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Amphiphile Nature of κ-Casein as the Basis for its Micelle Stabilizing Property

Nature volume 221, pages 635–639 (1969)Cite this article

Abstract

The N-terminal two-thirds of the milk micelle stabilizer κ-casein are hydrophobic and the C-terminal third is hydrophilic; the protein is an amphiphile. The two regions may function respectively to anchor the κ-casein molecule to the hydrophobic calcium αs-β-caseinate core and to provide a solvated coat which stabilizes the micelles against aggregation.

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Authors and Affiliations

  1. Department of Biochemistry, University of Sydney,

    R. J. HILL & R. G. WAKE

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  1. R. J. HILL
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  2. R. G. WAKE
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HILL, R., WAKE, R. Amphiphile Nature of κ-Casein as the Basis for its Micelle Stabilizing Property. Nature 221, 635–639 (1969). https://doi.org/10.1038/221635a0

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