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Purification of a lipase from the hepatopancreas of oil sardine (Sardinella longiceps linnaeus) and its characteristics and properties

✍ Scribed by M. K. Mukundan; K. Gopakumar; M. R. Nair


Book ID
102923448
Publisher
John Wiley and Sons
Year
1985
Tongue
English
Weight
568 KB
Volume
36
Category
Article
ISSN
0022-5142

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✦ Synopsis


Lipase has been purified from the hepatopancreas of oil sardine (Sardinellu longiceps) by defatting, water extraction, ammonium sulphate fractionation and chromatography on D E A E Sephadex and Sephadex G-100. The preparation was homogeneous on polyacrylamide disc gel electrophoresis and on gel filtration through Sephacryl S-200. The enzyme showed a molecular weight of 54000-57000 with 6.1% of carbohydrate. The p H and temperature optima of purified sardine lipase were 8 and 37Β°C respectively. Sardine lipase remained stable up to 45Β°C (15 min) and in the p H range 5 to 9.5. The K, values obtained for the substrates tributyrin and triacetin were 4X lo-' and 30X lo-', respectively. The effect of halogens and various metal ions on sardine lipase activity, substrate specificity, amino acid and carbohydrate composition are also reported.


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## Abstract Lipase activity in stomach and pyloric caeca, liver, intestine and red muscle of rohu (__Labeo rohita__ Hamilton), oil sardine (__Sardinella longiceps__ Linnaeus), mullet (__Liza subviridis__ Valenciennes) and Indian mackerel (__Rastrelliger kanagurta__ Cuvier) was studied. Distinct dif