Casein compositional studies: 1. The composition of casein from Friesian herd milks

Abstract

Casein composition in Friesian herd milks was examined by quantitative column chromatography on hydroxyapatite. Whole casein was resolved into 5 fractions: (1) γ-casein + para-κ-casein; (2) κ-casein + unidentified chymosin-resistant components; (3) unidentified minor protein; (4) β-casein; (5) αs1,0- + minor αs-caseins. Protein in fractions 1, 2, 4, 5 was measured by ultraviolet spectrometry, using appropriate specific absorption coefficients. The quantitative contribution of chymosin-resistant components to the κ-casein fraction was measured by a method involving hydroxyapatite chromatography of chymosin-treated whole casein. Compositional analysis was carried out throughout a lactation cycle on a total of 24 casein samples from the milks of a winter/spring calving and autumn-calving herd. Average composition (expressed as % total casein), which was similar for both herds, was 48·7% αs-, 33·8% β-, 4·9% γ-, 9·5% κ- and 3·2% unidentified components. Lactational effects on composition were also similar for both herds and were most pronounced in late lactation where increases were recorded in γ-casein and unidentified components, and decreases in β- and αs-caseins. Fluctuations in κ-casein proportions were small and slightly higher values were obtained in early and late lactation. Casein composition also appeared to be affected to some extent by season, as shown by differences in the proportions of αs-caseins and unidentified components between mid-lactation milks from the 2 herds. Compositional variations resulted partly from the action of milk proteinase on β-casein and also, apparently, from differences in relative rates of protein biosynthesis.