Characterization and biotechnological application of recombinant xylanases from Aspergillus nidulans

Detalhes bibliográficos
Autor(a) principal: Maitan-Alfenas, Gabriela P.
Data de Publicação: 2016
Outros Autores: Oliveira, Mariana B., Nagem, Ronaldo A.P., Vries, Ronald P. de, Guimarães, Valéria M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: http://dx.doi.org/10.1016/j.ijbiomac.2016.05.065
http://www.locus.ufv.br/handle/123456789/12449
Resumo: Two xylanases from Aspergillus nidulans, XlnB and XlnC, were expressed in Pichia pastoris, purified and characterized. XlnB and XlnC achieved maximal activities at 60 °C and pH 7.5 and at 50 °C and pH 6.0, respectively. XlnB showed to be very thermostable by maintaining 50% of its original activity after 49 h incubated at 50 °C. XlnB had its highest activity against wheat arabinoxylan while XlnC had the best activity against beechwood xylan. Both enzymes were completely inhibited by SDS and HgCl2. Xylotriose at 1 mg/ml also totally inibited XlnB activity. TLC analysis showed that the main product of beechwood xylan hydrolysis by XlnB and XlnC was xylotetraose. An additive effect was shown between XlnB and XlnC and the xylanases of two tested commercial cocktails. Sugarcane bagasse saccharification results showed that these two commercial enzymatic cocktails were able to release more glucose and xylose after supplementation with XlnB and XlnC.
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spelling Maitan-Alfenas, Gabriela P.Oliveira, Mariana B.Nagem, Ronaldo A.P.Vries, Ronald P. deGuimarães, Valéria M.2017-10-26T13:44:02Z2017-10-26T13:44:02Z2016-05-250141-8130http://dx.doi.org/10.1016/j.ijbiomac.2016.05.065http://www.locus.ufv.br/handle/123456789/12449Two xylanases from Aspergillus nidulans, XlnB and XlnC, were expressed in Pichia pastoris, purified and characterized. XlnB and XlnC achieved maximal activities at 60 °C and pH 7.5 and at 50 °C and pH 6.0, respectively. XlnB showed to be very thermostable by maintaining 50% of its original activity after 49 h incubated at 50 °C. XlnB had its highest activity against wheat arabinoxylan while XlnC had the best activity against beechwood xylan. Both enzymes were completely inhibited by SDS and HgCl2. Xylotriose at 1 mg/ml also totally inibited XlnB activity. TLC analysis showed that the main product of beechwood xylan hydrolysis by XlnB and XlnC was xylotetraose. An additive effect was shown between XlnB and XlnC and the xylanases of two tested commercial cocktails. Sugarcane bagasse saccharification results showed that these two commercial enzymatic cocktails were able to release more glucose and xylose after supplementation with XlnB and XlnC.engInternational Journal of Biological MacromoleculesV. 91, p.60–67, May 2015XylanaseAspergillus nidulansPichia pastorisSaccharificationSugarcane bagasseCharacterization and biotechnological application of recombinant xylanases from Aspergillus nidulansinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfinfo:eu-repo/semantics/openAccessreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINAL1-s2.0-S0141813016304779-main.pdf1-s2.0-S0141813016304779-main.pdftexto completoapplication/pdf1306401https://locus.ufv.br//bitstream/123456789/12449/1/1-s2.0-S0141813016304779-main.pdfa6521025c01e5b038cfe83fa427a516aMD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/12449/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAIL1-s2.0-S0141813016304779-main.pdf.jpg1-s2.0-S0141813016304779-main.pdf.jpgIM Thumbnailimage/jpeg4630https://locus.ufv.br//bitstream/123456789/12449/3/1-s2.0-S0141813016304779-main.pdf.jpg17a7a70ff3ae30b41034b8898f3527efMD53123456789/124492017-10-26 22:00:54.843oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452017-10-27T01:00:54LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.en.fl_str_mv Characterization and biotechnological application of recombinant xylanases from Aspergillus nidulans
title Characterization and biotechnological application of recombinant xylanases from Aspergillus nidulans
spellingShingle Characterization and biotechnological application of recombinant xylanases from Aspergillus nidulans
Maitan-Alfenas, Gabriela P.
Xylanase
Aspergillus nidulans
Pichia pastoris
Saccharification
Sugarcane bagasse
title_short Characterization and biotechnological application of recombinant xylanases from Aspergillus nidulans
title_full Characterization and biotechnological application of recombinant xylanases from Aspergillus nidulans
title_fullStr Characterization and biotechnological application of recombinant xylanases from Aspergillus nidulans
title_full_unstemmed Characterization and biotechnological application of recombinant xylanases from Aspergillus nidulans
title_sort Characterization and biotechnological application of recombinant xylanases from Aspergillus nidulans
author Maitan-Alfenas, Gabriela P.
author_facet Maitan-Alfenas, Gabriela P.
Oliveira, Mariana B.
Nagem, Ronaldo A.P.
Vries, Ronald P. de
Guimarães, Valéria M.
author_role author
author2 Oliveira, Mariana B.
Nagem, Ronaldo A.P.
Vries, Ronald P. de
Guimarães, Valéria M.
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Maitan-Alfenas, Gabriela P.
Oliveira, Mariana B.
Nagem, Ronaldo A.P.
Vries, Ronald P. de
Guimarães, Valéria M.
dc.subject.pt-BR.fl_str_mv Xylanase
Aspergillus nidulans
Pichia pastoris
Saccharification
Sugarcane bagasse
topic Xylanase
Aspergillus nidulans
Pichia pastoris
Saccharification
Sugarcane bagasse
description Two xylanases from Aspergillus nidulans, XlnB and XlnC, were expressed in Pichia pastoris, purified and characterized. XlnB and XlnC achieved maximal activities at 60 °C and pH 7.5 and at 50 °C and pH 6.0, respectively. XlnB showed to be very thermostable by maintaining 50% of its original activity after 49 h incubated at 50 °C. XlnB had its highest activity against wheat arabinoxylan while XlnC had the best activity against beechwood xylan. Both enzymes were completely inhibited by SDS and HgCl2. Xylotriose at 1 mg/ml also totally inibited XlnB activity. TLC analysis showed that the main product of beechwood xylan hydrolysis by XlnB and XlnC was xylotetraose. An additive effect was shown between XlnB and XlnC and the xylanases of two tested commercial cocktails. Sugarcane bagasse saccharification results showed that these two commercial enzymatic cocktails were able to release more glucose and xylose after supplementation with XlnB and XlnC.
publishDate 2016
dc.date.issued.fl_str_mv 2016-05-25
dc.date.accessioned.fl_str_mv 2017-10-26T13:44:02Z
dc.date.available.fl_str_mv 2017-10-26T13:44:02Z
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.ijbiomac.2016.05.065
http://www.locus.ufv.br/handle/123456789/12449
dc.identifier.issn.none.fl_str_mv 0141-8130
identifier_str_mv 0141-8130
url http://dx.doi.org/10.1016/j.ijbiomac.2016.05.065
http://www.locus.ufv.br/handle/123456789/12449
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartofseries.pt-BR.fl_str_mv V. 91, p.60–67, May 2015
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv International Journal of Biological Macromolecules
publisher.none.fl_str_mv International Journal of Biological Macromolecules
dc.source.none.fl_str_mv reponame:LOCUS Repositório Institucional da UFV
instname:Universidade Federal de Viçosa (UFV)
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