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On the Nature of Milk Lipase(S)

Department of Dairy Science, The Pennsylvania State University, University Park

ABSTRACT

We wish to bring to the attention of those interested in research on the nature of milk lipase or, for that matter, of lipases in general, certain observations concerning the chemical properties of casein which may bear on the problem. Our studies (3, 4) of lactose decomposition in heated milk have indicated that casein acts in the manner of a strong basic catalyst, even though its medium exhibits pH of 6.6. Similarly, on the basis of several reactions of casein in the "dry" state, Lea et al. (2) have noted that the surface of the protein appears to provide a more alkaline environment than would be expected from the pH of the solution before drying. It is generally recognized that these base properties of casein result from the epsilon amino groups of lysine (5), although other protein groups, such as the guanidyl group of arginine, may be involved to some extent.