Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents

Detalhes bibliográficos
Autor(a) principal: Costa, Silgia
Data de Publicação: 2001
Outros Autores: Tzanov, Tzanko, Paar, Andreas, Gudelj, Marinka, Gübitz, Georg M., 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/1822/2636
Resumo: A catalase preparation from a newly isolated Bacillus sp. was covalently immobilized on silanized alumina using glutaraldehyde as crosslinking agent. The effect of the coupling time of the enzyme-support reaction was determined in terms of protein recovery and immobilization yield and a certain balance point was found after which the activity recovery decreased. The activity profile of the immobilized catalase at high pH and temperature was investigated. The immobilized enzyme showed higher stabilities (214 h at pH 11, 30°C) at alkaline pH than the free enzyme (10 h at pH 11, 30°C). The immobilized catalase was inhibited by anionic stabilizers or surfactants added to the hydrogen peroxide substrate solution.
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spelling Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluentsCatalaseCovalent immobilizationThermo- and alkaline stabilityHydrogen peroxideScience & TechnologyA catalase preparation from a newly isolated Bacillus sp. was covalently immobilized on silanized alumina using glutaraldehyde as crosslinking agent. The effect of the coupling time of the enzyme-support reaction was determined in terms of protein recovery and immobilization yield and a certain balance point was found after which the activity recovery decreased. The activity profile of the immobilized catalase at high pH and temperature was investigated. The immobilized enzyme showed higher stabilities (214 h at pH 11, 30°C) at alkaline pH than the free enzyme (10 h at pH 11, 30°C). The immobilized catalase was inhibited by anionic stabilizers or surfactants added to the hydrogen peroxide substrate solution.A catalase preparation from a newly isolated Bacillus sp. was covalently immobilized on silanized alumina using glutaraldehyde as crosslinking agent. The effect of the coupling time of the enzyme-support reaction was determined in terms of protein recovery and immobilization yield and a certain balance point was found after which the activity recovery decreased. The activity profile of the immobilized catalase at high pH and temperature was investigated. The immobilized enzyme showed higher stabilities (214 h at pH 11, 30°C) at alkaline pH than the free enzyme (10 h at pH 11, 30°C). The immobilized catalase was inhibited by anionic stabilizers or surfactants added to the hydrogen peroxide substrate solution.ElsevierUniversidade do MinhoCosta, SilgiaTzanov, TzankoPaar, AndreasGudelj, MarinkaGübitz, Georg M.Paulo, Artur Cavaco20012001-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/2636eng"Enzyme and Microbial Technology". ISSN 0141-0229. 28:9-10 (June 2001) 815–819.0141-022910.1016/S0141-0229(01)00335-0info: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:RCAAP2023-07-21T11:59:51Zoai:repositorium.sdum.uminho.pt:1822/2636Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:49:40.075766Repositório 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 catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents
title Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents
spellingShingle Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents
Costa, Silgia
Catalase
Covalent immobilization
Thermo- and alkaline stability
Hydrogen peroxide
Science & Technology
title_short Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents
title_full Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents
title_fullStr Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents
title_full_unstemmed Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents
title_sort Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents
author Costa, Silgia
author_facet Costa, Silgia
Tzanov, Tzanko
Paar, Andreas
Gudelj, Marinka
Gübitz, Georg M.
Paulo, Artur Cavaco
author_role author
author2 Tzanov, Tzanko
Paar, Andreas
Gudelj, Marinka
Gübitz, Georg M.
Paulo, Artur Cavaco
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Costa, Silgia
Tzanov, Tzanko
Paar, Andreas
Gudelj, Marinka
Gübitz, Georg M.
Paulo, Artur Cavaco
dc.subject.por.fl_str_mv Catalase
Covalent immobilization
Thermo- and alkaline stability
Hydrogen peroxide
Science & Technology
topic Catalase
Covalent immobilization
Thermo- and alkaline stability
Hydrogen peroxide
Science & Technology
description A catalase preparation from a newly isolated Bacillus sp. was covalently immobilized on silanized alumina using glutaraldehyde as crosslinking agent. The effect of the coupling time of the enzyme-support reaction was determined in terms of protein recovery and immobilization yield and a certain balance point was found after which the activity recovery decreased. The activity profile of the immobilized catalase at high pH and temperature was investigated. The immobilized enzyme showed higher stabilities (214 h at pH 11, 30°C) at alkaline pH than the free enzyme (10 h at pH 11, 30°C). The immobilized catalase was inhibited by anionic stabilizers or surfactants added to the hydrogen peroxide substrate solution.
publishDate 2001
dc.date.none.fl_str_mv 2001
2001-01-01T00:00:00Z
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/1822/2636
url http://hdl.handle.net/1822/2636
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv "Enzyme and Microbial Technology". ISSN 0141-0229. 28:9-10 (June 2001) 815–819.
0141-0229
10.1016/S0141-0229(01)00335-0
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
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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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