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Hydrophobicity is thought to be one of the most important properties which affect the functionalities of proteins. The correlation between the hydrophobicity and such functional properties as the foaming, emulsifying and gel forming properties has been demonstrated by many investigators.1 ~3) The importance of the surface (effective) hydrophobicity of proteins in such functionalities was particularly emphasized and many methods for determining the surface hydrophobicity of proteins have been proposed. The fluorescent probe methods involving 8-anilinonaphthalene-l-sulfonate (ANS)4) and cisparinaric acid (ds-PnA)5) have been widely used to determine the surface hydrophobicity because of their simplicity. However, it is still questionable as to whether or not the hydrophobicity values obtained by these methods reflect the true hydrophobicities of the proteins. In this study, the hydrophobicity values for milk proteins obtained by the fluorescent probe methods were compared with those obtained by another three methods, hydrophobic affinity chromatography (reverse phase-high performance liquid chromatography), hydrophobic partition and heptane binding methods. Five major milk proteins (asl-casein, /?-casein, a-

Hydrophobicity and emulsifying activity of milk proteins.