EN
The paper difines the effect of casein carboxyl groups exterification on the following parameters of casein: thermal stability, stability against calcium and ethanol, hydration level, interaction with β-lactoglobulin, thermal stability of the resultant protein complex, electrophoretic properties, and the UV absorption spectrum. The results make it possible to suppose that organization of a casein micelle depends on hydrophobic interactions between casein fractions. The interactions result in formation of sub-units inside the micelle.