Purification and Biochemical Characterization of an Acid-Stable Lipase from the Pyloric Caeca of Sardine (Sardinella aurita) |
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Authors: | Nabil Smichi Ahmed Fendri Raja Chaabouni Faouzi Ben Rebah Youssef Gargouri and Nabil Miled |
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Institution: | (1) Laboratoire de Biochimie et de G?nie Enzymatique des Lipases, ENIS route de Soukra, 3038 Sfax, Tunisia;(2) Institut National des Sciences et Technologies de la Mer, Sfax, 3018, Tunisia; |
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Abstract: | A lipolytic activity was located in the sardine digestive glands (pyloric caeca), from which a sardine digestive lipase (SaDL)
was purified. Pure SaDL has a molecular mass of 43 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis
analysis. The enzyme was found to be more active on short-chain triacylglycerols than on long-chain ones. SaDL does not present
the interfacial activation phenomenon. Control experiments were performed under the same experimental conditions, with dromedary
and turkey pancreatic lipases and showed a positive interfacial activation phenomenon. Sodium deoxycholate (NaDC) has an inhibitory
effect on the lipase activity. The pure enzyme lost 40% of its activity in presence of 8 mM NaDC. SaDL was found to be mostly
stable at low pH values. Interestingly, no colipase was detected in the sardine pyloric caeca. Analogous results were reported
for the scorpion and the crab digestive systems. This is in line with the idea that colipase might has evolved in mammal animals
simultaneously with the appearance of an exocrine pancreas. No similarity was found between the NH2-terminal amino acid residues of SaDL and those of lipases from the digestive tract of other species. Altogether, these results
suggest that SaDL is a member of a new group of lipases belonging to aquatic species. |
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