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Journal of Dairy Science Vol. 54 No. 9 1275-1281
© 1971 by American Dairy Science Association ®
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Purification and Properties of a Bovine Milk Lipase

R. L. Richter1 and H. E. Randolf

Department of Animal Science, Texas A&M University, College Station 77843

ABSTRACT

A low molecular weight lipase was isolated from clarifier slime. It was precipitated from a water extract of an aceton powder prepared from clarifier slime at 20 to 45% of saturation with (NH4)2SO4 and was purified by ultrafiltration. Final isolation was with Sephadex G-75. Estimated molecular weight was 8,500 for the enzyme which contained 7.6% carbohydrate. The enzyme exhibited maximum activity at pH 9.2 and 37 C. It hydrolyzed a simple short-chain fatty acid triglyceride faster than long-chain fatty acid triglycerides, but had little specificity for natural oil emulsions. Enzyme activity rapidly decreased at 37 C and only 16% of the original activity existed after 5 hr. Storage for 48 hours at 23 and at 4 C decreased lipase activity 75 and 23% with complete inactivation after 1 hour at 45 C.


FOOTNOTES

1 Present address: Department of Food Science and Industries, University of Minnesota, St. Paul 55101.







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Copyright © 1971 by the American Dairy Science Association ®.