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Journal of Dairy Science Vol. 39 No. 11 1523-1531
© 1956 by American Dairy Science Association ®
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The Specificity of Milk Lipase. III. Differential Inactivation1, 2,

E. N. Frankel3 and N. P. Tarassuk

Department of Dairy Industry, University of California, Davis

ABSTRACT

In the previous paper of this series (5) preliminary evidence of the presence of multiple lipolytic enzymes in milk was obtained on the basis of variation in the relative lipolytic activity in different milks toward different esters. This paper presents further evidence of the multiplicity of lipolytic enzymes in milk.

Several workers have inferred the presence of more than one lipase in milk from variation in the inactivation of lipolysis in different milks by heat (2, 19), formaldehyde (6, 7, 8, 19), and copper (6), and from variation in loss of tributyrinase activity from aging milk in the cold (11). However, comparing diferent milks is difficult because of variations in environment and stability of milk lipase to aging in the cold (17). Moreover, determining the extent of lipolysis and tributyrinase activity as measures of lipase concentration in milk may be questionable (4). Some basic differences found in the conditions necessary to activate lipolysis in milk also have been attributed to the presence of multiple lipase systems (16, 17, 18, 19).


FOOTNOTES

1 The data are part of a thesis presented to the Graduate School of the University of California by the senior author in partial fulfillment of the requirements for the degree of Doctor of Philosophy, January, 1956.

2 This study was supported in part by funds from the California Dairy Industry Advisory Board.

3 Present address: Northern Utilization Research Branch, USDA, Peoria, Illinois.







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