Immobilization of proteases with a water soluble–insoluble reversible polymer for treatment of wool

Detalhes bibliográficos
Autor(a) principal: Silva, Carla J. S. M.
Data de Publicação: 2006
Outros Autores: Zhang, Qinghua, Shen, J., 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/1822/12947
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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spelling 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
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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