Stabilization of Lecitase Ultra® by immobilization and fixation of bimolecular aggregates. Release of omega-3 fatty acids by enzymatic hydrolysis of krill oil

Stabilization of Lecitase Ultra® by immobilization and fixation of bimolecular aggregates. Release of omega-3 fatty acids by enzymatic hydrolysis of krill oil

This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis.

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Bibliographic Details
Main Authors: Andrés-Sanz, Daniel, Fresan, Cristina, Fernández-Lorente, Gloria, Rocha-Martín, Javier, Guisán, José Manuel
Other Authors: Ministerio de Ciencia, Innovación y Universidades (España)
Format: artículo biblioteca
Language:English
Published: Multidisciplinary Digital Publishing Institute 2021
Subjects:Immobilized phospholipase A1, Omega-3 fatty acids, Hydrolysis of krill oil, Stability of the open form of Lecitase,
Online Access:http://hdl.handle.net/10261/263406
http://dx.doi.org/10.13039/501100011033
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spelling dig-cial-es-10261-2634062022-12-20T13:52:54Z Stabilization of Lecitase Ultra® by immobilization and fixation of bimolecular aggregates. Release of omega-3 fatty acids by enzymatic hydrolysis of krill oil Andrés-Sanz, Daniel Fresan, Cristina Fernández-Lorente, Gloria Rocha-Martín, Javier Guisán, José Manuel Ministerio de Ciencia, Innovación y Universidades (España) Agencia Estatal de Investigación (España) Immobilized phospholipase A1 Omega-3 fatty acids Hydrolysis of krill oil Stability of the open form of Lecitase This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis. 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. This research was funded by Plan Nacional (Spanish Ministerio de Ciencia) Grant No. RTI2018-093583-B-I00. Peer reviewed 2022-03-09T08:49:41Z 2022-03-09T08:49:41Z 2021 artículo http://purl.org/coar/resource_type/c_6501 Catalysts 11(9): 1067 (2021) http://hdl.handle.net/10261/263406 10.3390/catal11091067 2073-4344 http://dx.doi.org/10.13039/501100011033 en #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-093583-B-I00/ES/INGENIERIA DE PROCESOS ENZIMATICOS EN SOLVENT-FREE SYSTEMS:SINTESIS DE FOSFOLIPIDOS ESTRUCTURADOS DE ACIDO DOCOSAHEXAENOICO PARA TRATAMIENTO DE ENFERMEDADES NEURODEGENERATIVAS/ Publisher's version https://doi.org/10.3390/catal11091067 Sí open Multidisciplinary Digital Publishing Institute
institution CIAL ES
collection DSpace
country España
countrycode ES
component Bibliográfico
access En linea
databasecode dig-cial-es
tag biblioteca
region Europa del Sur
libraryname Biblioteca del CIAL España
language English
topic Immobilized phospholipase A1
Omega-3 fatty acids
Hydrolysis of krill oil
Stability of the open form of Lecitase
Immobilized phospholipase A1
Omega-3 fatty acids
Hydrolysis of krill oil
Stability of the open form of Lecitase
spellingShingle Immobilized phospholipase A1
Omega-3 fatty acids
Hydrolysis of krill oil
Stability of the open form of Lecitase
Immobilized phospholipase A1
Omega-3 fatty acids
Hydrolysis of krill oil
Stability of the open form of Lecitase
Andrés-Sanz, Daniel
Fresan, Cristina
Fernández-Lorente, Gloria
Rocha-Martín, Javier
Guisán, José Manuel
Stabilization of Lecitase Ultra® by immobilization and fixation of bimolecular aggregates. Release of omega-3 fatty acids by enzymatic hydrolysis of krill oil
description This article belongs to the Special Issue Application of Immobilized Enzyme as Catalysts in Chemical Synthesis.
author2 Ministerio de Ciencia, Innovación y Universidades (España)
author_facet Ministerio de Ciencia, Innovación y Universidades (España)
Andrés-Sanz, Daniel
Fresan, Cristina
Fernández-Lorente, Gloria
Rocha-Martín, Javier
Guisán, José Manuel
format artículo
topic_facet Immobilized phospholipase A1
Omega-3 fatty acids
Hydrolysis of krill oil
Stability of the open form of Lecitase
author Andrés-Sanz, Daniel
Fresan, Cristina
Fernández-Lorente, Gloria
Rocha-Martín, Javier
Guisán, José Manuel
author_sort Andrés-Sanz, Daniel
title Stabilization of Lecitase Ultra® by immobilization and fixation of bimolecular aggregates. Release of omega-3 fatty acids by enzymatic hydrolysis of krill oil
title_short Stabilization of Lecitase Ultra® by immobilization and fixation of bimolecular aggregates. Release of omega-3 fatty acids by enzymatic hydrolysis of krill oil
title_full Stabilization of Lecitase Ultra® by immobilization and fixation of bimolecular aggregates. Release of omega-3 fatty acids by enzymatic hydrolysis of krill oil
title_fullStr Stabilization of Lecitase Ultra® by immobilization and fixation of bimolecular aggregates. Release of omega-3 fatty acids by enzymatic hydrolysis of krill oil
title_full_unstemmed Stabilization of Lecitase Ultra® by immobilization and fixation of bimolecular aggregates. Release of omega-3 fatty acids by enzymatic hydrolysis of krill oil
title_sort stabilization of lecitase ultra® by immobilization and fixation of bimolecular aggregates. release of omega-3 fatty acids by enzymatic hydrolysis of krill oil
publisher Multidisciplinary Digital Publishing Institute
publishDate 2021
url http://hdl.handle.net/10261/263406
http://dx.doi.org/10.13039/501100011033
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