Please use this identifier to cite or link to this item: https://hdl.handle.net/11000/4586
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dc.contributor.authorBello Gil, Daniel-
dc.contributor.authorMaestro García-Donas, Beatriz-
dc.contributor.authorFonseca, Jennifer-
dc.contributor.authorDinjaski, Nina-
dc.contributor.authorPrieto, M. Auxiliadora-
dc.contributor.authorSanz, Jesús M.-
dc.contributor.otherDepartamentos de la UMH::Bioquímica y Biología Moleculares
dc.date.accessioned2018-04-10T11:25:28Z-
dc.date.available2018-04-10T11:25:28Z-
dc.date.created2017-11-01-
dc.date.issued2018-04-10-
dc.identifier.issn0099-2240-
dc.identifier.issn1098-5336-
dc.identifier.urihttp://hdl.handle.net/11000/4586-
dc.description.abstractPolyhydroxyalkanoates (PHAs) are biodegradable polyesters that accumulate in the cytoplasm of certain bacteria. One promising biotechnological application utilizes these biopolymers as supports for protein immobilization. Here, the PHA-binding domain of the Pseudomonas putida KT2440 PhaF phasin (BioF polypeptide) was investigated as an affinity tag for the in vitro functionalization of poly-3- hydroxybutyrate (PHB) particles with recombinant proteins, namely, full-length PhaF and two fusion proteins tagged to BioF (BioF–C-LytA and BioF–_-galactosidase, containing the choline-binding module C-LytA and the _-galactosidase enzyme, respectively). The protein-biopolyester interaction was strong and stable in a wide range of pHs and temperatures, and the bound protein was highly protected from selfdegradation, while the binding strength could be modulated by coating with amphiphilic compounds. Finally, BioF–_-galactosidase displayed very stable enzymatic activity after several continuous activity-plus-washing cycles when immobilized in a minibioreactor. Our results demonstrate the potentialities of PHA and the BioF tag for the construction of novel bioactive materials.en
dc.description.sponsorshipThis work was supported by the Spanish Ministry of Economy and Competitiveness (grants BFU2010-17824)-
dc.description.sponsorshipThis work was supported by the Spanish Ministry of Economy and Competitiveness (Grants BIO2013-44878-R)-
dc.description.sponsorshipThis work was supported by the Spanish Ministry of Economy and Competitiveness (Grants BIO2013-47684-R)-
dc.description.sponsorshipThis work was supported by the Spanish Ministry of Economy and Competitiveness (Grants BIO2016-79323-R)-
dc.description.sponsorshipTthe Community of Madrid (Spain) (NanoBIOSOMA S20 1473 3/M lT-2807).-
dc.formatapplication/pdfen
dc.format.extent12es
dc.language.isoengen
dc.rightsinfo:eu-repo/semantics/openAccessen
dc.subjectPHBen
dc.subjectphasinsen
dc.subjectaffinity tagen
dc.subjectprotein immobilizationen
dc.subjectpolyhydroxyalkanoatesen
dc.subject.other57 - Biologíaes
dc.titlePoly-3-Hydroxybutyrate Functionalization with BioF-Tagged Recombinant Proteinsen
dc.typeinfo:eu-repo/semantics/articleen
dc.contributor.instituteInstituto de Biología Molecular y Celulares
dc.identifier.doi10.1128/AEM.02595-17-
dc.relation.publisherversionhttps://doi.org/10.1128/AEM.02595-17-
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Instituto de Biología Molecular y Celular


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