Author:
Davies D. Thomas,Law Andrew J. R.
Abstract
SummaryThe caseinate complex in bovine milk was partitioned by differential centrifugation at both 20 and 4 °C into 4 micellar fractions and a fraction representing serum casein, and the protein composition of the fractions determined. At both temperatures the relative amount of κ-casein in the micellar caseins increased markedly and that of β-casein decreased appreciably with decreasing micelle size. The relative amount of αs2-casein also tended to decrease with decreasing micelle size, but the relative amounts of αs1- and γ-caseins, and an unidentified casein fraction, showed little systematic variation. The serum casein differed appreciably in composition from the micellar caseins, being very rich in β-casein and comparatively poor in αsl- and αs2-caseins, and the amount present at 4 °C was considerably greater than at 20 °C, with the increase being due almost entirely to β-casein, but with γ-casein also making a significant contribution. The changes in the composition and distribution of micellar and serum caseins induced by cooling milk at 4 °C were completely reversible when the milk was re-equilibrated at 20 °C for 18 h.
Publisher
Cambridge University Press (CUP)
Subject
Animal Science and Zoology,General Medicine,Food Science
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