibitor (SBTI). The final third remained in the serum phase.

Polyacrylamide gel electrophoresis (PAGE) showed that αsl- and β-caseins were degraded at about the same overall rate. The plasmin produced the usual readily identified fragments from β-casein, but incubation of mastitic milk also produced changes in patterns in the γ-casein region differing from plasmin-induced changes which were also apparent when the micellar fraction was incubated. As they were inhibited by SBTI, a second trypsin-like enzyme in addition to plasmin may also have been present. Other proteinase(s) not inhibited by SBTI was also associated with casein micelles and produced at least 3 characteristic protein fragments seen on PAGE. The serum phase proteinase(s) was likewise not inhibited by SBTI, and did not produce any well-defined electrophoretic bands, suggesting a rather non-specific breakdown of caseins. After separation of mastitic whole milk, a considerable proportion of the proteolytic activity was found in the cream phase. The proportion was enhanced by freezing and thawing, and the enzyme appeared to be identical to the SBTI-resistant micellar proteinase.

Because of the considerable proteolysis likely to occur under the time and temperature conditions involved, our results may provide some explanation for the problems encountered in cheesemaking with mastitic milks (e.g. yield losses, poor curd strength and off-flavour development).

The heat stability–pH profile of milk is shifted to more acidic values by anionic compounds such as SDS, lysolecithin and β-lactoglobulin and to more alkaline values by cationic compounds such as quaternary ammonium compounds. Proline, which reduces the hydrophobicity of proteins, destabilized milk slightly. The results suggest that the heat stability of milk and the shape of the HCT–pH curve may be dependent on micellar charge effects.

Several dicarbonyl compounds (glyoxal, substituted glyoxals, diacetyl and 1, 2-cyclohexadione) had a marked stabilizing effect on the heat stability of milk, especially in the presence of urea. These reagents are believed to modify arginine more or less specifically suggesting an important role for arginine residues in heat stability. In contrast, modification of lysine residiles with dansyl chloride, acetic anhydride or cyanoborohydride had little effect on maximum heat stability although it did alter the HCT-pH profile. Since diacetyl is a natural constituent of fermented milks and cheese, it may be acceptable as an additive to increase the heat stability of ṃilk.

The keeping quality of commercial HTST-pasteurized milk and laboratory pasteurized milk from a common bulk raw supply has been investigated for 5 dairies. Spoilage occurred at levels of total bacterial counts around 107 colony forming units/ml, but with a slightly higher off-flavour threshold for the commercial milks than the laboratory pasteurized milks. The predominant microflora at spoilage and the type of off-flavour produced differed between the 2 types of milk. Raising the storage temperature from 5 to 11 °C caused a slight shift in the spoilage microflora and led to an average reduction in the shelf life of the laboratory pasteurized milk from 28 to 6 d and of the commercial pasteurized milk from 13 to 5 d. Changes in the level of post-pasteurization contamination (PPC) were reflected in changes in keeping quality, particularly at 5 °C. However, the greatest improvements were found in the absence of PPC.

The rates of milk clotting and of formation of para-κ-casein in milk, colloidal phosphate-free milk and isolated κ-casein by pepsin and by its soluble size-fractionated conjugates with dextran were determined. Milk clotting with all the enzyme derivatives was dependent on the rate of the enzymic phase and required essentially complete κ-casein hydrolysis at 30 °C and throughout the range of pH 5·6–6·7. κ-Casein hydrolysis by pepsin at pH 6·6 was fastest in milk and slowest in isolated κ-casein, but the rate decreased as the enzyme size increased, especially with milk. When corrected for the changes in pepsin activity, the rates of κ-casein hydrolysis in all substrates were identical at 30 and 5 °C, but increased with decrease in pH, especially with the larger enzyme conjugates. Hydrolysis of the C-terminal bonds of β-and κ-casein in native and disrupted casein micelles by carboxypeptidase A and soluble conjugates of it were also investigated. κ-Casein was hydrolysed much faster, and β-casein slightly faster, in native than in disrupted micelles by the native enzyme. Increase in the size of carboxypeptidase A increased the rate of hydrolysis of κ-casein in disrupted micelles and also induced lag periods before hydrolysis commenced, especially with disrupted micelles. The results are compatible with a model for the casein micelle in which the κcasein is on the outside and the casein components are in a more ordered arrangement than in the casein complexes formed on micelle disruption. They also indicate that immobilized coagulants would be unable to clot milk.

A scintillation counter was used to measure chemiluminescence (CL) from milk powder and reconstituted milk. Only a small amount of CL, just above the background level, was observed from powders, but reconstituted milks emitted easily measurable CL. CL from milk was stimulated by exposure to light and found to decline gradually but non-exponentially after the exposure ceased. CL was at a maximum immediately after the milk was reconstituted from milk powder. Without light exposure, CL then declined gradually but non-exponentially over several hours to reach a constant value related to the level of oxidation of the powder. When determined under standard conditions 60 min after reconstitution, CL of milk reconstituted from stored milk powders correlated well with peroxide values and oxidized flavour as assessed by a taste panel.

The apparent relative viscosity (ηr) of stored homogenized ultra-heat-treated ‘coffee’ cream increased with time (t) at a rate which was a function of mean fat globule diameter (d) and fat volume fraction (ø); the rate was also influenced by Na2CO3 and Na citrate when present as stabilizing additives. Viscosity increases were attributed to the progressive flocculation of fat globules and to the strengthening of the structure formed by the gradual accretion of casein micelles on to globule surfaces and their points of contact (bridging). The expression

where t is in days and d in μm, was found to hold over a 12-week storage period for a batch of creams (ø = 0·143) of different d values prepared from the bulk cream containing carbonate and citrate stabilizers; η0 is the relative viscosity at t = 0 and k is a rate parameter. In the absence of stabilizers the parameter k assumed a smaller value and so appeared to be a function of chemical composition of the cream and of forces of particle interaction; seasonal factors were also suspected of influencing k. The effect of the fat volume fraction on storage behaviour was not fully resolved, but there was some evidence that the proportionality log ηrα1/ø½ was appropriate.

A fermented milk with typical yoghurt flavour and aroma was prepared using a human strain of Lactobacillus acidophilus. Growth of the lactobacillus was stimulated when the whey proteins of the ultrafiltered skim-milk substrate were increased by addition of ultrafiltered Cheddar cheese whey. Fermentation, which was carried out at 37 °C, was accelerated by addition of lactase. The resulting product had a smooth consistency, a pH of 4⋅2, acetaldehyde levels up to 15 p.p.m. and no off-flavours. L. acidophilus remained viable at a level of approx. 108 colony forming units/ml, with no impairment of quality, for up to 14 d at 4 °C.

The proteins of bovine milk are the best-characterized food-protein system. Lactoproteins, which have high biological value, contribute ∼25% of dietary protein in North West Europe, North America and Oceania. However, in protein-rich western diets, milk proteins are frequently more highly valued for their functional properties than for their nutritional qualities. The remarkably high heat stability of the caseinate system permits the manufacture of a range of sterilized, concentrated and dehydrated products while its gelation on very limited proteolysis is the basis of cheese manufacture. Skim-milk powders, caseinates and whey protein concentrates are the most flexible and widely used functional proteins in food processing.

This communication reviews recent studies on milk proteins with respect to molecular and colloidal properties; coagulation by Ca2+, heat and ethanol; and functional properties and their chemical and enzymic modification.

Destabilization of emulsion droplets is described in terms of flocculation, coalescence and adsorption processes, and then discussed with reference to various technological aspects of dairy emulsions. A semi-quantitative measurement of homogenization-induced flocculation of cream is described using measurements on the time-dependent decrease in viscosity that occurs during shear. The whipping of cream is discussed in terms of the adsorption of fat droplets to air bubbles and the formation of a fat particle network with the fat directly in contact with air. The whipping of homogenized creams is shown to be dependent upon the structure of the newly formed milk fat globule membrane. Since the major protein component of the membrane is casein, any change in casein micelle stability is reflected in the whipping properties of the cream.

The presence of crystalline fat within emulsion droplets is essential for many destabilization processes. Fat crystals pierce the film between 2 approaching interfaces, thus leading to aggregation. The contact angle between fat crystal, oil and aqueous phase can be used to describe the susceptibility of an emulsion to destabilize.

A quantitative measure of emulsion destabilization under shear is described kinetically in terms of reversible flocculation followed by coalescence. The measurement of emulsion viscosity as a function of time at constant shear stress is used to monitor the aggregation processes and the 3 rate constants evaluated by computer curve fitting.

Regioselective esterification and acetalation reactions of lactose have produced partly protected derivatives which have significant value in the further modification of lactose and as precursors for the synthesis of higher oligosaccharides.

Treatment of food proteins with heat and/or alkali may convert some of the constituent amino acids into the unnatural amino acid lysinoalanine (LAL), which has been found to cause kidney damage (nephrocytomegaly) when fed to rats. LAL may be produced by β-elimination of a phosphoseryl, of a glycosylated seryl or of a cystyl residue followed by a nucleophilic addition to a lysyl residue. The formation of LAL in αs0-, αsl- and β-casein is discussed in relation to the location of phosphoseryl residues immediately adjacent to lysyl residues. The influence of pH, temperature and exposure time on the formation of LAL in whole casein is described in detail. The formation of LAL can be prevented by the addition of reducing agents, dephosphorylation or chemical modification of the є-amino group of lysine. The LAL content of foodstuffs can be measured accurately by ion-exchange chromatography and a survey is given of the LAL content of commercial milk and milk products.

The biological effects of free and protein-bound LAL are discussed. It seems that renal changes due to the presence of LAL in the diet are species-specific to the rat although recent findings have shown that no effect is observed in rats fed a mixed diet containing proteins with and without protein-bound LAL. When LAL is removed from the diet, nephrocytomegaly disappears. From these results it may be concluded that the health risks for man, connected with the eating of proteins which have been subjected to treatment with heat and/or alkali, are small.

The decrease in lysine content of milk and milk products due to formation of LAL is small (0–1 or 2%) in comparison with the decrease in available lysine possibly caused by the Maillard reaction (0–24%) and so the decrease in nutritive value of food products due to LAL formation may be neglected.

Cheesemaking is initiated by specific hydrolysis of κ-casein, followed by random aggregation of casein particles to form a network. The structure of this curd determines its subsequent behaviour and the composition and texture of the cheese. It is affected by previous homogenization or concentration of the milk. The composition of the milk and the distribution of components in it, which are affected by season, mastitic infection and cold storage, also influence its curd-forming properties, and the composition and yield of cheese. During ripening of cheese, the final texture and the development of flavour occur. Both are influenced by the type and extent of proteolysis, catalysed by coagulant, bacterial and milk enzymes. These and other enzymic and non-enzymic reactions responsible for flavour development depend on the composition and environment within the product. Some of these reactions can be accelerated by incorporating enzymes and chemical reagents into the curd, resulting in the production of an enhanced flavour. A number of compounds responsible for the flavour of cheese and yoghurt have been identified and mechanisms for their formation and retention in the product have been postulated.

Ion exchange is a unit operation which has several applications in the processing of skim-milk and whey. For example, in the field of whey processing, ion exchange is used in demineralization, lactose hydrolysis and in the pre-treatment of whey prior to protein recovery. In the case of skim-milk, applications include the manufacture of low Na milk and pre-acidification of skim-milk in casein manufacture. However, the ion exchange treatment of skim-milk to replace Ca ions with Na ions leads to far more fundamental changes with regard to the native protein conformation.

The effect of Ca removal from skim-milk is essentially to disrupt the native casein micelle structure into unassociated molecules of Na caseinate. Skim-milk modified in this way shows increased stability to alcohol and heat and increased functionality of the skim-milk protein in terms of water binding, emulsification and foaming capacity. The viscosity of Ca-reduced skim-milk is also substantially increased.

The improved functionality of Ca-reduced skim-milk makes the latter a potentially useful food ingredient in products where the above mentioned properties are important.