Milk from French-Alpine goats and Holstein cows was obtained from a bulk tank immediately prior to analyses. Fat globule size was determined by laser particle size analysis. Individual globules of fat in goat milk ranged from 0.73 to 8.58 microm in diameter. The average diameter of particles based on volume to surface area ratio (dvs) was 2.76 microm and was less than the mean (dvs) of 3.51 microm for bovine milk, in which fat globules ranged from 0.92 to 15.75 microm in diameter. The specific surface area of particles in caprine milk was 21,778 cm2/ml, whereas the specific surface area of particles in bovine milk was 17,117 cm2/ml. Ninety percent of the total particles found in goat milk were less than 5.21 microm in diameter, whereas 90% of the total particles in bovine milk were less than 6.42 microm based on the volume frequency distribution. Dissociation of casein micelles by urea in goat whole and skim milk caused larger dvs values due to the effect of fat particles and reduced the specific surface area in both milks because the total number of detectable particles in both whole and skim milk was reduced.

No abstract

Goat milk Jack cheeses were manufactured with different levels of proteolytic endo-and exopeptidases from lysed bacterial cultures and aged for 30 wk. The aroma compounds that are potentially important in contributing the typical flavor of goat milk Jack cheese were quantified using static headspace gas chromatography. The concentrations of volatile compounds were evaluated every 6 wk throughout the aging period. Odor activity values of volatile compounds were calculated using the sensory threshold values reported in literature and their concentrations in Jack cheeses. Odor activity values of identified compounds were used to assess their potential contribution to the aroma of goat milk Jack cheeses. The odor activity values indicated that the ketones 2-hexanone, 2-heptanone, 2-nonanone, and 2,3-butanedione (diacetyl) were important odor-active compounds. The major odor-active acids found in this semi-hard goat milk cheese were butanoic, 2-methyl butanoic, pentanoic, hexanoic, and octanoic acids. Among the aldehydes, propanal and pentanal had high odor activity values and likely contributed to the aroma of this cheese. The concentrations of butanoic, pentanoic, hexanoic, heptanoic, octanoic, and nonanoic acids increased significantly in goat milk Jack cheese throughout aging. The extracted enzymes from lysed bacterial cultures that were added to the cheeses during manufacturing caused considerable increases in the concentrations of butanoic and hexanoic acids compared with the control. However, the lower concentration of peptidases resulted in an increased concentration of butanal, whereas more peptidases resulted in a lower concentration of 2-nonanone in goat milk Jack cheeses.

Caseins (alpha(s1)-, alpha(s2)-, and beta-casein) are phosphoproteins that are capable of binding transition metals and scavenging free radicals; this property makes them good candidates to be used as natural antioxidants in oil-in-water emulsions. Caprine casein exhibits variability in alpha(s1)-casein content generated by genetic polymorphism. This variability in composition could lead to altered antioxidant properties. Thus, the ability of two caprine caseins differing in alpha(s1)-casein content to inhibit lipid oxidation in algae oil-in-water emulsions at 5% oil was investigated and compared to bovine caseinate. All caseins inhibited the formation of lipid oxidation at pH 7.0 as determined by lipid hydroperoxides and thiobarbituric acid reactive substances (TBARS). However, caprine caseins were in general more effective inhibitors of lipid oxidation than the bovine caseins, which may be attributed to their altered casein amino acid content and/or metal binding capabilities. The combination of the carotenoids with bovine and caprine caseins was highly effective at repressing oxidation leading to the speculation that the caseins may inhibit the loss of the carotenoids and/or react with and enhance the carotenoid activity; again some differences between bovine and caprine caseins were observed with caprine caseins being slightly more effective in the presence of carotenoids.

Lutein is an important xanthophyll carotenoid with many benefits to human health. Factors affecting the application of lutein as a functional ingredient in low-fat dairy-like beverages (pH 6.0-7.0) are not well understood. The interactions of bovine and caprine caseins with hydrophobic lutein were studied using UV/visible spectroscopy as well as fluorescence. Our studies confirmed that the aqueous solubility of lutein is improved after binding with bovine and caprine caseins. The rates of lutein solubilization by the binding to bovine and caprine caseins were as follows: caprine α-II-casein 34%, caprine α-I-casein 10%, and bovine casein 7% at 100 μM lutein. Fluorescence of the protein was quenched on binding supporting complex formation. The fluorescence experiments showed that the binding involves tryptophan residues and some nonspecific interactions. Scatchard plots of lutein binding to the caseins demonstrated competitive binding between the caseins and their sites of interaction with lutein. Competition experiments suggest that caprine α-II casein will bind a larger number of lutein molecules with higher affinity than other caseins. The chemical stability of lutein was largely dependent on casein type and significant increases occurred in the chemical stability of lutein with the following pattern: caprine α-II-casein > caprine α-I-casein > bovine casein. Addition of arabinogalactan to lutein-enriched emulsions increases the chemical stability of lutein-casein complexes during storage under accelerated photo-oxidation conditions at 25°C. Therefore, caprine α-II-casein alone and in combination with arabinogalactan can have important applications in the beverage industry as carrier of this xanthophyll carotenoid (lutein).