Studies on the interaction between .ALPHA.SI- and .BETA.-caseins.

DOI DOI Open Access
  • YOSHIKAWA Masaaki
    Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
  • SUGIMOTO Etsuro
    Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
  • CHIBA Hideo
    Department of Food Science and Technology, Faculty of Agriculture, Kyoto University

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  • Studies on the Interaction between α<sub>s1</sub>- and β-Caseins

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The interaction of αS1-casein with β-, dephosphorylated β-, γ- and R-caseins was studied. It was proved by the sedimentation velocity experiments that αSl-casein formed a complex with each of these components at 25°C in the presence of 3mM CaCl2.<br> In the presence of 10mM CaCl2, β- and dephosphorylated β-casein prevented the precipitation of αS1-casein and gave micelle-like turbid solutions. However, γ- and R-caseins, fragments of β-casein, did not stabilize αS1-casein. It was concluded from these results that β-casein interacted with αS1-casein through its hydropholic region corresponding to R-casein and that hydrophilic region of β-casein was responsible for the stabilization of αS1-casein.

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