Studies on the digestive lipase of the surf clam Spisula solidissima
Document Type
Article
Date of Original Version
7-1-1973
Abstract
Crude molluscan lipase was prepared by homogenizing in tris buffer either fresh or lyophilized crystalline styles of Spisula solidissima. Both preparations showed specific activities less than 2% of standard hog pancreatic lipase, and pH and temperature optima of 8.0 and 20°C, respectively. When compared with mammalian hog pancreatic lipase, the clam lipase was found to be the more versatile enzyme on primary wax esters as well as methyl esters. Neither lipase was capable of hydrolyzing the oleate or palmitate esters of the secondary alcohols of glycerol, cholesterol or isopropyl alcohol; however, both showed activity on the oleate ester of isobutyl alcohol, a primary alcohol. S. solidissima lipase, hog pancreatic lipase, and a lipase isolated from the pancreas of the skate Raja erinacea, all demonstrated an inability to hydrolyze the methyl esters of eicosatetraenoic, eicosapentaenoic and docosahexaenoic acids. The lipase-resistant polyunsaturated fatty acid esters are discussed in terms of their role in the lipid biochemistry of marine organisms. © 1973 Springer-Verlag.
Publication Title, e.g., Journal
Marine Biology
Volume
21
Issue
1
Citation/Publisher Attribution
Patton, J. A., and J. G. Quinn. "Studies on the digestive lipase of the surf clam Spisula solidissima." Marine Biology 21, 1 (1973). doi: 10.1007/BF00351192.