Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis
Autor(a) principal: | |
---|---|
Data de Publicação: | 2016 |
Outros Autores: | , , , , |
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. |
id |
UNSP_60b61d735a5d4618442530aed4cd99f6 |
---|---|
oai_identifier_str |
oai:repositorio.unesp.br:11449/172612 |
network_acronym_str |
UNSP |
network_name_str |
Repositório Institucional da UNESP |
repository_id_str |
2946 |
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 |
|
_version_ |
1808128823017865216 |