A comparison of dogfish and porcine pancreatic lipases.
1. A 16-fold purification of lipase activity from the pancreas of the dogfish (Squalus acanthias) was obtained by preparative isoelectric focussing. 2. The dogfish enzyme has a higher pH optimum (8.5) and a broader spectrum of activity above and below its optimum than a commercial porcine lipase preparation (optimum, 7.5). 3. The temperature optimum of dogfish lipase was 35 degrees C and it displayed greater stability than the porcine lipase preparation towards higher temperatures in the absence of substrate. 4. Dogfish lipase was active against a broad range of triacylglycerols and a wax ester. It had greater relative activity against the latter than the porcine lipase but hydrolyzed low mol. wt fatty acids less readily. In general, the effect of temperature was less on the dogfish enzyme than the porcine one.
Rasco
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Department of Food Science and Nutrition, University of Massachusetts Marine Station, Gloucester 01930.
Hultin
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D000818:Animals; D004284:Dogfish; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D005232:Fatty Acids, Volatile / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000032:analysis*; D010179:Pancreas / Q000201:enzymology*; D013045:Species Specificity; D013552:Swine
D005232:Fatty Acids, Volatile; D008049:Lipase