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Purification of a lipase from the hepatopancreas of oil sardine ( Sardinella longiceps linnaeus ) and its characteristics and properties
Author(s) -
Mukundan M. K.,
Gopakumar K.,
Nair M. R.
Publication year - 1985
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740360310
Subject(s) - lipase , chromatography , sardine , sardinella , fractionation , chemistry , hepatopancreas , size exclusion chromatography , sephadex , food science , biochemistry , biology , enzyme , fishery , fish <actinopterygii>
Lipase has been purified from the hepatopancreas of oil sardine ( Sardinella longiceps ) by defatting, water extraction, ammonium sulphate fractionation and chromatography on DEAE 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 pH and temperature optima of purified sardine lipase were 8 and 37°C respectively. Sardine lipase remained stable up to 45°C (15 min) and in the pH range 5 to 9.5. The K m values obtained for the substrates tributyrin and triacetin were 4 × 10 −2 and 30 × 10 −2 , respectively. The effect of halogens and various metal ions on sardine lipase activity, substrate specificity, amino acid and carbohydrate composition are also reported.