A lipase has been partially purified from the bile of salmon (<i>Salmo salar</i>) with an apparent molecular size of 35 kDa and pI of pH 5.25. The enzyme was shown to preferentially cleave C20:5 and C18:4 fatty acids from the liver triacylglycerol of cod (<i>Gadus morhua</i>) as well as hydrolyse sterol and wax ester substrates. The enzyme was shown to hydrolyse substrate optimally at pH 7.1 in the presence of both 0.3M sodium chloride and low concentrations of bile alcohol sulphates. Sodium taurocholate could also partially activate the enzyme in the absence or at low concentrations of the alcohol sulphates. The enzyme was inhibited by 1 mM phenylmethylsulphonyl fluoride and was therefore assumed to be a serine esterase similar to the carboxyl ester lipase of human milk. The salmon enzyme was similarly shown to cleave Sn-2 ester bonds of triacylglycerol after initial hydrolysis of an SN-1(3) bond. The human milk carboxyl lipase was similarly shown to preferentially cleave C20:5 and C18:4 fatty acids from the cod liver triacylglycerol.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:359635 |
| Date | January 1992 |
| Creators | Reece, P. |
| Publisher | University of Aberdeen |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
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