Lipase-catalyzed glycerolysis of an oil rich in eicosapentaenoic acid residues

Author: Torres C.  

Publisher: Springer Publishing Company

ISSN: 0141-5492

Source: Biotechnology Letters, Vol.24, Iss.9, 2002-05, pp. : 667-673

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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.