Fine Modulation of the Catalytic Properties of Rhizomucor miehei Lipase Driven by Different Immobilization Strategies for the Selective Hydrolysis of Fish Oil

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dc.contributor.authorYousefi, Maryam
dc.contributor.authorMarciello, Marzia
dc.contributor.authorGuisan, José Manuel
dc.contributor.authorFernandez-Lorente, Gloria
dc.contributor.authorMohammadi, Mehdi
dc.contributor.authorFilice, Marco
dc.date.accessioned2023-06-17T09:18:48Z
dc.date.available2023-06-17T09:18:48Z
dc.date.issued2020-01-27
dc.description.abstractFunctional properties of each enzyme strictly depend on immobilization protocol used for linking enzyme and carrier. Different strategies were applied to prepare the immobilized derivatives of Rhizomucor miehei lipase (RML) and chemically aminated RML (NH2-RML). Both RML and NH2-RML forms were covalently immobilized on glyoxyl sepharose (Gx-RML and GxNH2-RML), glyoxyl sepharose dithiothreitol (Gx-DTT-RML and Gx-DTT-NH2-RML), activated sepharose with cyanogen bromide (CNBr-RML and CNBr-NH2-RML) and heterofunctional epoxy support partially modified with iminodiacetic acid (epoxy IDA-RML and epoxy-IDA-NH2-RML). Immobilization varied from 11% up to 88% yields producing specific activities ranging from 0.5 up to 1.9 UI/mg. Great improvement in thermal stability for Gx-DTT-NH2-RML and epoxy-IDA-NH2-RML derivatives was obtained by retaining 49% and 37% of their initial activities at 70 ◦C, respectively. The regioselectivity of each derivative was also examined in hydrolysis of fish oil at three different conditions. All the derivatives were selective between cis-5,8,11,14,17-eicosapentaenoic acid (EPA) and cis-4,7,10,13,16,19-docosahexaenoic acid (DHA) in favor of EPA. The highest selectivity (32.9 folds) was observed for epoxy-IDA-NH2-RML derivative in the hydrolysis reaction performed at pH 5 and 4 ◦C. Recyclability study showed good capability of the immobilized biocatalysts to be used repeatedly, retaining 50–91% of their initial activities after five cycles of the reaction.
dc.description.departmentDepto. de Química en Ciencias Farmacéuticas
dc.description.facultyFac. de Farmacia
dc.description.refereedTRUE
dc.description.sponsorshipComunidad de Madrid/ FEDER
dc.description.sponsorshipUniversidad Complutense de Madrid/Comunidad de Madrid
dc.description.sponsorshipNational Institute of Genetic Engineering and Biotechnology
dc.description.statuspub
dc.eprint.idhttps://eprints.ucm.es/id/eprint/69260
dc.identifier.doi10.3390/molecules25030545
dc.identifier.issn1420-3049
dc.identifier.officialurlhttps://doi.org/10.3390/molecules25030545
dc.identifier.relatedurlhttps://www.mdpi.com/1420-3049/25/3/545
dc.identifier.urihttps://hdl.handle.net/20.500.14352/8581
dc.issue.number3
dc.journal.titleMolecules
dc.language.isoeng
dc.page.initial545
dc.publisherMDPI
dc.relation.projectIDNIETO-CM (B2017-BMD3731)
dc.relation.projectID2017-T1/BIO-4992
dc.relation.projectID587
dc.rightsAtribución 3.0 España
dc.rights.accessRightsopen access
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/es/
dc.subject.cdu547
dc.subject.keywordlipase immobilization
dc.subject.keywordRhizomucor miehei lipase
dc.subject.keywordoriented immobilization
dc.subject.keywordprotein chemical modification
dc.subject.keywordfish oil hydrolysis
dc.subject.keywordomega-3 polyunsaturated fatty acids
dc.subject.ucmQuímica farmaceútica
dc.subject.unesco2390 Química Farmacéutica
dc.titleFine Modulation of the Catalytic Properties of Rhizomucor miehei Lipase Driven by Different Immobilization Strategies for the Selective Hydrolysis of Fish Oil
dc.typejournal article
dc.volume.number25
dspace.entity.typePublication
relation.isAuthorOfPublicationb66b3a6e-1c2b-4ffe-b371-afb239918774
relation.isAuthorOfPublication5a0a21c2-f525-4c2c-a3b2-ab78f25604b1
relation.isAuthorOfPublication.latestForDiscoveryb66b3a6e-1c2b-4ffe-b371-afb239918774
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