The enhancement of the cellulolytic activity of cellobiohydrolase I and endoglucanase by the addition of cellulose binding domains derived from trichoderma reesei
Autor(a) principal: | |
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Data de Publicação: | 2003 |
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/1822/1086 |
Resumo: | The effect of isolated cellulose binding domains (CBDs) on the hydrolysis of filter paper and microcrystalline cellulose by both cellobiohydrolase I and endoglucanase, was studied. CBDs were obtained by proteolysis from cellulases using a scaled-up variant of our previous method. Experiments were performed for different enzyme/substrate ratios in both the absence and presence of CBDs. Hydrolysis of filter paper by intact cellobiohydrolase I in the presence of additional CBDs was found to have a synergistic effect, leading to an increase of the sugar production of up to 30%. The effect was less pronounced using microcrystalline cellulose, where an increase up to 16% was observed. Similar trends were found during the hydrolysis of both substrates by endoglucanase. |
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The enhancement of the cellulolytic activity of cellobiohydrolase I and endoglucanase by the addition of cellulose binding domains derived from trichoderma reeseiCellulose binding domainsSynergismCellulasesScience & TechnologyThe effect of isolated cellulose binding domains (CBDs) on the hydrolysis of filter paper and microcrystalline cellulose by both cellobiohydrolase I and endoglucanase, was studied. CBDs were obtained by proteolysis from cellulases using a scaled-up variant of our previous method. Experiments were performed for different enzyme/substrate ratios in both the absence and presence of CBDs. Hydrolysis of filter paper by intact cellobiohydrolase I in the presence of additional CBDs was found to have a synergistic effect, leading to an increase of the sugar production of up to 30%. The effect was less pronounced using microcrystalline cellulose, where an increase up to 16% was observed. Similar trends were found during the hydrolysis of both substrates by endoglucanase.Fundação para a Ciência e a Tecnologia (FCT) – PRAXIS XXI.ElsevierUniversidade do MinhoLemos, M. A.Teixeira, J. A.Domingues, M. R. M.Mota, M.Gama, F. M.20032003-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/1086eng"Enzyme and microbial technology". ISSN 0141-0229. 32:1 (2003) 35-40.0141-022910.1016/S0141-0229(02)00235-1info: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:RCAAP2023-07-21T11:59:56Zoai:repositorium.sdum.uminho.pt:1822/1086Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:49:45.172067Repositório 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 |
The enhancement of the cellulolytic activity of cellobiohydrolase I and endoglucanase by the addition of cellulose binding domains derived from trichoderma reesei |
title |
The enhancement of the cellulolytic activity of cellobiohydrolase I and endoglucanase by the addition of cellulose binding domains derived from trichoderma reesei |
spellingShingle |
The enhancement of the cellulolytic activity of cellobiohydrolase I and endoglucanase by the addition of cellulose binding domains derived from trichoderma reesei Lemos, M. A. Cellulose binding domains Synergism Cellulases Science & Technology |
title_short |
The enhancement of the cellulolytic activity of cellobiohydrolase I and endoglucanase by the addition of cellulose binding domains derived from trichoderma reesei |
title_full |
The enhancement of the cellulolytic activity of cellobiohydrolase I and endoglucanase by the addition of cellulose binding domains derived from trichoderma reesei |
title_fullStr |
The enhancement of the cellulolytic activity of cellobiohydrolase I and endoglucanase by the addition of cellulose binding domains derived from trichoderma reesei |
title_full_unstemmed |
The enhancement of the cellulolytic activity of cellobiohydrolase I and endoglucanase by the addition of cellulose binding domains derived from trichoderma reesei |
title_sort |
The enhancement of the cellulolytic activity of cellobiohydrolase I and endoglucanase by the addition of cellulose binding domains derived from trichoderma reesei |
author |
Lemos, M. A. |
author_facet |
Lemos, M. A. Teixeira, J. A. Domingues, M. R. M. Mota, M. Gama, F. M. |
author_role |
author |
author2 |
Teixeira, J. A. Domingues, M. R. M. Mota, M. Gama, F. M. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Lemos, M. A. Teixeira, J. A. Domingues, M. R. M. Mota, M. Gama, F. M. |
dc.subject.por.fl_str_mv |
Cellulose binding domains Synergism Cellulases Science & Technology |
topic |
Cellulose binding domains Synergism Cellulases Science & Technology |
description |
The effect of isolated cellulose binding domains (CBDs) on the hydrolysis of filter paper and microcrystalline cellulose by both cellobiohydrolase I and endoglucanase, was studied. CBDs were obtained by proteolysis from cellulases using a scaled-up variant of our previous method. Experiments were performed for different enzyme/substrate ratios in both the absence and presence of CBDs. Hydrolysis of filter paper by intact cellobiohydrolase I in the presence of additional CBDs was found to have a synergistic effect, leading to an increase of the sugar production of up to 30%. The effect was less pronounced using microcrystalline cellulose, where an increase up to 16% was observed. Similar trends were found during the hydrolysis of both substrates by endoglucanase. |
publishDate |
2003 |
dc.date.none.fl_str_mv |
2003 2003-01-01T00:00:00Z |
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/1822/1086 |
url |
http://hdl.handle.net/1822/1086 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
"Enzyme and microbial technology". ISSN 0141-0229. 32:1 (2003) 35-40. 0141-0229 10.1016/S0141-0229(02)00235-1 |
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 |
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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 |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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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) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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