The status of casein micelles in chilled milk from the buffalo and the cow

Abstract

SummaryWhen milk was chilled for 12 and 24 h at 0 °C, a decrease in the calcium and phosphorus contents of the casein micelle of both buffalo and cow's milk was observed. This decrease was directly proportional to the cooling period. A proportionate increase with cooling in the sialic-acid content of the casein micelle of chilled milk was noticed. Casein micelle isolated from chilled milk exhibited low opacity compared with the normal counterpart.A decrease in micellar casein and an increase in soluble casein were observed in both buffalo and cow's milk, in proportion to the cooling period. Similar results were obtained when casein micelles were resuspended in milk dialysate and centrifuged.Casein micelles from chilled milk showed different patterns on starch-gel electrophoresis compared with normal micelles. The intensity of the κ-casein band was relatively higher in the chilled samples. Gel-filtration studies suggest that some molecular rearrangement occurs in the casein micelle when milk is chilled.The release of sialopeptide from micellar casein by rennet was not influenced by chilling. However, a decrease in the rate of turbidity development in renneted suspensions of casein micelles was noted in chilled milk, which suggests a change in the structure of the casein micelle.No difference was noticed between buffalo and cow's milk in these respects.