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- W2009282007 abstract "The thermal inactivation of alkaline phosphatase (ALP) in raw bovine and caprine milk was investigated in the temperature range 54 to 69 °C. To assess the stabilizing effect of milk compounds on ALP, inactivation experiments were also carried out in 0.1 m potassium phosphate buffer, pH 6.6. Each set of inactivation experiments was fitted simultaneously using kinetic models that were based on either one-step or two-step mechanisms. The parameters of the Arrhenius equation showed that the stabilization effect of milk compounds on ALP had an entropic character. They also indicated a different structure of bovine and caprine milk ALPs, which was reflected by a higher stability of the bovine milk enzyme." @default.
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- W2009282007 date "2007-06-01" @default.
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- W2009282007 title "Kinetics of thermal inactivation of alkaline phosphatase in bovine and caprine milk and buffer" @default.
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- W2009282007 doi "https://doi.org/10.1016/j.idairyj.2006.08.008" @default.
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