Laccase immobilization on enzymatically functionalized polyamide 6,6 fibres
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Publication Date: | 2007 |
Other Authors: | , , , |
Format: | Article |
Language: | eng |
Source: | Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
Download full: | https://hdl.handle.net/1822/13847 |
Summary: | Polyamide matrices, such as membranes, gels and non-wovens, have been applied as supports for enzyme immobilization, although in literature the enzyme immobilization on woven nylon matrices is rarely reported. In this work, a protocol for a Trametes hirsuta laccase immobilization using woven polyamide 6,6 (nylon) was developed. A 24 full factorial design was used to study the influence of pH, spacer (1,6-hexanediamine), enzyme and crosslinker concentration on the efficiency of immobilization. The factors enzyme dosage and spacer seem to have played a critical role in the immobilization of laccase onto nylon support. Under optimized working conditions (29 U mL−1 of laccase, 10% of glutaraldehyde, pH = 5.5, with the presence of the spacer), the half-life time attained was about 78 h (18% higher than that of free enzyme), the protein retention was 30% and the immobilization yield was 2%. The immobilized laccase has potential for application in the continuous decolourization of textile effluents, where it can be applied into a membrane reactor. |
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Laccase immobilization on enzymatically functionalized polyamide 6,6 fibresPolyamideNylonImmobilizationCrosslinkingGlutaraldehydeLaccaseScience & TechnologyPolyamide matrices, such as membranes, gels and non-wovens, have been applied as supports for enzyme immobilization, although in literature the enzyme immobilization on woven nylon matrices is rarely reported. In this work, a protocol for a Trametes hirsuta laccase immobilization using woven polyamide 6,6 (nylon) was developed. A 24 full factorial design was used to study the influence of pH, spacer (1,6-hexanediamine), enzyme and crosslinker concentration on the efficiency of immobilization. The factors enzyme dosage and spacer seem to have played a critical role in the immobilization of laccase onto nylon support. Under optimized working conditions (29 U mL−1 of laccase, 10% of glutaraldehyde, pH = 5.5, with the presence of the spacer), the half-life time attained was about 78 h (18% higher than that of free enzyme), the protein retention was 30% and the immobilization yield was 2%. The immobilized laccase has potential for application in the continuous decolourization of textile effluents, where it can be applied into a membrane reactor.ElsevierUniversidade do MinhoSilva, Carla Manuela Pereira MarinhoSilva, Carla J. S. M.Zille, AndreaGübitz, Georg M.Paulo, Artur Cavaco2007-112007-11-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/1822/13847eng0141-022910.1016/j.enzmictec.2007.07.010http://www.sciencedirect.com/science/article/pii/S0141022907002463info: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:RCAAP2025-04-12T04:20:35Zoai:repositorium.sdum.uminho.pt:1822/13847Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T15:03:29.274220Repositórios 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 |
Laccase immobilization on enzymatically functionalized polyamide 6,6 fibres |
title |
Laccase immobilization on enzymatically functionalized polyamide 6,6 fibres |
spellingShingle |
Laccase immobilization on enzymatically functionalized polyamide 6,6 fibres Silva, Carla Manuela Pereira Marinho Polyamide Nylon Immobilization Crosslinking Glutaraldehyde Laccase Science & Technology |
title_short |
Laccase immobilization on enzymatically functionalized polyamide 6,6 fibres |
title_full |
Laccase immobilization on enzymatically functionalized polyamide 6,6 fibres |
title_fullStr |
Laccase immobilization on enzymatically functionalized polyamide 6,6 fibres |
title_full_unstemmed |
Laccase immobilization on enzymatically functionalized polyamide 6,6 fibres |
title_sort |
Laccase immobilization on enzymatically functionalized polyamide 6,6 fibres |
author |
Silva, Carla Manuela Pereira Marinho |
author_facet |
Silva, Carla Manuela Pereira Marinho Silva, Carla J. S. M. Zille, Andrea Gübitz, Georg M. Paulo, Artur Cavaco |
author_role |
author |
author2 |
Silva, Carla J. S. M. Zille, Andrea 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 Silva, Carla J. S. M. Zille, Andrea Gübitz, Georg M. Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Polyamide Nylon Immobilization Crosslinking Glutaraldehyde Laccase Science & Technology |
topic |
Polyamide Nylon Immobilization Crosslinking Glutaraldehyde Laccase Science & Technology |
description |
Polyamide matrices, such as membranes, gels and non-wovens, have been applied as supports for enzyme immobilization, although in literature the enzyme immobilization on woven nylon matrices is rarely reported. In this work, a protocol for a Trametes hirsuta laccase immobilization using woven polyamide 6,6 (nylon) was developed. A 24 full factorial design was used to study the influence of pH, spacer (1,6-hexanediamine), enzyme and crosslinker concentration on the efficiency of immobilization. The factors enzyme dosage and spacer seem to have played a critical role in the immobilization of laccase onto nylon support. Under optimized working conditions (29 U mL−1 of laccase, 10% of glutaraldehyde, pH = 5.5, with the presence of the spacer), the half-life time attained was about 78 h (18% higher than that of free enzyme), the protein retention was 30% and the immobilization yield was 2%. The immobilized laccase has potential for application in the continuous decolourization of textile effluents, where it can be applied into a membrane reactor. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-11 2007-11-01T00:00:00Z |
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 |
https://hdl.handle.net/1822/13847 |
url |
https://hdl.handle.net/1822/13847 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0141-0229 10.1016/j.enzmictec.2007.07.010 http://www.sciencedirect.com/science/article/pii/S0141022907002463 |
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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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