Influence of mechanical agitation on cutinases and protease activity towards polyamide substrates
Autor(a) principal: | |
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Data de Publicação: | 2007 |
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/1822/13141 |
Resumo: | Two polyamide 6,6 substrates with different constructions, namely a model substrate and a fabric, were hydrolyzed using native cutinase and L182A cutinase mutant (from Fusarium solani pisi) and a protease (subtilisin from Bacillus sp.). The catalytic efficiency of these enzymes, measured in terms of hydrolysis products release, was measured for both substrates and the protease released five times more amines to the bath treatment. The L182A cutinase mutant showed higher activity when compared with the native enzyme. All enzymes have shown activity additive effects with higher levels of mechanical agitation for polyamide fabrics. The results achieved are of paramount importance on the design of a process of enzymatic functionalization of polyamide. |
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7160 |
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Influence of mechanical agitation on cutinases and protease activity towards polyamide substratesPolyamideCutinaseProteaseHydrolysisScience & TechnologyTwo polyamide 6,6 substrates with different constructions, namely a model substrate and a fabric, were hydrolyzed using native cutinase and L182A cutinase mutant (from Fusarium solani pisi) and a protease (subtilisin from Bacillus sp.). The catalytic efficiency of these enzymes, measured in terms of hydrolysis products release, was measured for both substrates and the protease released five times more amines to the bath treatment. The L182A cutinase mutant showed higher activity when compared with the native enzyme. All enzymes have shown activity additive effects with higher levels of mechanical agitation for polyamide fabrics. The results achieved are of paramount importance on the design of a process of enzymatic functionalization of polyamide.European Community - Biosyntex Project, G5RD-CT-2000-30110Fundação para a Ciência e a Tecnologia (FCT) - SFRH/BD/22490/2006ElsevierUniversidade do MinhoSilva, Carla Manuela Pereira Marinho daAraújo, RitaCasal, MargaridaGübitz, Georg M.Paulo, Artur Cavaco2007-062007-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/13141eng0141-022910.1016/j.enzmictec.2006.09.001http://www.sciencedirect.com/info: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:RCAAP2023-07-21T12:29:38Zoai:repositorium.sdum.uminho.pt:1822/13141Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:24:39.387427Repositório 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 |
Influence of mechanical agitation on cutinases and protease activity towards polyamide substrates |
title |
Influence of mechanical agitation on cutinases and protease activity towards polyamide substrates |
spellingShingle |
Influence of mechanical agitation on cutinases and protease activity towards polyamide substrates Silva, Carla Manuela Pereira Marinho da Polyamide Cutinase Protease Hydrolysis Science & Technology |
title_short |
Influence of mechanical agitation on cutinases and protease activity towards polyamide substrates |
title_full |
Influence of mechanical agitation on cutinases and protease activity towards polyamide substrates |
title_fullStr |
Influence of mechanical agitation on cutinases and protease activity towards polyamide substrates |
title_full_unstemmed |
Influence of mechanical agitation on cutinases and protease activity towards polyamide substrates |
title_sort |
Influence of mechanical agitation on cutinases and protease activity towards polyamide substrates |
author |
Silva, Carla Manuela Pereira Marinho da |
author_facet |
Silva, Carla Manuela Pereira Marinho da Araújo, Rita Casal, Margarida Gübitz, Georg M. Paulo, Artur Cavaco |
author_role |
author |
author2 |
Araújo, Rita Casal, Margarida Gübitz, Georg M. Paulo, Artur Cavaco |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Silva, Carla Manuela Pereira Marinho da Araújo, Rita Casal, Margarida Gübitz, Georg M. Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Polyamide Cutinase Protease Hydrolysis Science & Technology |
topic |
Polyamide Cutinase Protease Hydrolysis Science & Technology |
description |
Two polyamide 6,6 substrates with different constructions, namely a model substrate and a fabric, were hydrolyzed using native cutinase and L182A cutinase mutant (from Fusarium solani pisi) and a protease (subtilisin from Bacillus sp.). The catalytic efficiency of these enzymes, measured in terms of hydrolysis products release, was measured for both substrates and the protease released five times more amines to the bath treatment. The L182A cutinase mutant showed higher activity when compared with the native enzyme. All enzymes have shown activity additive effects with higher levels of mechanical agitation for polyamide fabrics. The results achieved are of paramount importance on the design of a process of enzymatic functionalization of polyamide. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-06 2007-06-01T00:00:00Z |
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/1822/13141 |
url |
http://hdl.handle.net/1822/13141 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0141-0229 10.1016/j.enzmictec.2006.09.001 http://www.sciencedirect.com/ |
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 |
institution |
RCAAP |
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 |
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1799132727823302656 |