Abstract
The activities of four immobilized lipases for glycerolysis of a commercially available fish oil (TG500) rich in eicosapentaenoic residues (>58%, w/w) have been characterized in solvent-free systems. The effects of the mole ratio of TG500 to glycerol and temperature have been investigated. The highest conversion was obtained at 60 °C with a Candida antarctica fraction B lipase (Chirazyme L-2) and a mole ratio of TG500 (based on fatty acid equivalents) to glycerol of 1.5 to 1.
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Torres, C., Lin, B. & Hill, C.G. Lipase-catalyzed glycerolysis of an oil rich in eicosapentaenoic acid residues. Biotechnology Letters 24, 667–673 (2002). https://doi.org/10.1023/A:1015298728683
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DOI: https://doi.org/10.1023/A:1015298728683