Ten pregnant heifers were inoculated in both hind udder quarters with a mixture of Actinomyces pyogenes, Fusobacterium necrophorum and Peptostreptococcus indolicus. Development of the experimental mastitis was monitored by sequential clinical and bacteriological examinations, and by blood acute phase protein profiles. Sequential changes in plasma fibrinogen, serum haptoglobin, acid-soluble glycoproteins and α1-proteinase inhibitor activity were analysed and compared with both the clinical and bacteriological findings and the final outcome of the disease after calving. All ten heifers developed moderate to severe clinical mastitis. Four recovered completely, had a normal lactation after calving and exhibited only transient fever and moderate local signs. In six of the heifers the course of the disease was severe, and the inoculated quarters failed to produce milk after calving. The acute phase response of the four heifers that recovered was also significantly milder than that of the other six heifers. Haptoglobin and acid-soluble glycoproteins were most effective in indicating the severity of the infection and predicting the final outcome of the disease. Fibrinogen was a reliable indicator for detecting the presence of bacterial infection in all heifers. α1-Proteinase inhibitor activity was of low diagnostic value in this study.

The aim of this study was to describe the results of teat thickness measurement applied routinely in three commercial dairy herds and to evaluate the influence of machine-induced teat thickness changes on intramammary infection and the frequency of new infection. A total of 1018 fore milk samples and the same number of teat apex measurements have been evaluated. Overall, relative teat thickness changes were normally distributed (mean −0·16%, SD 10·15%), while a specific pattern could be observed within herds. Increases in teat thickness of > 5% were significantly associated with infection and new infection (odds ratio > 1), but the association was not significant when teat thickness decreased by more than 5%. When results were classified according to aetiology, analysis showed that coagulase-negative staphylococcal infections were significantly associated with both increases and decreases in teat thickness numerically greater than 5%.

Post-milking measurements of teat skin chapping score, teat thickness and colonization by Staphylococcus aureus were determined for 11·5 d. Three teats on each of twelve Holstein cows, free from Staph, aureus intramammary infections, were immersed in 1 M-NaOH solution to induce teat chapping; the fourth teat served as a control. To achieve different degrees of chapping, one teat per cow received one immersion after each milking for three consecutive milking periods, a second teat received two immersions, and the third teat received one immersion which coincided with the last immersion of the other two teats. All teats were challenged twice with a skim milk broth culture of Staph, aureus (5 × 106 cfu) after the first and second milking following NaOH treatment. Measures were initiated with the milking following the last Staph, aureus challenges. Tissue thickness of the lateral side of the teat (barrel) and colonization by Staph, aureus declined with time. Thickness of the teat end varied more erratically. Teat skin chapping score was positively correlated (P < 0·001) with tissue thickness of the barrel and Staph, aureus colonization. Thickness of the barrel was not significantly correlated with Staph, aureus colonization. Barrel thickness as a covariate had a significant effect (P < 0·05) on teat skin colonization of Staph, aureus, whereas teat skin score and teat end thickness had no significant effect. Thus, thickness of the lateral side of the teat explained the greatest variation in Staph, aureus teat skin colonization in the model tested.

The effects of bulk milk cell count (BMCC) and stage of lactation on the quality and storage characteristics of UHT milk were investigated. The UHT milk was manufactured in a pilot plant using milk of low BMCC from early and late lactation, and milk of high BMCC from early and late lactation. Upon storage at 20°C, early lactation UHT milk gelled far ahead of late lactation milk. Within each stage of lactation, high BMCC milk tended to gel first. Few differences in the organoleptic properties of the UHT milks were observed. It was apparent that the onset of age gelation may not always be related directly to the level of proteolysis, and that other factors influencing milk composition and the reactions between milk components may play more important roles. At a particular stage of lactation, proteolysis induced by mastitis may hasten the onset of gelation.

Measurements of the zeta potential and particle size of casein micelles in skim milk suspensions at natural and lower pH have been made using the technique of electroacoustics. This technique requires no dilution or change of environment of the casein micelles. The zeta potential obtained at natural pH for a commercial skim milk suspension was −18 mV; it became less negative with decreasing pH. The median particle size observed at natural pH for a commercial skim milk suspension was 0·2 εm, in good agreement with previously reported values. The particle size increased as the pH was decreased.

After extended tryptic hydrolysis of large bovine casein micelles, a mineral-rich peptide fraction was recovered by ultracentrifugation. Its mineral part contained 72% of the colloidal Ca and 49% of the colloidal Pi originally present in the native micelle. Colloidal nitrogenous components were also present, amounting to 27% of the original N content. They contained most of the phosphopeptides and 82% of the micellar phosphoseryl residues. These tryptic peptides were characterized by reversed-phase HPLC on-line electrospray ion source–mass spectrometry analysis. Among the peptides produced 14 phosphopeptides were identified: αs2-CN(l–24), αs2-CN(1–21), αs1-CN(43–79), αs1-CN(35–79)7P, αs1-CN(35–79)8P, αs1-CN(37–79), αs1-CN(104–119), αs1-CN(104–124), β-CN(1–25), β-CN(1–28), β-CN(1–29), β-CN(30–97), β-CN(33–97) and β-CN(29–97). The proportion of the phosphopeptides interacting with colloidal calcium phosphate was correlated with their relative content of phosphoserine residues, since phosphopeptides containing more than four phos-phoserine residues were consistently present within this fraction. It also appeared that other types of peptides, some of them hydrophobic in nature, were also partly or completely present within the colloidal fraction, including αs1-CN(91–100), αs1-CN(152–193), αs1-CN(23–34), αs1-CN(125–193), αs1-CN(125–199), β-CN(177–209), β-CN( 184–209), β-CN(114–169) and β-CN(108–169). Their possible involvement in the micellar backbone is discussed.

In situ light scattering, where light scattered from a sample is measured directly while the sample is heated in the instrument, is presented as a simple and effective technique for studying the heat-induced aggregation of β-lactoglobulin. This technique was shown to be applicable not only to monitoring the initial aggregation steps, but to following the overall aggregation process with time. The experiments gave results similar to measurements carried out after a heat-quench treatment, but were more informative. From experiments on a standard NIZO β-lactoglobulin sample, a strongly desalted standard NIZO sample, different genetic variants of β-lactoglobulin and a mixture of these, we concluded that the standard NIZO sample was suitable for studying heat-induced aggregation. This sample has been investigated more extensively. Results with β-lactoglobulin (10–100 g/1) at 65 °C fitted a kinetic model for the denaturation and aggregation of β-lactoglobulin. This model, which held for β-lactoglobulin dissolved in water at near neutral pH and at 60–75 °C, recognizes an initiation, propagation and termination reaction, by analogy with polymer radical chemistry. It gave a quantitatively correct description of the dependence of the scattering intensity on the initial β-lactoglobulin concentration. Salt composition, pH and temperature strongly influenced the aggregation of β-lactoglobulin. Particle size increased with salt concentration in the range studied (up to 20 mM-NaCl and 1·0 mM-CaCl2). When the pH increased from 6°9 to 8·0 particle size was strongly reduced, whereas it strongly increased when pH was lowered to 6·2. Between 61·5 and 70 °C temperature did not affect particle size, whereas aggregation rate strongly increased. These effects could be incorporated in the kinetic model via the reaction constants of the reaction kinetic pathway.

The heat-induced binding of whey proteins to milk fat globule membranes in whole milk was investigated by quantitative electrophoresis and laser scanning densitometry. Both α-lactalbumin and β-lactoglobulin bound to the surfaces of fat globules when milk was heated in a water bath in the temperature range 65–85 °C. The interaction behaviour of α-lactalbumin did not seem to change with temperature, and the total amount of protein bound was ∼ 0·2 mg/g fat contained in the cream. The quantity of βlactoglobulin interacting with the milk fat globules increased with temperature from 02 to 0·7 mg/g fat between 65° and 85 °C. Even in whole milk heated at batch pasteurization temperatures (60–65 °C), α-lactalbumin and β-lactoglobulin were found attached to the fat globules. The interactions of the whey proteins with intact fat globule membranes were also investigated in milk heated in an industrial system (a pilot scale UHT and high temperature short time module), and the results were compared with those from the laboratory treatment (simple batch heating). The binding of the whey proteins to fat globules differed between milk heated by UHT using indirect steam heating or direct steam injection (DSI). However, the surface load in milk treated by DSI was not comparable to that of milk treated by batch heating or indirect steam heating, because of the changes in fat globule size and membrane composition caused by the DSI process.

Conversion of plasminogen to plasmin provides an important source of proteolytic activity in the bovine mammary gland. Plasminogen activator inhibitor 1 (PAI-1) plays a key role in limiting plasminogen activation. The PAI-1 biosynthetic capabilities of various bovine mammary cells were determined. The immortalized epithelial cell lines MAC-T and BME-UV and the myoepithelial cell line BMM-UV were used as model systems. Northern blot analysis indicated that both epithelial and myoepithelial cells contained PAI-1 mRNA. Bovine PAI-1 was encoded by a single mRNA species ∼ 3·0 kb long. BME-UV cells contained 2·0-fold (P < 0·01) the PAI-1 mRNA of MAC-T or BMM-UV cells. Reverse zymography indicated that both epithelial and myoepithelial cells synthesized PAI-1 protein with a molecular mass of ∼ 50 kDa.

The aim of this work was to develop new oriental style dairy products coagulated with culture filtrates from lao-chao, a traditional fermented rice product. The fermenting fungal cultures screened were Rhizopus javanicus, Rhiz. oryzae, Rhiz. chinensis, Rhiz. oligosporus, Aspergillus oryzae, Mucor racemosus and chiu-yao, a commercial starter. All the inocula liquefied a steamed glutinous rice base and produced culture filtrates with both milk-clotting and proteolytic activities. Of the fungal products tested, Rhiz. javanicus was the most successful, producing a good yield of culture filtrate with the desired milk-clotting activity, and the resultant yogurt-like product was more acceptable to consumers than any except that from chiu-yao. The firmness was less acceptable, but this could be improved by using mixed pure cultures of Rhiz. javanicus and M. racemosus.

Fresh rennet-coagulated cottage cheese whey was vacuum concentrated to 400 g total solids kg−1, and part of this evaporated whey was acidified to pH 4·6 to prepare whey protein concentrate. Both products were used separately to replace non-fat dried milk in yogurt. Diacetyl concentration increased on fortification with whey protein concentrate, and acetaldehyde increased with evaporated whey. However, the use of Bifidobacterium bifidum as a supplementary starter culture in addition to Streptococcus thermophilus and Lactobacillus delbrueckii subsp. bulgaricus reduced the concentration of diacetyl and acetaldehyde. Incorporation of whey solids stimulated the growth of Str. thermophilus and Bifid. bifidum in yogurt but the count of Lb. bulgaricus was reduced when Bifid. bifidum was incorporated. Examination of the organoleptic properties of the yogurts showed that both forms of whey solids were satisfactory replacements for non-fat dried milk. Fortification by whey protein concentrate improved the textural properties. Supplementation by Bifid. bifidum had only a marginal effect on the flavour of the product.