The temperature of inactivation of ALP is slightly higher than that required for the destruction of pathogenic bacteria. The phosphatase enzyme should be inactivated by pasteurisation. Phosphatase enzymes are essential to many biological functions, because phosphorylation and dephosphorylation serve diverse roles in cellular regulation and signaling. Each monomer contains five cysteine residues, two zinc atoms and one magnesium atom crucial to its catalytic function, and it is optimally active at alkaline pH environments. 1 Alkaline Phosphatase test is used to indicate whether milk has been adequately pasteurised or whether it has been contaminated with raw milk after pasteurisation. Complete pasteurization will inactivate the enzyme to below levels which are detectable by conventional methods. This test is based on the principle that the alkaline phosphatase enzyme in raw milk liberates phenol from a disodium para-nitro phenyl phosphate and forms a yellow coloured complex at alkaline pH (Scharer, 1943). The acid phosphatase activity in milk increases four- to 10-fold during mastitis (Mullen, 1950). Whereas phosphatases remove phosphate groups from molecules, kinases catalyze the transfer of phosphate gro Introduction. The method given below is an expansion of phosphatase (residual) in milk to cheese (1). The alkaline phosphatase (ALP) is an enzyme normally present in raw milk and it is inactivated in conditions of heat treatment. ALP has the physiological role of dephosphorylating compounds. If the phosphatase test is not negative, there is a problem with pasteurisation or recontamination with unpasteurised milk. Alkaline phosphatase (ALP) activity in milk has been used to demonstrate correct pasteurization of milk since the 1930s. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function but in different structural forms suitable to the Alkaline Phosphatase (ALP) is an enzyme naturally present in all raw milks, which is used as an indicator of proper milk pasteurization. The buffer has been changed because it was found that carbonate ions are inhibitory to bovine ALPs (5). It was shown that the time–temperature conditions required to inactivate ALP were slightly higher than those required to kill Mycobacterium tuberculosis, the most heat resistant pathogen in raw milk at the time (Fox and Kelly 2006). Because a phosphatase enzyme catalyzes the hydrolysis of its substrate, it is a subcategory of hydrolases. If milk is properly pasteurized, alkaline phosphatase is inactivated. Alkaline phosphatase is a heat sensitive enzyme in milk that is used as indicator of pasteurization. However, the phosphatase action in cheese is due largely to the milk enzyme with the starter enzyme being of minor importance (Andrews & Alichanidis, 1975a). A phosphatase is an enzyme that uses water to cleave a phosphoric acid monoester into a phosphate ion and an alcohol. Lactoperoxidase is one of the most heat-stable enzymes found in milk.

Alkaline phosphatase, or basic phosphatase, is a homodimeric protein enzyme of 86 kilodaltons. It could therefore be used as a marker for mastitis along with lysozyme and NAGase.

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