Purification and Properties of a Bovine Milk Lipase

A low molecular weight lipase was isolated from elarifier slime. It was precipitated from a water extract of an acetone powder prepared from clarifier slime at 20 to 45% of saturation with (NH4)2S04 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.