Interactions in Micellar Solutions of β-Casein

E. Leclerc and P. Calmettes
Phys. Rev. Lett. 78, 150 – Published 6 January 1997
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Abstract

β-casein is a flexible amphiphilic milk protein which forms spherical micelles in very dilute solution. The magnitude of the weight-average interactions between the solute particles has been inferred from small-angle neutron scattering experiments. At relatively high protein concentrations the interactions between micelles are repulsive, whatever the temperature. At lower concentration these interactions vanish and become more and more attractive when the critical micelle concentration is approached. Although indispensable for micelle formation, this fact seems to have not been previously reported.

  • Received 24 June 1996

DOI:https://doi.org/10.1103/PhysRevLett.78.150

©1997 American Physical Society

Authors & Affiliations

E. Leclerc and P. Calmettes

  • Laboratoire Léon Brillouin (C.E.A.-C.N.R.S.), C.E.-Saclay, 91191 Gif-sur-Yvette cedex, France

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Vol. 78, Iss. 1 — 6 January 1997

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