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Purification and biochemical properties of Hexaplex trunculus digestive lipase
► This is the first report of purification of lipase (mSDL) from the marine snail. ► This novel lipase has a high molecular mass of 70kDa. ► The N-terminal sequence was totally different to known lipases. ► The mSDL appears to be a member of a new group of lipases. ► Neither colipase, nor bile salts...
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Published in: | Process biochemistry (1991) 2012-12, Vol.47 (12), p.2434-2439 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | ► This is the first report of purification of lipase (mSDL) from the marine snail. ► This novel lipase has a high molecular mass of 70kDa. ► The N-terminal sequence was totally different to known lipases. ► The mSDL appears to be a member of a new group of lipases. ► Neither colipase, nor bile salts were detected.
Enzymes from fish and aquatic invertebrates have recently been characterized and their study has led to the emergence of some new applications of these classes of enzymes. However, very little is known about lipases from mollusks. A lipolytic activity was located in the marine snail digestive glands (hepatopancreas), from which a marine snail digestive lipase named mSDL was purified. Pure mSDL has a molecular mass of about 70kDa as determined by SDS/PAGE analysis. Unlike the known digestive lipases while acting at 37°C, the mSDL displayed its maximal activity on long and short-chain triacylglycerols at 50°C. A specific activity of 400U/mg and 100U/mg was obtained with TC4 or olive oil as substrate respectively. Only 25% of the maximal activity was measured at 37°C. Interestingly, neither colipase, nor bile salts were detected in the marine snail hepatopancreas, which suggests that colipase evolved in invertebrates simultaneously with the appearance of an exocrine pancreas and a true liver which produces bile salts. No similarity was found between the N-terminal amino acids sequence of the mSDL and those of the known digestive lipases. Altogether, these results suggest that the mSDL is a member of a new group of digestive lipases belonging to invertebrates. |
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ISSN: | 1359-5113 1873-3298 |
DOI: | 10.1016/j.procbio.2012.10.004 |