pH-dependent structures and properties of casein micelles

• DOI: 10.1016/j.bpc.2008.03.012
• Publication Date: 2008-04-08T16:18:06Z
• Authors: Yan Liu; Rong Guo
• Keywords: Hydrophobic effect; Electrostatics; Turbidity

The association behavior of casein over a broad pH range has first been investigated by fluorescent technique together with DLS and turbidity measurements. Casein molecules can self-assemble into casein micelles in the pH ranges 2.0 to 3.0, and 5.5 to 12.0. The hydrophobic interaction, hydrogen bond and electrostatic action are the main interactions in the formation of casein micelles. The results show that the structure of casein micelles is more compact at low pH and looser at high pH. The casein micelle has the most compact structure at pH 5.5, when it has almost no electrostatic repulsion between casein molecules.