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Semi-crystalline Fe-BTC MOF material as an efficient support for enzyme immobilization

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dc.contributor.author Gascón, Victoria
dc.contributor.author Jiménez, Mayra Belen
dc.contributor.author Blanco, Rosa María
dc.contributor.author Sanchez-Sanchez, Manuel
dc.date.accessioned 2018-02-19T16:09:11Z
dc.date.issued 2018
dc.identifier.uri http://hdl.handle.net/10344/6581
dc.description peer-reviewed en_US
dc.description.abstract Metal-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. en_US
dc.language.iso eng en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Catalysis Today;304, pp. 119-126
dc.relation.uri https://doi.org/10.1016/j.cattod.2017.10.022
dc.rights This is the author’s version of a work that was accepted for publication in Catalysis Today. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Catalysis Today, 2018, 304, 119-126, https://doi.org/10.1016/j.cattod.2017.10.022 en_US
dc.subject biocatalyst en_US
dc.subject enzyme immobilization en_US
dc.subject Fe-BTC en_US
dc.subject in-situ en_US
dc.subject post-synthesis en_US
dc.subject laccase en_US
dc.subject lipase en_US
dc.title Semi-crystalline Fe-BTC MOF material as an efficient support for enzyme immobilization en_US
dc.type info:eu-repo/semantics/article en_US
dc.type.supercollection all_ul_research en_US
dc.type.supercollection ul_published_reviewed en_US
dc.identifier.doi 10.1016/j.cattod.2017.10.022
dc.contributor.sponsor Spanish State Research Agency en_US
dc.contributor.sponsor ERDF en_US
dc.relation.projectid MAT2016-77496-R (AEI/FEDER, UE) en_US
dc.date.embargoEndDate 2019-10-26
dc.embargo.terms 2019-10-26 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US


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