Enzymatic synthesis of structured lipids from single cell oil of high docosahexaenoic acid content

The lipase-catalyzed acidolysis of a single-cell oil (SCO) containing docosahexaenoic acid (DHA) and docosapentaenoic acid (DPA) with caprylic acid (CA) was investigated. The targeted products were structured lipids containing CA residues at the sn-1 and -3 positions and a DHA or DPA residue at the sn-2 position of glycerol. Rhizomucor miehei lipase (RML) and Pseudomonas sp. KWI-56 lipase (PSL) were used as the biocatalysts. When PSL was used >60 mol% of total SCO fatty acids (FA) were exchanged with CA, with DHA and DPA as well as the other saturated FA being exchanged. The content of the triacylglycerols (TG) containing two CA and one DHA or DPA (number of carbon atoms = 41, i.e., C41) residue was high (36%), and the isomer with the desired configuration (unsaturated FA residue at the sn-2 position) represented 77-78% of C41. In the case of RML, CA content reached only 23 mol% in the TG. A large amount of DHA and DPA residues remained unexchanged with RML, so that the resulting oil was rich in TG species containing two or three DHA or DPA residues (46%). TG C41 amounted to 22%, almost all of which had the desired configuration. This result suggested that the difference in the degree of acidolysis by the two enzymes was due to their different selectivity toward DHA and DPA, as well as the difference in their positional specificities.