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

Bibliographic Details
Main Author: Silva, Carla J. S. M.
Publication Date: 2006
Other Authors: Zhang, Qinghua, Shen, J., Paulo, Artur Cavaco
Format: Article
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: https://hdl.handle.net/1822/12947
Summary: 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/pdfhttps://hdl.handle.net/1822/12947eng0141-022910.1016/j.enzmictec.2005.11.016http://www.sciencedirect.com/science/article/pii/S0141022905005004info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2025-04-12T04:01:03Zoai:repositorium.sdum.uminho.pt:1822/12947Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T14:48:34.067259Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
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 https://hdl.handle.net/1822/12947
url https://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
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instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
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reponame_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
collection Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
repository.name.fl_str_mv Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
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