Heat-related changes to the hydrophobicity of cheese whey correlate with levels of native beta-lactoglobulin and alpha-lactalbumin.

Correlations were identified between levels of the native whey proteins, beta-lactoglobulin and alpha-lactalbumin and the surface and total hydrophobicities of cheese whey in response to different heat treatments. Heat-induced changes in the native beta-lactoglobulin content and surface hydrophobicity of whey exhibited the most significant linear relationship while correlations between total hydrophobicity and the native proteins were less significant because of an atypical rise in the n-heptane-binding capacity of whey after high-temperature treatment. The content of native beta-lactoglobulin in whey was more sensitive to heating than the content of native alpha-lactalbumin, while heat-related changes in the total hydrophobicity of whey were generally greater than similar changes in surface hydrophobicity.