Abstract
Lecitase Ultra® 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.
Highlights
Enzymes are excellent catalysts throughout the chemical industry, but they have two limitations: they are water-soluble and usually very unstable
At concentrations higher than 2 mg/mL, Lecitase mostly formed bimolecular aggregates, where two open structures of two enzyme molecules were associated though their active centers
The simultaneous immobilization on a solid support of the two molecules of the bimolecular aggregate of the open structure of Lecitase was proposed as a novel strategy to stabilize Lecitase
Summary
Enzymes are excellent catalysts throughout the chemical industry, but they have two limitations: they are water-soluble and usually very unstable. In contrast to most lipases, the open structure of Lecitase that is adsorbed and fixed to hydrophobic supports is hyperactivated, and only four times more stable compared with diluted soluble enzymes [5]. The isolated open form can be stabi lized by forming bimolecular aggregates associated with their active cente2rosft1h3at becom unexposed to the aqueous medium. At high1c.oncentrations, the isolated open form can be stabilized by forming bimolecular aggregates associated with their active centers that become unexposed to the aqueous medium. RAtst;ththisapt His,, lbyysinsiemreuslitdauneesoaurselypoiomrl-y reactiv mobilizing thfeotrwthoeeinntzeyrmmoelemcuollaercurelaecstitohnatwfiothrmthtehseuapgpgorret.gTahtee bsoimtohlaetcuitlacranagngortebgaetceoims feixed when dimismsooBcbiaaislteiezddataoitoniTavtndhsta–shitrfisoweiorxfopuaustanutsiimocroptfnniiaHonocnopenasrtnaeoofdrnotfmoritotceTihnonmTeilicsLpabe,rewxietrmocapehtrolwauaelncehrecegcidhcsueh.rolisansLrettehnhcareiogttsauogasgrmebehgesethahhtoteeeeusmrltoedeigfsdbipoT.ehnLevTLorehefre(yatFhnfisiedgirmaursgetirlgleaairsrte2igv[c)2,aeo]ltv.tyewTachlhloeaoenvsmsitenetaigcomiontenh-adechhisiogitohhneesir mobilization of the bimolecular aggregate on cyanogen bromide (CNBr)-activated agarose at pH 8.5 via the two amino termini of the aggregate At this pH, lysine residues are poorly reactive for the intermolecular reaction with the support. This was imatm4o◦Cb.ilAizfteerdimbmyoobniliez-aptiooni,ntthecosuvrafalcetanntt iwmasmreomboivliezdattoiofonrmotnheCimNmBorb-ialiczteidvcalotesedd astgruacrtuorsee at pH min ato4f t°hCe.eAnzfytmere.immobilization, the surfactant was removed to form the immobilized clo ture of the enzyme
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