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Symposium: Dynamic State of Milk

Phosphatase Reactivation

Milk and Food Research, Robert A. Taft Sanitary Engineering Center, U. S. Department of Health, Education, and Welfare, Public Health Service, Cincinnati, Ohio

ABSTRACT

The relationship between thermal inactivation of phosphatase and the pasteurization of milk has been of great value to regulatory agents in milk control. While this enzyme is a constituent of normal raw milk, there is no evidence to indicate it has a role in the nutritional aspects of milk; consequently, phosphatase probably functions solely in synthesis and is an incidental additive during milk secretion (6). The significance of phosphatase in pasteurized milk products has public health importance, since its presence indicates improper pasteurization or contamination by raw milk.

The enzyme in question is technically known as alkaline phosphomonoesterase, so named because it is capable of hydrolyzing monoesters of phosphoric acid in an alkaline environment. Phosphatase, like other enzymes, undoubtedly exists in a specific, highly organized structure consisting chiefly of protein. The enzyme is intimately associated with milk fat and apparently adsorbed to phospholipid particles of the fat globule membrane, referred to as microsomes (9).