Influence of mechanical agitation on cutinases and protease activity towards polyamide substrates

Detalhes bibliográficos
Autor(a) principal: Silva, Carla Manuela Pereira Marinho da
Data de Publicação: 2007
Outros Autores: Araújo, Rita, Casal, Margarida, Gübitz, Georg M., Paulo, Artur Cavaco
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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spelling 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)
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