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dc.contributor.authorFanchini Terrasan, César Rafael-
dc.contributor.authorTrobo-Maseda, Lara-
dc.contributor.authorMoreno-Pérez, Sonia-
dc.contributor.authorCano Carmona, Eleonora-
dc.contributor.authorPessela, Benevides C.-
dc.contributor.authorGuisán, José Manuel-
dc.date.accessioned2017-05-22T11:37:18Z-
dc.date.available2017-05-22T11:37:18Z-
dc.date.issued2016-
dc.identifierdoi: 10.1016/j.procbio.2016.02.014-
dc.identifierissn: 1359-5113-
dc.identifiere-issn: 1873-3298-
dc.identifier.citationProcess Biochemistry 51(5): 614-623 (2016)-
dc.identifier.urihttp://hdl.handle.net/10261/150099-
dc.description.abstractDifferently activated agarose-based supports were evaluated for co-immobilization of a crude extract from Penicillium janczewskii containing xylanase, β-xylosidase and α-l-arabinofuranosidase activities. Adequately selecting support and immobilization conditions (8 h, using agarose with 10% crosslinking) increased enzyme levels substantially, mainly in relation to the xylanase (2-fold). A coating with dextran aldehyde MW 6000 Da, partially oxidized, covalently attached the enzymes to the support. Optimum activity was verified in the pH range 2-4, and at 50, 65 and 80 °C for the xylanase, α-l-arabinofuranosidase and β-xylosidase, respectively. The xylanase was highly thermostable retaining more than 70% of activity even after 24 h incubation at 60 and 70 °C; and at 80 °C its half-life was 1.7 h. The half-lives of the β-xylosidase and α-l-arabinofuranosidase at 50 °C were 2.3 and 3.8 h, respectively. The co-immobilization of the enzymes on a single support give raise to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the α-l-arabinofuranosidase presented high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles.-
dc.publisherElsevier-
dc.relation.isversionofPostprint-
dc.rightsopenAccess-
dc.subjectXylanase-
dc.subjectXylan hydrolysis-
dc.subjectβ-xylosidase-
dc.subjectα-l-arabinofuranosidase-
dc.subjectEnzyme co-immobilization-
dc.subjectPenicillium janczewskii-
dc.titleCo-immobilization and stabilization of xylanase, β-xylosidase and α-L-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis-
dc.typeArtículo-
dc.identifier.doi10.1016/j.procbio.2016.02.014-
dc.relation.publisherversionhttps://doi.org/10.1016/j.procbio.2016.02.014-
dc.date.updated2017-05-22T11:37:18Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.rights.licensehttp://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.relation.csic-
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