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Journal of Dairy Science Vol. 39 No. 10 1364-1374
© 1956 by American Dairy Science Association ®
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The Milk Lipase System. I. Effect of Time, pH and Concentration of Substrate on Activity1

D. P. Schwartz2, I. A. Gould and W. J. Harper

Department of Dairy Technology, The Ohio State University, Columbus

ABSTRACT

Herrington has presented two reviews of the literature on milk lipase (5, 6). The enzyme is acknowledged to have a pH optimum between 8 and 9, to hydrolyze tributyrin more readily than milk fat, and to be activated by various mechanical and thermal treatments of milk.

From time to time, attention has been focused on the possibility of the existence of more than one lipase in milk but, in general, the evidence to support this has been more speculative than conclusive (1, 7, 8, 10, 12, 13). Dorner and Widmer (1) noted that pasteurized, homogenized milk occasionally became rancid and suggested that two lipases may be present in milk, one more thermolabile than the other. These investigators also reported that the rancidity which occasionally developed in pasteurized milk was atypical in odor and flavor. Herrington and Krukovsky (7) postulated that a formalin-sensitive and a formalin-tolerant lipase exists in milk and that the concentration of the two enzymes varied in the milk of individual cows (8).

FOOTNOTES

1 Scientific paper 2-55, Department of Dairy Technology, The Ohio State University. Supported in part by funds presented to the Ohio State University by the Research Foundation for support of fundamental research.

2 Present address: Dairy Products Section, Eastern Utilization Research Branch, USDA, Washington, D. C.






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Copyright © 1956 by the American Dairy Science Association ®.