Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of wool
Autor(a) principal: | |
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Data de Publicação: | 2006 |
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/1822/12947 |
Resumo: | A commercial protease, Esperase, was covalently linked to Eudragit S-100, a reversible soluble–insoluble polymer by carbodiimide coupling. When compared to the native enzyme, the immobilized form presented a lower specific activity towards high molecular weight substrates but a higher thermal stability at all temperatures tested. The optimum pH of the immobilized protease was shifted towards the alkaline side by about one pH unit while there was no change in optimum temperature between the free and immobilized protease. The immobilized protease exhibited a good storage stability and re-usability. Enzymatic treatment of wool using proteases has been investigated for wool shrink-resist finishing. It was found that using the immobilized protease in the enzymatic treatment of wool there was a reduction of weight and fibre tensile strength loss because the proteolytic attack is only limited to the cuticle surfaces of wool fibres. This novel approach is a promising alternative for wool shrink-resist finishing to replace the conventional chlorine treatments. This environmentally friendly bioprocess needs to be further characterized to a complete understanding and optimization. |
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Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of woolSerine proteasesWool bio-finishingStabilityImmobilizationEudragitScience & TechnologyA commercial protease, Esperase, was covalently linked to Eudragit S-100, a reversible soluble–insoluble polymer by carbodiimide coupling. When compared to the native enzyme, the immobilized form presented a lower specific activity towards high molecular weight substrates but a higher thermal stability at all temperatures tested. The optimum pH of the immobilized protease was shifted towards the alkaline side by about one pH unit while there was no change in optimum temperature between the free and immobilized protease. The immobilized protease exhibited a good storage stability and re-usability. Enzymatic treatment of wool using proteases has been investigated for wool shrink-resist finishing. It was found that using the immobilized protease in the enzymatic treatment of wool there was a reduction of weight and fibre tensile strength loss because the proteolytic attack is only limited to the cuticle surfaces of wool fibres. This novel approach is a promising alternative for wool shrink-resist finishing to replace the conventional chlorine treatments. This environmentally friendly bioprocess needs to be further characterized to a complete understanding and optimization.ElsevierUniversidade do MinhoSilva, Carla J. S. M.Zhang, QinghuaShen, J.Paulo, Artur Cavaco2006-08-022006-08-02T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/12947eng0141-022910.1016/j.enzmictec.2005.11.016http://www.sciencedirect.com/science/article/pii/S0141022905005004info: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:RCAAP2023-07-21T11:58:46Zoai:repositorium.sdum.uminho.pt:1822/12947Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:48:32.840825Repositório 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 |
Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of wool |
title |
Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of wool |
spellingShingle |
Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of wool Silva, Carla J. S. M. Serine proteases Wool bio-finishing Stability Immobilization Eudragit Science & Technology |
title_short |
Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of wool |
title_full |
Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of wool |
title_fullStr |
Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of wool |
title_full_unstemmed |
Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of wool |
title_sort |
Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of wool |
author |
Silva, Carla J. S. M. |
author_facet |
Silva, Carla J. S. M. Zhang, Qinghua Shen, J. Paulo, Artur Cavaco |
author_role |
author |
author2 |
Zhang, Qinghua Shen, J. 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. Zhang, Qinghua Shen, J. Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Serine proteases Wool bio-finishing Stability Immobilization Eudragit Science & Technology |
topic |
Serine proteases Wool bio-finishing Stability Immobilization Eudragit Science & Technology |
description |
A commercial protease, Esperase, was covalently linked to Eudragit S-100, a reversible soluble–insoluble polymer by carbodiimide coupling. When compared to the native enzyme, the immobilized form presented a lower specific activity towards high molecular weight substrates but a higher thermal stability at all temperatures tested. The optimum pH of the immobilized protease was shifted towards the alkaline side by about one pH unit while there was no change in optimum temperature between the free and immobilized protease. The immobilized protease exhibited a good storage stability and re-usability. Enzymatic treatment of wool using proteases has been investigated for wool shrink-resist finishing. It was found that using the immobilized protease in the enzymatic treatment of wool there was a reduction of weight and fibre tensile strength loss because the proteolytic attack is only limited to the cuticle surfaces of wool fibres. This novel approach is a promising alternative for wool shrink-resist finishing to replace the conventional chlorine treatments. This environmentally friendly bioprocess needs to be further characterized to a complete understanding and optimization. |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006-08-02 2006-08-02T00:00:00Z |
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/1822/12947 |
url |
http://hdl.handle.net/1822/12947 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0141-0229 10.1016/j.enzmictec.2005.11.016 http://www.sciencedirect.com/science/article/pii/S0141022905005004 |
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 |
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RCAAP |
institution |
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) |
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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1799132247509434368 |