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Department of Dairy Technology, The Ohio State University, Columbus
ABSTRACT
Sephadex gel filtration and ultracentrifugation at temperatures up to 8.5 C demonstrated a reversible heat-induced dissociation of the alpha-casein complex into
s1-casein and
-casein, which occurred between 45 and 54 C. Presumably, the dissociation is the result of a transition from predominantly hydrophilic interactions (hydrogen bonds) between
s1- and
-casein at low temperature to hydrophobic interactions involving only
-casein at elevated temperature.
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