Effect of Oxidative Sardin Fish Oil for Food Utilization

Sardine is an economic fish industry product in Indonesia. Sardin fish oil of fish meal by-product can be processed into ethyl ester as a food grade product. The purpose of this study were to determine the chemical and physical the best ethyl ester of Semirefined and refined oil from sardine fish meal by-products. Results showed that heavy metals detected was cadmium (Cd) value, i.e. 0.02 ppm. SFA content of crude oil sardines was 29.39% with palmitic acid (16.24%) as the predominant fatty acids. The MUFA content amounted to 14.87% with palmitic acid as the predominant fatty acid (5.76%). The PUFA content were 35.47% with DHA (17.07%) as the predominant fatty acid, while EPA amounted to 13.82%. Semirefined oil transformed into Semirefined ethyl ester oil was the best on oxidative and physical parameters. Oxidation process produced Semirefined ethyl ester with 1.50±0.00 mEq/kg peroxide value (PV), 0.90±0.15% fatty<br />acids (% FFA), 5.46±0.32 mEq/kg Anisidin p-value (p-AV), 8.46±0.32 mEq/kg oxidation (TOTOKS), 62.15±0.27%T viscosity and and 5.65±0,26 cP clarity.

Caenorhabditis elegans mboa-7, a Member of the MBOAT Family, Is Required for Selective Incorporation of Polyunsaturated Fatty Acids into Phosphatidylinositol

Phosphatidylinositol (PI) is a component of membrane phospholipids, and it functions both as a signaling molecule and as a compartment-specific localization signal in the form of polyphosphoinositides. Arachidonic acid (AA) is the predominant fatty acid in the sn-2 position of PI in mammals. LysoPI acyltransferase (LPIAT) is thought to catalyze formation of AA-containing PI; however, the gene that encodes this enzyme has not yet been identified. In this study, we established a screening system to identify genes required for use of exogenous polyunsaturated fatty acids (PUFAs) in Caenorhabditis elegans. In C. elegans, eicosapentaenoic acid (EPA) instead of AA is the predominant fatty acid in PI. We showed that an uncharacterized gene, which we named mboa-7, is required for incorporation of PUFAs into PI. Incorporation of exogenous PUFA into PI of the living worms and LPIAT activity in the microsomes were greatly reduced in mboa-7 mutants. Furthermore, the membrane fractions of transgenic worms expressing recombinant MBOA-7 and its human homologue exhibited remarkably increased LPIAT activity. mboa-7 encodes a member of the membrane-bound O-acyltransferase family, suggesting that mboa-7 is LPIAT. Finally, mboa-7 mutants had significantly lower EPA levels in PI, and they exhibited larval arrest and egg-laying defects.