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

Detalhes bibliográficos
Autor(a) principal: Fanchini Terrasan, César Rafael
Data de Publicação: 2016
Outros Autores: Trobo-Maseda, Lara, Moreno-Pérez, Sonia, Carmona, Eleonora Cano [UNESP], Pessela, Benevides Costa, Guisan, José Manuel
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.procbio.2016.02.014
http://hdl.handle.net/11449/172612
Resumo: Differently 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.
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spelling Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysisEnzyme co-immobilizationPenicillium janczewskiiXylan hydrolysisXylanaseα-l-arabinofuranosidaseβ-xylosidaseDifferently 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.Departamento de Biocatálisis Instituto de Catálisis y Petroleoquimica (ICP) Consejo Superior de Investigaciones Científicas (CSIC) Campus Universidad Autónoma de Madrid (UAM), CantoblancoBiochemistry and Microbiology Department Biosciences Institute Univ. Estadual Paulista - UNESP, PO 199Departamento 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), CantoblancoBiochemistry and Microbiology Department Biosciences Institute Univ. Estadual Paulista - UNESP, PO 199Consejo Superior de Investigaciones Científicas (CSIC)Universidade Estadual Paulista (Unesp)Fanchini Terrasan, César RafaelTrobo-Maseda, LaraMoreno-Pérez, SoniaCarmona, Eleonora Cano [UNESP]Pessela, Benevides CostaGuisan, José Manuel2018-12-11T17:01:26Z2018-12-11T17:01:26Z2016-05-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article614-623application/pdfhttp://dx.doi.org/10.1016/j.procbio.2016.02.014Process Biochemistry, v. 51, n. 5, p. 614-623, 2016.1359-5113http://hdl.handle.net/11449/17261210.1016/j.procbio.2016.02.0142-s2.0-849594197642-s2.0-84959419764.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengProcess Biochemistry0,761info:eu-repo/semantics/openAccess2023-11-13T06:08:15Zoai:repositorio.unesp.br:11449/172612Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T17:32:33.618802Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis
title Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis
spellingShingle Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis
Fanchini Terrasan, César Rafael
Enzyme co-immobilization
Penicillium janczewskii
Xylan hydrolysis
Xylanase
α-l-arabinofuranosidase
β-xylosidase
title_short Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis
title_full Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis
title_fullStr Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis
title_full_unstemmed Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis
title_sort Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis
author Fanchini Terrasan, César Rafael
author_facet Fanchini Terrasan, César Rafael
Trobo-Maseda, Lara
Moreno-Pérez, Sonia
Carmona, Eleonora Cano [UNESP]
Pessela, Benevides Costa
Guisan, José Manuel
author_role author
author2 Trobo-Maseda, Lara
Moreno-Pérez, Sonia
Carmona, Eleonora Cano [UNESP]
Pessela, Benevides Costa
Guisan, José Manuel
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas (CSIC)
Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Fanchini Terrasan, César Rafael
Trobo-Maseda, Lara
Moreno-Pérez, Sonia
Carmona, Eleonora Cano [UNESP]
Pessela, Benevides Costa
Guisan, José Manuel
dc.subject.por.fl_str_mv Enzyme co-immobilization
Penicillium janczewskii
Xylan hydrolysis
Xylanase
α-l-arabinofuranosidase
β-xylosidase
topic Enzyme co-immobilization
Penicillium janczewskii
Xylan hydrolysis
Xylanase
α-l-arabinofuranosidase
β-xylosidase
description Differently 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.
publishDate 2016
dc.date.none.fl_str_mv 2016-05-01
2018-12-11T17:01:26Z
2018-12-11T17:01:26Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.procbio.2016.02.014
Process Biochemistry, v. 51, n. 5, p. 614-623, 2016.
1359-5113
http://hdl.handle.net/11449/172612
10.1016/j.procbio.2016.02.014
2-s2.0-84959419764
2-s2.0-84959419764.pdf
url http://dx.doi.org/10.1016/j.procbio.2016.02.014
http://hdl.handle.net/11449/172612
identifier_str_mv Process Biochemistry, v. 51, n. 5, p. 614-623, 2016.
1359-5113
10.1016/j.procbio.2016.02.014
2-s2.0-84959419764
2-s2.0-84959419764.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Process Biochemistry
0,761
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 614-623
application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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