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Título: | Stabilization of Lecitase Ultra® by immobilization and fixation of bimolecular aggregates. Release of omega-3 fatty acids by enzymatic hydrolysis of krill oil |
Autor: | Andrés-Sanz, Daniel; Fresan, Cristina; Fernández-Lorente, Gloria CSIC ORCID ; Rocha-Martín, Javier CSIC ORCID ; Guisán, José Manuel CSIC ORCID | Palabras clave: | Immobilized phospholipase A1 Omega-3 fatty acids Hydrolysis of krill oil Stability of the open form of Lecitase |
Fecha de publicación: | 2021 | Editor: | Multidisciplinary Digital Publishing Institute | Citación: | Catalysts 11(9): 1067 (2021) | Resumen: | 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. | Descripción: | This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis. | Versión del editor: | https://doi.org/10.3390/catal11091067 | URI: | http://hdl.handle.net/10261/263406 | DOI: | 10.3390/catal11091067 | E-ISSN: | 2073-4344 |
Aparece en las colecciones: | (CIAL) Artículos (ICP) Artículos |
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stabilizatioil.pdf | 2,58 MB | Adobe PDF | Visualizar/Abrir |
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