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Dephosphorization of Casein by Heat Treatment. II. In Skimmilks¹

Department of Agricultural Biochemistry, University of Minnesota, St. Paul

ABSTRACT

Heating skimmilks at 110 to 140 C 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 90 C for 10 min 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 27 kcal per mole. The free energy change of the activated complex was about 30 kcal per mole and the entropy change –11 to –13 cal per degree.

¹ Paper No. 4683, Scientific Journal Series, Minnesota Agricultural Experiment Station. Data presented herein are taken from a thesis presented by John Belec in partial fulfillment of the requirements for the degree of Master of Science, University of Minnesota, April, 1961.

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