An acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourization
Autor(a) principal: | |
---|---|
Data de Publicação: | 2003 |
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/1822/2392 |
Resumo: | The plant pathogen basidiomycete S. rolfsii secretes two laccases (SRL1 and SRL2) with molecular weights of 55 and 86 kDa, respectively. Laccase production was shown to be inducible by the addition of 2,5-xylidine to the cultural media. After treatment with a combination of chitinase and -1,3-glucanase, two different laccases were isolated from the sclerotia depending on the stage of sclerotia development. The more prominent laccase, SRL1, was purified and found to decolourize the industrially important wool azo dye Diamond Black PV 200 without the addition of redox mediators. The enzyme (pI 5.2) was active in the acidic pH range, showing an optimal activity at pH 2.4, with ABTS as substrate. The optimum temperature for activity was determined to be 62 ◦C. Enzyme stability studies revealed that SRL1 was notably stable at 18 ◦C and pH 4.5, retaining almost full activity after a week. Oxidation of tyrosine was not detectable under the reaction conditions but the enzyme did oxidize a variety of the usual laccase substrates. SRL1 was strongly inhibited by sodium azide and fluoride. Dye solutions decolourized with the immobilized laccase were successfully used for redyeing. |
id |
RCAP_62bb460066439cfaf548d0e50740b683 |
---|---|
oai_identifier_str |
oai:repositorium.sdum.uminho.pt:1822/2392 |
network_acronym_str |
RCAP |
network_name_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository_id_str |
7160 |
spelling |
An acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourizationLaccasePurificationCharacterizationSclerotium rolfsiiThe plant pathogen basidiomycete S. rolfsii secretes two laccases (SRL1 and SRL2) with molecular weights of 55 and 86 kDa, respectively. Laccase production was shown to be inducible by the addition of 2,5-xylidine to the cultural media. After treatment with a combination of chitinase and -1,3-glucanase, two different laccases were isolated from the sclerotia depending on the stage of sclerotia development. The more prominent laccase, SRL1, was purified and found to decolourize the industrially important wool azo dye Diamond Black PV 200 without the addition of redox mediators. The enzyme (pI 5.2) was active in the acidic pH range, showing an optimal activity at pH 2.4, with ABTS as substrate. The optimum temperature for activity was determined to be 62 ◦C. Enzyme stability studies revealed that SRL1 was notably stable at 18 ◦C and pH 4.5, retaining almost full activity after a week. Oxidation of tyrosine was not detectable under the reaction conditions but the enzyme did oxidize a variety of the usual laccase substrates. SRL1 was strongly inhibited by sodium azide and fluoride. Dye solutions decolourized with the immobilized laccase were successfully used for redyeing.(undefined)ElsevierUniversidade do MinhoRyan, S.Schnitzhofer, W.Tzanov, TzankoPaulo, Artur Cavaco2003-112003-11-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/2392eng"Enzyme and microbial technology". ISSN 0141-0229. 33:6 (Nov. 2003) 766–774.0141-022910.1016/S0141-0229(03)00162-5info: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:RCAAP2023-07-21T11:56:10Zoai:repositorium.sdum.uminho.pt:1822/2392Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:45:47.808445Repositório 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 |
An acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourization |
title |
An acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourization |
spellingShingle |
An acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourization Ryan, S. Laccase Purification Characterization Sclerotium rolfsii |
title_short |
An acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourization |
title_full |
An acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourization |
title_fullStr |
An acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourization |
title_full_unstemmed |
An acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourization |
title_sort |
An acid-stable laccase from sclerotium rolfsii with potential for wool dye decolourization |
author |
Ryan, S. |
author_facet |
Ryan, S. Schnitzhofer, W. Tzanov, Tzanko Paulo, Artur Cavaco |
author_role |
author |
author2 |
Schnitzhofer, W. Tzanov, Tzanko Paulo, Artur Cavaco |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Ryan, S. Schnitzhofer, W. Tzanov, Tzanko Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Laccase Purification Characterization Sclerotium rolfsii |
topic |
Laccase Purification Characterization Sclerotium rolfsii |
description |
The plant pathogen basidiomycete S. rolfsii secretes two laccases (SRL1 and SRL2) with molecular weights of 55 and 86 kDa, respectively. Laccase production was shown to be inducible by the addition of 2,5-xylidine to the cultural media. After treatment with a combination of chitinase and -1,3-glucanase, two different laccases were isolated from the sclerotia depending on the stage of sclerotia development. The more prominent laccase, SRL1, was purified and found to decolourize the industrially important wool azo dye Diamond Black PV 200 without the addition of redox mediators. The enzyme (pI 5.2) was active in the acidic pH range, showing an optimal activity at pH 2.4, with ABTS as substrate. The optimum temperature for activity was determined to be 62 ◦C. Enzyme stability studies revealed that SRL1 was notably stable at 18 ◦C and pH 4.5, retaining almost full activity after a week. Oxidation of tyrosine was not detectable under the reaction conditions but the enzyme did oxidize a variety of the usual laccase substrates. SRL1 was strongly inhibited by sodium azide and fluoride. Dye solutions decolourized with the immobilized laccase were successfully used for redyeing. |
publishDate |
2003 |
dc.date.none.fl_str_mv |
2003-11 2003-11-01T00:00:00Z |
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 |
http://hdl.handle.net/1822/2392 |
url |
http://hdl.handle.net/1822/2392 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
"Enzyme and microbial technology". ISSN 0141-0229. 33:6 (Nov. 2003) 766–774. 0141-0229 10.1016/S0141-0229(03)00162-5 |
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 |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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 |
repository.mail.fl_str_mv |
|
_version_ |
1799132211831635968 |