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Journal of Dairy Science Vol. 81 No. 4 932-938
© 1998 by American Dairy Science Association ®
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Identification of Interactions Among Casein Gels Using Dissociating Chemical Agents

E. Lefebvre-Cases 1, E. Gastadaldi 1, V. Vidal 1, S. Marchesseu 1, A. Lagaude 1, J.-L. Cuq 1, and B. Tarodo De La Fuente 1

1 Laboratoire de Génie Biologique et Sciences des Aliments, Université Montpellier II, Montpellier 34095, Cedex 5, France

To evaluate the nature of the main interactions that are involved in the formation of casein gels made by the acidification or rennet coagulation of milk, we investigated the combined effects of ultracentrifugation and specific dissociating agents on protein solubilization. The method used was based on the ability of gelled proteins to resist the dissociating action of solutions of urea, sodium dodecyl sulfate, or EDTA. Results showed that hydrophobic interactions and calcium bonds were the most important forces involved in the rennet milk gel matrix; hydrophobic, hydrogen, and electrostatic interactions were homogeneously distributed in the gel formed from acidified milk.

Key Words: acid coagulation • rennet coagulation • protein interactions • dissociating agents

Submitted on April 2, 1997
Accepted on October 30, 1997




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M. C. Michalski, R. Cariou, F. Michel, and C. Garnier
Native vs. Damaged Milk Fat Globules: Membrane Properties Affect the Viscoelasticity of Milk Gels
J Dairy Sci, October 1, 2002; 85(10): 2451 - 2461.
[Abstract] [Full Text] [PDF]




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