SUMMARYHigh performance gel chromatography of the casein micelles disaggregated by 6 m-urea was carried out on a TSK-GEL G4000SW column using 6 M-urea synthetic milk serum as the effluent. The eluate was divided into two fractions. Fast eluted fraction 1 decreased from 67·5 to 57·3% on reduction of casein micelles and was not observed in reduced colloidal phosphate-free casein micelles. Fraction 1 from reduced casein micelles contained 1·7 times as much Ca and Pi bound to casein as did whole casein micelles, while fraction 2 essentially contained only bound Ca. These facts indicated that fraction 1 of reduced casein micelles consisted of the casein aggregates cross-linked by colloidal Ca phosphate (CCP). Polyacrylamide-gel electrophoresis showed that fraction 1 of reduced casein micelles contained more αs1- and αs2-caseins and less β-casein than whole micellar casein. No κ-casein was detected in fraction 1 of reduced casein micelles. It is suggested that the ester phosphate groups of casein are the sites for interaction with CCP.

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SummaryIn order to examine the influence of micelle size on the formation of soluble casein brought about by heating concentrated milk, casein micelles were separated into 3 fractions by differential centrifugation. The micelles were dispersed in the ultrafiltrate of skim-milk and the preparations were concentrated to 1/2·5 of the original volume. When the concentrated milk samples were heated at 135–140 °C, a larger amount of soluble casein was formed from smaller micelles than from larger micelles. Only a slight effect on the formation of soluble casein on heating was observed when colloidal calcium phosphate (CCP) was removed from the large micelles to a level lower than that associated with the small micelles or when the CCP in the small micelles was increased to a level higher than that of the large micelles. The soluble caseins formed on heating from different sizes of micelles were similar in composition. The fact that the formation of soluble casein on heating was affected by micelle size may be ascribed to variation in the κ-casein content of micelles rather than to variation in CCP content.

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SummaryCasein micelles separated by ultracentrifugation of raw skim milk were dispersed at a casein concentration of 2·5% in simulated milk ultrafiltrate and dialysed against 10 mM-imidazole buffer (pH 7·0) at 5 °C. The amounts of colloidal Ca and inorganic P decreased from 77 to 11 mg and from 31 to 2 mg respectively in 100 ml during 72 h of dialysis. Micellar casein content was reduced to 43 and 11% after 48 and 72 h of dialysis respectively. In high-performance gel chromatography of casein micelles in the presence of 6 M-urea, fraction 1, consisting of the casein aggregates cross-linked by colloidal Ca phosphate (CCP) decreased during dialysis and the retention time of the peak of fraction 1 was prolonged, suggesting that the cross-linkage between CCP and casein molecules was disrupted. The dissociation rates of the individual casein constituents from the casein aggregates cross-linked by CCP during dialysis were in the order β-> αs1 - > αs2-casein. The higher the ester phosphate content, the slower was the dissociation rate of the individual casein constituent. It is suggested that the strength of interaction between CCP and casein molecules depends on the ester phosphate content.