Temperature-dependent dissociation of human micellar β-casein: Implications of its phosphorylation degrees and casein...

Temperature-dependent dissociation of human micellar β-casein regarding its phosphorylation degrees and micelle structures were studied. Human milk was fractionated at 25 °C into soluble (S-25 °C) and micellar (M-25 °C) fractions, and the latter was fractionated at 4 °C into soluble (S-4 °C) and micellar (M-4 °C) fractions. β-casein ratios among S-25 °C, S-4 °C and M-4 °C were 19%, 59% and 22%. β-casein isoforms were predominated by 0-P, 1-P and 2-P in S-25 °C, by 0-P, 1-P, 2-P and 4-P in S-4 °C, and by 0-P in M-4 °C. For micelles remained after dissociation of β-casein and calcium, the size increased, molar mass decreased, morphologies were maintained, and internal protein inhomogeneities disappeared, compared with micelles in M-25 °C. β-casein isoforms with lower phosphorylation degrees may form a frame mainly through hydrophobic interactions, attached with more highly phosphorylated isoforms and colloidal calcium phosphate via calcium bridges for forming human micelle.