Lipase-catalyzed glycerolysis of an oil rich in eicosapentaenoic acid residues |
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| Authors: | Carlos Torres Betty Lin Charles G. Hill Jr. |
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| Affiliation: | (1) Department of Chemical Engineering, University of Wisconsin-Madison, 1415 Engineering Dr., Madison, WI 53706, USA |
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| 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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| Keywords: | eicosapentaenoic acid glycerolysis lipases omega-3 fatty acids solvent-free reaction |
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