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dc.contributor.authorGascón Pérez, Victoriaes_ES
dc.contributor.authorJiménez, Mayra B.es_ES
dc.contributor.authorBlanco Martín, Rosa Maríaes_ES
dc.contributor.authorSánchez Sánchez, Manueles_ES
dc.date.accessioned2018-03-19T12:27:15Z-
dc.date.available2018-03-19T12:27:15Z-
dc.date.issued2018-04-15-
dc.identifier.citationCatalysis Today 304: 119-126 (2018)es_ES
dc.identifier.issn0920-5861-
dc.identifier.urihttp://hdl.handle.net/10261/162446-
dc.description.abstractMetal-organic frameworks (MOFs) have revolutionized the potential applications of nanoporous materials. One of the most recent and promising applications of these materials is their use as supports for enzyme immobilization. In this context, the in-situ (one-step) methodologies, which do not require the use of MOFs with pores larger than the enzyme to be immobilized, seem to be particularly encouraging. This work presents a systematic study of the semi-crystalline Fe-BTC MOF material (commercialized as Basolite F300) employed as support of the enzymes laccase and lipase through either in-situ or post-synthesis methodology. The presence of the enzyme in the resultant solid biocatalysts was proved by CHNS chemical analysis, thermogravimetric analysis, Bradford assays and by SDS-PAGE electrophoresis. The enzymatic activity of the resultant Fe-BTC-based biocatalysts was also tested. The in-situ approach is particularly relevant due to various reasons: (i) the enzyme immobilization is given in one step; (ii) it is rapid (10 min); (iii) it is very efficient in terms of encapsulation capacity (≥98% for laccase and ≥87% for lipase); (iv) the enzymes are fully retained and no leaching is observed after an initial release of only around 10% of the enzyme molecules weakly immobilized; and (v) the activity of the retained enzyme can be substantially maintained (97% with respect to the free enzyme in the case of lipase). Any of these parameters systematically improves these given by the post-synthesis (two-step) approach. Moreover, Fe-BTC widely surpasses the benefits given by other MOF-based supports either by in-situ or post-synthesis approaches.es_ES
dc.description.sponsorshipThis work has been partially financed by the Spanish State Research Agency (Agencia Española de Investigación, AEI) and the European Regional Development Fund (Fondo Europeo de Desarrollo Regional, FEDER) through the Project MAT2016-77496-R (AEI/FEDER, UE).es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.relationinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/MAT2016-77496-Res_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccessen_EN
dc.subjectBiocatalystes_ES
dc.subjectEnzyme immobilizationes_ES
dc.subjectFe-BTCes_ES
dc.subjectIn-situes_ES
dc.subjectMOFes_ES
dc.subjectPost-synthesises_ES
dc.subjectLaccasees_ES
dc.subjectLipasees_ES
dc.titleSemi-crystalline Fe-BTC MOF material as an efficient support for enzyme immobilizationes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1016/j.cattod.2017.10.022-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.cattod.2017.10.022es_ES
dc.embargo.terms2020-04-15es_ES
dc.rights.licensehttp://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.contributor.funderEuropean Commissiones_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairetypeartículo-
item.cerifentitytypePublications-
item.languageiso639-1en-
item.grantfulltextopen-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextWith Fulltext-
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