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-LactalbuminDepartment of Food Science, University of Alberta, Edmonton, Alberta, Canada T6G 2P5
ABSTRACT
The role of calcium in thermal behavior of bovine ;-lactalbumin in the region; of pH 2.5 to 6.5 was studied by differential scanning calorimetry with model solutions of
-lactalbumin in simulated milk ultrafiltrate. When .1 M ethylene-diaminetetraacetate was used to chelate the calcium2+, major effects were an average decrease of 20°C of denaturation temperature, significant reduction of enthalpy of denaturation in simulated milk ultrafiltrate, and loss of ability of protein to regain its original tertiary structure. Calcium binding appeared to be essential for stabilization of
-lactalbumin.
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