Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysis

Detalhes bibliográficos
Autor(a) principal: Almeida, Maíra Nicolau de
Data de Publicação: 2011
Outros Autores: Guimarães, Valéria Monteze, Bischoff, Kenneth M., Falkoski, Daniel Luciano, Pereira, Olinto Liparini, Gonçalves, Dayelle S. P. O., Rezende, Sebastião Tavares de
Tipo de documento: Artigo
Idioma: por
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: https://doi-org.ez35.periodicos.capes.gov.br/10.1007/s12010-011-9278-z
http://www.locus.ufv.br/handle/123456789/18150
Resumo: The aim of this work was to have cellulase activity and hemicellulase activity screenings of endophyte Acremonium species (Acremonium zeae EA0802 and Acremonium sp. EA0810). Both fungi were cultivated in submerged culture (SC) containing L -arabinose, D -xylose, oat spelt xylan, sugarcane bagasse, or corn straw as carbon source. In solid-state fermentation, it was tested as carbon source sugarcane bagasse or corn straw. The highest FPase, endoglucanase, and xylanase activities were produced by Acremonium sp. EA0810 cultivated in SC containing sugarcane bagasse as a carbon source. The highest β-glucosidase activity was produced by Acremonium sp. EA0810 cultivated in SC using D -xylose as carbon source. A. zeae EA0802 has highest α-arabinofuranosidase and α-galactosidase activities in SC using xylan as a carbon source. FPase, endoglucanase, β-glucosidase, and xylanase from Acremonium sp. EA0810 has optimum pH and temperatures of 6.0, 55 °C; 5.0, 70 °C; 4.5, 60 °C; and 6.5, 50 °C, respectively. α-Arabinofuranosidase and α-galactosidase from A. zeae EA0802 has optimum pH and temperatures of 5.0, 60 °C and 4.5, 45 °C, respectively. It was analyzed the application of Acremonium sp. EA0810 to hydrolyze sugarcane bagasse, and it was achieved 63% of conversion into reducing sugar and 42% of conversion into glucose.
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spelling Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysisCellulaseHemicellulaseAcremoniumEndophyteEthanolAgroindustrial residueThe aim of this work was to have cellulase activity and hemicellulase activity screenings of endophyte Acremonium species (Acremonium zeae EA0802 and Acremonium sp. EA0810). Both fungi were cultivated in submerged culture (SC) containing L -arabinose, D -xylose, oat spelt xylan, sugarcane bagasse, or corn straw as carbon source. In solid-state fermentation, it was tested as carbon source sugarcane bagasse or corn straw. The highest FPase, endoglucanase, and xylanase activities were produced by Acremonium sp. EA0810 cultivated in SC containing sugarcane bagasse as a carbon source. The highest β-glucosidase activity was produced by Acremonium sp. EA0810 cultivated in SC using D -xylose as carbon source. A. zeae EA0802 has highest α-arabinofuranosidase and α-galactosidase activities in SC using xylan as a carbon source. FPase, endoglucanase, β-glucosidase, and xylanase from Acremonium sp. EA0810 has optimum pH and temperatures of 6.0, 55 °C; 5.0, 70 °C; 4.5, 60 °C; and 6.5, 50 °C, respectively. α-Arabinofuranosidase and α-galactosidase from A. zeae EA0802 has optimum pH and temperatures of 5.0, 60 °C and 4.5, 45 °C, respectively. It was analyzed the application of Acremonium sp. EA0810 to hydrolyze sugarcane bagasse, and it was achieved 63% of conversion into reducing sugar and 42% of conversion into glucose.Appl Biochem Biotechnol2018-03-09T11:10:06Z2018-03-09T11:10:06Z2011-05-02info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlepdfapplication/pdf15590291https://doi-org.ez35.periodicos.capes.gov.br/10.1007/s12010-011-9278-zhttp://www.locus.ufv.br/handle/123456789/18150porVolume 165, Issue 2, pp 594–610, September 2011Springer International Publishing AG. Part of Springer Natureinfo:eu-repo/semantics/openAccessAlmeida, Maíra Nicolau deGuimarães, Valéria MontezeBischoff, Kenneth M.Falkoski, Daniel LucianoPereira, Olinto LipariniGonçalves, Dayelle S. P. O.Rezende, Sebastião Tavares dereponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFV2024-07-12T06:48:38Zoai:locus.ufv.br:123456789/18150Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452024-07-12T06:48:38LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.none.fl_str_mv Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysis
title Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysis
spellingShingle Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysis
Almeida, Maíra Nicolau de
Cellulase
Hemicellulase
Acremonium
Endophyte
Ethanol
Agroindustrial residue
title_short Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysis
title_full Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysis
title_fullStr Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysis
title_full_unstemmed Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysis
title_sort Cellulases and hemicellulases from endophytic acremonium species and its application on sugarcane bagasse hydrolysis
author Almeida, Maíra Nicolau de
author_facet Almeida, Maíra Nicolau de
Guimarães, Valéria Monteze
Bischoff, Kenneth M.
Falkoski, Daniel Luciano
Pereira, Olinto Liparini
Gonçalves, Dayelle S. P. O.
Rezende, Sebastião Tavares de
author_role author
author2 Guimarães, Valéria Monteze
Bischoff, Kenneth M.
Falkoski, Daniel Luciano
Pereira, Olinto Liparini
Gonçalves, Dayelle S. P. O.
Rezende, Sebastião Tavares de
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Almeida, Maíra Nicolau de
Guimarães, Valéria Monteze
Bischoff, Kenneth M.
Falkoski, Daniel Luciano
Pereira, Olinto Liparini
Gonçalves, Dayelle S. P. O.
Rezende, Sebastião Tavares de
dc.subject.por.fl_str_mv Cellulase
Hemicellulase
Acremonium
Endophyte
Ethanol
Agroindustrial residue
topic Cellulase
Hemicellulase
Acremonium
Endophyte
Ethanol
Agroindustrial residue
description The aim of this work was to have cellulase activity and hemicellulase activity screenings of endophyte Acremonium species (Acremonium zeae EA0802 and Acremonium sp. EA0810). Both fungi were cultivated in submerged culture (SC) containing L -arabinose, D -xylose, oat spelt xylan, sugarcane bagasse, or corn straw as carbon source. In solid-state fermentation, it was tested as carbon source sugarcane bagasse or corn straw. The highest FPase, endoglucanase, and xylanase activities were produced by Acremonium sp. EA0810 cultivated in SC containing sugarcane bagasse as a carbon source. The highest β-glucosidase activity was produced by Acremonium sp. EA0810 cultivated in SC using D -xylose as carbon source. A. zeae EA0802 has highest α-arabinofuranosidase and α-galactosidase activities in SC using xylan as a carbon source. FPase, endoglucanase, β-glucosidase, and xylanase from Acremonium sp. EA0810 has optimum pH and temperatures of 6.0, 55 °C; 5.0, 70 °C; 4.5, 60 °C; and 6.5, 50 °C, respectively. α-Arabinofuranosidase and α-galactosidase from A. zeae EA0802 has optimum pH and temperatures of 5.0, 60 °C and 4.5, 45 °C, respectively. It was analyzed the application of Acremonium sp. EA0810 to hydrolyze sugarcane bagasse, and it was achieved 63% of conversion into reducing sugar and 42% of conversion into glucose.
publishDate 2011
dc.date.none.fl_str_mv 2011-05-02
2018-03-09T11:10:06Z
2018-03-09T11:10:06Z
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 15590291
https://doi-org.ez35.periodicos.capes.gov.br/10.1007/s12010-011-9278-z
http://www.locus.ufv.br/handle/123456789/18150
identifier_str_mv 15590291
url https://doi-org.ez35.periodicos.capes.gov.br/10.1007/s12010-011-9278-z
http://www.locus.ufv.br/handle/123456789/18150
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv Volume 165, Issue 2, pp 594–610, September 2011
dc.rights.driver.fl_str_mv Springer International Publishing AG. Part of Springer Nature
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Springer International Publishing AG. Part of Springer Nature
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv pdf
application/pdf
dc.publisher.none.fl_str_mv Appl Biochem Biotechnol
publisher.none.fl_str_mv Appl Biochem Biotechnol
dc.source.none.fl_str_mv reponame:LOCUS Repositório Institucional da UFV
instname:Universidade Federal de Viçosa (UFV)
instacron:UFV
instname_str Universidade Federal de Viçosa (UFV)
instacron_str UFV
institution UFV
reponame_str LOCUS Repositório Institucional da UFV
collection LOCUS Repositório Institucional da UFV
repository.name.fl_str_mv LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)
repository.mail.fl_str_mv fabiojreis@ufv.br
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