Stabilization of Lecitase Ultra(R) by Immobilization and Fixation of Bimolecular Aggregates. Release of Omega-3 Fatty Acids by Enzymatic Hydrolysis of Krill Oil

Lecitase Ultra(R) solutions are mainly composed of bimolecular aggregates of two open structures of the enzyme. The immobilization and fixation of these bimolecular aggregates onto support surfaces is here proposed as a novel protocol for the immobilization and stabilization of Lecitase. The resulting derivatives of Lecitase aggregates were much more stable than the diluted solutions of the enzyme. The most stable of them was obtained by covalent immobilization of the bimolecular aggregate: 300-fold more stable than the diluted enzyme and 75-fold more stable than open Lecitase adsorbed onto hydrophobic supports. The bimolecular aggregate that adsorbed onto polyethyleneimine-agarose exhibited the best combination of activity and stability for the hydrolysis of krill oil. Omega-3 acids are in the sn-2 position of the krill oil, but they are also released by a phospholipase A1 because of migration issues.

Automated summary

The study proposes a novel protocol for immobilization and stabilization of Lecitase Ultra (R) by fixing bimolecular aggregates onto support surfaces, resulting in significantly increased stability compared to diluted enzyme solutions. The most stable derivative was obtained through covalent immobilization, showing a 300-fold increase in stability compared to diluted enzyme and 75-fold increase compared to open Lecitase adsorbed onto hydrophobic supports. The bimolecular aggregate adsorbed onto polyethyleneimine-agarose exhibited the best combination of activity and stability for hydrolysis of krill oil. Omega-3 acids in the krill oil at the sn-2 position are released by phospholipase A1 due to migration issues.