초록
<P><B>Abstract</B></P> <P>This work examined catalytic specificity and fatty acid selectivity of five liquid lipases <I>C. antarctica</I> lipase A and B (CAL-A/B), and lipase TL (<I>T. lanuginosus</I>), Eversa Transfrom and NS in ethanolysis of fish oil with the aim to concentrate n-3 PUFAs into monoacylglycerols (MAGs) products. Lipase TL, Eversa Transform & NS entail a much faster reaction and produce higher MAGs yield (>30%); whereas CAL-A obtains the highest concentration of n-3 PUFAs/DHA/EPA into MAGs products (88.30%); followed by lipase NS (81.02%). <SUP>13</SUP>C NMR analysis indicates that CAL-B and lipase TL are sn-1,3 specific; but CAL-A and lipase Eversa Transform are non-regiospecific or weak sn-2 specific; which plausibly explains high enrichment effect of the latter two lipases. All liquid lipases are observed reusable for a certain times (lipase Eversa Transform up to 12 times), demonstrating their competitive advantage over immobilized form for industrial application because of their higher activity and cheaper operation cost.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Five liquid lipases are examined for catalytic ethanolysis of fish oil to produce MAGs. </LI> <LI> Lipase TL, Eversa Transform & NS afford faster reaction/higher MAGs yield (>30%). </LI> <LI> CAL-A gives MAGs containing the highest n-3 PUFAs (88%), followed by lipase NS (81%). </LI> <LI> <SUP>13</SUP>C NMR analysis indicates CAL-A/lipase Eversa Transform are non-regiospecific. </LI> <LI> Higher activity/lower operation cost endows liquid lipases with competitive advantage. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>