• Korean Journal of Food Science and Technology
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• v.10 no.4
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• pp.409-414
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• 1978

The total amount of lipid content in the mullet roe is 20.5%, and iodine value and unsaponifiable matters content are 118 and 38.7%, respectively. The lipid composition of the muscle, roe and liver of the mullet, Mugil cephalus, shows differences. Triglyceride, wax esters, and free fatty acids are mainly contained in the lipids of the muscle, roe and liver, respectively. The mullet roe lipids are mainly composed of 59.1% of wax esters with a trace of sterol esters, 26.9% of polar lipids with pigments, 9.0% of triglyceride plus a trace of free fatty alcohols and fatty acids, and 3.0% of sterol contaminated with a trace of fatty alcohols. The major fatty acids of wax esters are C16 : 0, 47.5%, C18 : 1, 23.0%, C16 : 3, 6.5%, C20 : 5, 4.0%, those of triglyceride are C16 : 1, 25.1%, C18: 1, 16.7%, C16 : 0, 16.3%, C22 : 1, 7.9%, C18 : 0, 5.5%, C22 : 6, 4.4%, and those of polar lipids are C16 : 0, 35.0%, C18 : 1, 24.7%, C16 : 1, 6.1%, C20 : 5, 5.3%, C22 : 6, 4.2%. The major alcohols of wax esters are 51.0% of cetyl alcohol, 18.2% of palmitoleyl alcohol, and 10.7% of oleyl alcohol, and considerable amounts of odd-numbered alcohols such as C15 : 0, C15 : 1, C17 : 0, C17 : 1 and C19 : 1 are also found.

• Journal of Microbiology and Biotechnology
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• v.11 no.6
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• pp.951-956
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• 2001

A 28-kDa extracellular lipase (pI 8.7) was purified to homogeneity from the culture supernatant of Trichosporon sp. Y- 11 by mmonium sulfate precipitation, DEAE-Sephadex A-50, Bio-Gel P-30, CM- Sephadex C-50, and Bio-Gel P- 10 chromatographies. The purified enzyme exhibited a specific activity of $2,741{\;}{\mu}mol/min/mg$ based on the hydrolysis of triolein, and the optimal hydrolysis activity was dentified at pH 8.0 and $40^{\circ}C$. The enzyme activity was inhibited by $Ag^+$ and enhanced by $Fe^{2+}$, $Fe^{3+}$, $Mg^{2+}$, $Mn^{2+}$, and $Li^{+}$. The enzyme activity exhibited for the hydrolysis of both tributyrin and trilinolein. The ester synthesis of unsaturated fatty acids with various alcohols catalyzed by the purified lipase in a nonaqueous medium or microaqueous system was also investigated. The esterification activity of the lipase increased with an increase of the carbon chain length in the alcohol. The synthesis rate of linoleic acid and oleyl alcohol was the highest with an optimal temperature and pH of $40^{\circ}C$ and 8.0, respectively. The water content and agitation also affected the esterification activity of the lipase.