Treatment of wool fibres with subtilisin and subtilisin-PEG
Autor(a) principal: | |
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Data de Publicação: | 2005 |
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/1822/2655 |
Resumo: | In this work the diffusion of serine proteases into wool fabrics and yarns was studied. The proteases used were free subtilisin and subtilisin-PEG (the same enzyme that was covalently cross linked to polyethylene glycol). It is shown that the adsorption and diffusion is facilitated by the pre-treatment performed, being the alkaline surfactant washing and bleaching the most effective in what concerns enzyme adsorption. Furthermore, this study suggests that the diffusion of proteases into wool is dependent on the size of the protease. The free enzyme penetrates into wool fibre cortex while the modified bigger enzyme is retained only at the surface, in the cuticle layer. Also, proteins without proteolytic activity do not adsorb considerably on wool due to its hydrophobic nature, therefore the diffusion is facilitated by hydrolytic action. These results have important practical implications for the establishment of enzymatic wool finishing processes, since they allow for control of the enzyme hydrolysis, which was the major drawback of this environmental friendly option to the conventional chlorine treatments. |
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Treatment of wool fibres with subtilisin and subtilisin-PEGSerine proteasesProtein adsorptionWool fibreClean technologyCross linkingwool fibres clean technologyScience & TechnologyIn this work the diffusion of serine proteases into wool fabrics and yarns was studied. The proteases used were free subtilisin and subtilisin-PEG (the same enzyme that was covalently cross linked to polyethylene glycol). It is shown that the adsorption and diffusion is facilitated by the pre-treatment performed, being the alkaline surfactant washing and bleaching the most effective in what concerns enzyme adsorption. Furthermore, this study suggests that the diffusion of proteases into wool is dependent on the size of the protease. The free enzyme penetrates into wool fibre cortex while the modified bigger enzyme is retained only at the surface, in the cuticle layer. Also, proteins without proteolytic activity do not adsorb considerably on wool due to its hydrophobic nature, therefore the diffusion is facilitated by hydrolytic action. These results have important practical implications for the establishment of enzymatic wool finishing processes, since they allow for control of the enzyme hydrolysis, which was the major drawback of this environmental friendly option to the conventional chlorine treatments.ElsevierUniversidade do MinhoSilva, Carla J. S. M.Prabaharan, M.Gübitz, Georg M.Paulo, Artur Cavaco20052005-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/2655eng"Enzyme and microbial technology". ISSN 0141-0229. 36:7 (2005) 917-922.0141-022910.1016/j.enzmictec.2005.01.017info: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:RCAAP2023-07-21T11:55:51Zoai:repositorium.sdum.uminho.pt:1822/2655Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:45:24.368297Repositório 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 |
Treatment of wool fibres with subtilisin and subtilisin-PEG |
title |
Treatment of wool fibres with subtilisin and subtilisin-PEG |
spellingShingle |
Treatment of wool fibres with subtilisin and subtilisin-PEG Silva, Carla J. S. M. Serine proteases Protein adsorption Wool fibre Clean technology Cross linking wool fibres clean technology Science & Technology |
title_short |
Treatment of wool fibres with subtilisin and subtilisin-PEG |
title_full |
Treatment of wool fibres with subtilisin and subtilisin-PEG |
title_fullStr |
Treatment of wool fibres with subtilisin and subtilisin-PEG |
title_full_unstemmed |
Treatment of wool fibres with subtilisin and subtilisin-PEG |
title_sort |
Treatment of wool fibres with subtilisin and subtilisin-PEG |
author |
Silva, Carla J. S. M. |
author_facet |
Silva, Carla J. S. M. Prabaharan, M. Gübitz, Georg M. Paulo, Artur Cavaco |
author_role |
author |
author2 |
Prabaharan, M. Gübitz, Georg M. Paulo, Artur Cavaco |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Silva, Carla J. S. M. Prabaharan, M. Gübitz, Georg M. Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Serine proteases Protein adsorption Wool fibre Clean technology Cross linking wool fibres clean technology Science & Technology |
topic |
Serine proteases Protein adsorption Wool fibre Clean technology Cross linking wool fibres clean technology Science & Technology |
description |
In this work the diffusion of serine proteases into wool fabrics and yarns was studied. The proteases used were free subtilisin and subtilisin-PEG (the same enzyme that was covalently cross linked to polyethylene glycol). It is shown that the adsorption and diffusion is facilitated by the pre-treatment performed, being the alkaline surfactant washing and bleaching the most effective in what concerns enzyme adsorption. Furthermore, this study suggests that the diffusion of proteases into wool is dependent on the size of the protease. The free enzyme penetrates into wool fibre cortex while the modified bigger enzyme is retained only at the surface, in the cuticle layer. Also, proteins without proteolytic activity do not adsorb considerably on wool due to its hydrophobic nature, therefore the diffusion is facilitated by hydrolytic action. These results have important practical implications for the establishment of enzymatic wool finishing processes, since they allow for control of the enzyme hydrolysis, which was the major drawback of this environmental friendly option to the conventional chlorine treatments. |
publishDate |
2005 |
dc.date.none.fl_str_mv |
2005 2005-01-01T00:00:00Z |
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/1822/2655 |
url |
http://hdl.handle.net/1822/2655 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
"Enzyme and microbial technology". ISSN 0141-0229. 36:7 (2005) 917-922. 0141-0229 10.1016/j.enzmictec.2005.01.017 |
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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1799132206774353920 |