Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2435806 | International Dairy Journal | 2007 | 8 Pages |
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.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Food Science
Authors
Alina Wilińska, Jolanta Bryjak, Viera Illeová, Milan Polakovič,