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Department of Food Science and Technology, University of Nebraska, Lincoln 68503
ABSTRACT
Purified bovine pancreatic lipase was highly unstable at and above refrigeration temperature. However, it could be stored frozen without loss of activity. Milk solids had some protective effect upon the enzyme against
-irradiation. Low concentrations of sodium, calcium, and magnesium salts stimulated lipolytic activity. However, heavy metal salts, such as ferric, cupric, and mercuric chlorides, were highly inhibitory. The bovine pancreatic lipase appeared to contain sulf-hydryl groups which may be essential for the lipolytic activity since p-chloromer-curibenzoate, N-ethylmaleimide, sodium arsenite, and iodoacetate inhibited the enzyme. A comparison of bovine pancreatic lipase and milk lipase revealed that the two enzymes were similar in thermal stability and effect of some of the activators and inhibitors on lipolytic activity.
1 Published with the approval of the Director as Paper No. 3900, Journal Series, Agricultural Experiment Station, Lincoln, NE. Research work was conducted on Project 16-17. This study was supported in part by grants from American Dairy Association and Dairy Research, Inc. (DRINC).
2 The Cary Memorial Hospital, 3 3 Lyndon Street, Caribou, ME 04736
3 Purity Cheese Company, Mayville, WI 53050.
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