Abstract
Summary Heating skimmilks at 110 to 140C caused extensive dephosphorization of the casein; the liberated phosphate accumulated in the inorganic colloidal fraction. Concentration of skimmilk to one-half of its original volume increased the rate of dephosphorization and preheating at 90C for 10min before concentrating decreased the rate in the 2:1 concentrate. At a given temperature, dephosphorization was slower in skimmilk than in sodium caseinate sols. The heat-induced dephosphorization of casein in skimmilk conformed to first-order kinetics with an energy of activation of 25 to 27kcal per mole. The free energy change of the activated complex was about 30kcal per mole and the entropy change −11 to −13cal per degree.
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