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dc.contributor.authorGascón Pérez, Victoriaes_ES
dc.contributor.authorCastro-Miguel, Elsaes_ES
dc.contributor.authorDíaz-García, Manueles_ES
dc.contributor.authorBlanco Martín, Rosa Maríaes_ES
dc.contributor.authorSánchez Sánchez, Manueles_ES
dc.date.accessioned2018-03-19T12:36:02Z-
dc.date.available2018-03-19T12:36:02Z-
dc.date.issued2017-10-
dc.identifier.citationJournal of Chemical Technology and Biotechnology 92(10): 2583-2593 (2017)es_ES
dc.identifier.issn0268-2575-
dc.identifier.urihttp://hdl.handle.net/10261/162451-
dc.description.abstract[Background] Very recently, metal‐organic framework (MOF) materials have been postulated as emerging supports to achieve solid‐state enzyme‐contained biocatalysts. In this work, post‐synthesis and in situ strategies to immobilize β‐glucosidase and laccase on different MOF materials were studied. The MOF‐based supports, i.e. MIL‐53(Al), NH2‐MIL‐53(Al) and Mg‐MOF‐74, were prepared under soft and sustainable conditions (room temperature and pH values compatible with enzymatic activity), allowing development of the in situ strategy.es_ES
dc.description.abstract[Results] In both post‐synthesis and in situ approaches, the intercrystalline mesoporosity of the MOF‐based support favored the immobilization efficiency or the specific activity. The latter expressed as units per milligram of immobilized enzyme was higher in the post‐synthesis immobilization, whereas the biocatalysts prepared in situ gave much higher enzyme loading (over 85%) and lower enzyme leaching (around 5%). The in situ approach even worked in a non‐aqueous (N,N‐dimethylformamide) media in which the free enzyme was completely inactive. The immobilized enzymes are much larger than the structural pores of the MOFs.es_ES
dc.description.abstract[Conclusions] Enzymes can be efficiently immobilized on nanocrystalline MOFs prepared under soft and sustainable conditions despite the supports lacking large enough pores to host the enzymes. The in situ approach is very efficient capturing enzymes and preserving some of their activity even under adverse conditions. © 2017 Society of Chemical Industryes_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.publisherJohn Wiley & Sonses_ES
dc.relationMINECO/ICTI2013-2016/MAT2016‐77496‐Res_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccessen_EN
dc.subjectPost-synthesis enzyme immobilizationes_ES
dc.subjectB-glucosidasees_ES
dc.subjectIn situ immobilizationes_ES
dc.subjectMetal-organic frameworkes_ES
dc.subjectNanocrystallinityes_ES
dc.titleIn situ and post‐synthesis immobilization of enzymes on nanocrystalline MOF platforms to yield active biocatalystses_ES
dc.typeartículoes_ES
dc.identifier.doi10.1002/jctb.5274-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1002/jctb.5274es_ES
dc.identifier.e-issn1097-4660-
dc.embargo.terms2018-10-01es_ES
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
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