Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis

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dc.contributor.authorFanchini Terrasan, César Rafael
dc.contributor.authorTrobo-Maseda, Lara
dc.contributor.authorMoreno-Pérez, Sonia
dc.contributor.authorCarmona, Eleonora Cano [UNESP]
dc.contributor.authorPessela, Benevides Costa
dc.contributor.authorGuisan, José Manuel
dc.contributor.institutionConsejo Superior de Investigaciones Científicas (CSIC)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2018-12-11T17:01:26Z
dc.date.available2018-12-11T17:01:26Z
dc.date.issued2016-05-01
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.en
dc.description.affiliationDepartamento de Biocatálisis Instituto de Catálisis y Petroleoquimica (ICP) Consejo Superior de Investigaciones Científicas (CSIC) Campus Universidad Autónoma de Madrid (UAM), Cantoblanco
dc.description.affiliationBiochemistry and Microbiology Department Biosciences Institute Univ. Estadual Paulista - UNESP, PO 199
dc.description.affiliationDepartamento de Biotecnología y Microbiología de Alimentos Instituto de Investigación en Ciencias de Los Alimentos (CIAL) Consejo Superior de Investigaciones Científicas (CSIC) Campus Universidad Autónoma de Madrid (UAM), Cantoblanco
dc.description.affiliationUnespBiochemistry and Microbiology Department Biosciences Institute Univ. Estadual Paulista - UNESP, PO 199
dc.format.extent614-623
dc.identifierhttp://dx.doi.org/10.1016/j.procbio.2016.02.014
dc.identifier.citationProcess Biochemistry, v. 51, n. 5, p. 614-623, 2016.
dc.identifier.doi10.1016/j.procbio.2016.02.014
dc.identifier.file2-s2.0-84959419764.pdf
dc.identifier.issn1359-5113
dc.identifier.scopus2-s2.0-84959419764
dc.identifier.urihttp://hdl.handle.net/11449/172612
dc.language.isoeng
dc.relation.ispartofProcess Biochemistry
dc.relation.ispartofsjr0,761
dc.rights.accessRightsAcesso aberto
dc.sourceScopus
dc.subjectEnzyme co-immobilization
dc.subjectPenicillium janczewskii
dc.subjectXylan hydrolysis
dc.subjectXylanase
dc.subjectα-l-arabinofuranosidase
dc.subjectβ-xylosidase
dc.titleCo-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysisen
dc.typeArtigo

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