Recycling of cellulases in lignocellulosic hydrolysates using alkaline elution

Detalhes bibliográficos
Autor(a) principal: Rodrigues, Ana Cristina Costa
Data de Publicação: 2012
Outros Autores: Leitão, Alexandre F., Moreira, Susana Margarida Gomes, Felby, Claus, Gama, F. M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/22400
Resumo: The recovery of cellulases from lignin, lignocellulosic hydrolysates and cellulose by alkaline washes at pH 9 and 10 was examined. The effect of the pH on the structural stability of purified Cel7A was analyzed by circular dichroism. Purified Cel7A showed conformational changes at pH 9 and 10 that were reversible at pH 4.8. Temperature influenced the enzymatic hydrolysis of wheat straw and may be critical for the efficiency of cellulase recycling from wheat straw hydrolysates. Operation at moderate temperatures (37 °C) resulted in a rate of saccharification 19% higher than that obtained at 50° C, improving cellulase recycling by 49%. Over 60% of the enzyme activity on the synthetic substrate 4-methylumbelliferyl-β-d-cellobioside (MUC) may be recovered by using a simple alkaline wash. This is thus a promising strategy for enzyme recycling that is simple to implement at industrial scale, economical and effective.
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spelling Recycling of cellulases in lignocellulosic hydrolysates using alkaline elutionWheat strawLigninCelluloseCellulase adsorption/desorptionEnzyme recoveryScience & TechnologyThe recovery of cellulases from lignin, lignocellulosic hydrolysates and cellulose by alkaline washes at pH 9 and 10 was examined. The effect of the pH on the structural stability of purified Cel7A was analyzed by circular dichroism. Purified Cel7A showed conformational changes at pH 9 and 10 that were reversible at pH 4.8. Temperature influenced the enzymatic hydrolysis of wheat straw and may be critical for the efficiency of cellulase recycling from wheat straw hydrolysates. Operation at moderate temperatures (37 °C) resulted in a rate of saccharification 19% higher than that obtained at 50° C, improving cellulase recycling by 49%. Over 60% of the enzyme activity on the synthetic substrate 4-methylumbelliferyl-β-d-cellobioside (MUC) may be recovered by using a simple alkaline wash. This is thus a promising strategy for enzyme recycling that is simple to implement at industrial scale, economical and effective.The authors acknowledge funding through FP7 KACELLE (Kalundborg Cellulosic Ethanol) project for supporting his work. We also thank Dr. Mai Ostergaard Haven for critical reviewing of the manuscript and Dr. Jane Lindedam for supplying the lignin.ElsevierUniversidade do MinhoRodrigues, Ana Cristina CostaLeitão, Alexandre F.Moreira, Susana Margarida GomesFelby, ClausGama, F. M.20122012-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/22400eng0960-852410.1016/j.biortech.2012.01.14022357293http://ac.els-cdn.com/S0960852412001836/1-s2.0-S0960852412001836-main.pdf?_tid=e4d8b430-59c5-11e2-84b5-00000aab0f01&acdnat=1357671905_2f0cd0335d8db4c50d35882f56978a9dinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:40:57Zoai:repositorium.sdum.uminho.pt:1822/22400Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:37:50.528922Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Recycling of cellulases in lignocellulosic hydrolysates using alkaline elution
title Recycling of cellulases in lignocellulosic hydrolysates using alkaline elution
spellingShingle Recycling of cellulases in lignocellulosic hydrolysates using alkaline elution
Rodrigues, Ana Cristina Costa
Wheat straw
Lignin
Cellulose
Cellulase adsorption/desorption
Enzyme recovery
Science & Technology
title_short Recycling of cellulases in lignocellulosic hydrolysates using alkaline elution
title_full Recycling of cellulases in lignocellulosic hydrolysates using alkaline elution
title_fullStr Recycling of cellulases in lignocellulosic hydrolysates using alkaline elution
title_full_unstemmed Recycling of cellulases in lignocellulosic hydrolysates using alkaline elution
title_sort Recycling of cellulases in lignocellulosic hydrolysates using alkaline elution
author Rodrigues, Ana Cristina Costa
author_facet Rodrigues, Ana Cristina Costa
Leitão, Alexandre F.
Moreira, Susana Margarida Gomes
Felby, Claus
Gama, F. M.
author_role author
author2 Leitão, Alexandre F.
Moreira, Susana Margarida Gomes
Felby, Claus
Gama, F. M.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Rodrigues, Ana Cristina Costa
Leitão, Alexandre F.
Moreira, Susana Margarida Gomes
Felby, Claus
Gama, F. M.
dc.subject.por.fl_str_mv Wheat straw
Lignin
Cellulose
Cellulase adsorption/desorption
Enzyme recovery
Science & Technology
topic Wheat straw
Lignin
Cellulose
Cellulase adsorption/desorption
Enzyme recovery
Science & Technology
description The recovery of cellulases from lignin, lignocellulosic hydrolysates and cellulose by alkaline washes at pH 9 and 10 was examined. The effect of the pH on the structural stability of purified Cel7A was analyzed by circular dichroism. Purified Cel7A showed conformational changes at pH 9 and 10 that were reversible at pH 4.8. Temperature influenced the enzymatic hydrolysis of wheat straw and may be critical for the efficiency of cellulase recycling from wheat straw hydrolysates. Operation at moderate temperatures (37 °C) resulted in a rate of saccharification 19% higher than that obtained at 50° C, improving cellulase recycling by 49%. Over 60% of the enzyme activity on the synthetic substrate 4-methylumbelliferyl-β-d-cellobioside (MUC) may be recovered by using a simple alkaline wash. This is thus a promising strategy for enzyme recycling that is simple to implement at industrial scale, economical and effective.
publishDate 2012
dc.date.none.fl_str_mv 2012
2012-01-01T00:00:00Z
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://hdl.handle.net/1822/22400
url http://hdl.handle.net/1822/22400
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0960-8524
10.1016/j.biortech.2012.01.140
22357293
http://ac.els-cdn.com/S0960852412001836/1-s2.0-S0960852412001836-main.pdf?_tid=e4d8b430-59c5-11e2-84b5-00000aab0f01&acdnat=1357671905_2f0cd0335d8db4c50d35882f56978a9d
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 Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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