Recycling of cellulases in lignocellulosic hydrolysates using alkaline elution
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , , |
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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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 |
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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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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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 |
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1799132913907793920 |