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http://hdl.handle.net/10261/155877
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Mtibaà, Rim | es_ES |
dc.contributor.author | Eugenio, Laura I. de | es_ES |
dc.contributor.author | Ghariani, Bouthaina | es_ES |
dc.contributor.author | Louati, Ibtihel | es_ES |
dc.contributor.author | Belbahri, Lassaad | es_ES |
dc.contributor.author | Nasri, M. | es_ES |
dc.contributor.author | Mechichi, Tahar | es_ES |
dc.date.accessioned | 2017-09-29T11:06:20Z | - |
dc.date.available | 2017-09-29T11:06:20Z | - |
dc.date.issued | 2017-09-18 | - |
dc.identifier.citation | 3 Biotech 7:329 (2017) | es_ES |
dc.identifier.issn | 2190-572X | - |
dc.identifier.uri | http://hdl.handle.net/10261/155877 | - |
dc.description | 13 p.-6 fig.-3 tab. | es_ES |
dc.description.abstract | A novel fungal laccase produced by the ascomycete Chaetomium sp. isolated from arid soil was purified and characterized and its ability to remove dyes was determined. Extracellular laccase was purified 15-fold from the crude culture to homogeneity with an overall yield of 50% using ultrafiltration and anion-exchange chromatography. The purified enzyme was found to be a monomeric protein with a molecular mass of 68 kDa, estimated by SDS-PAGE, and with an isoelectric point of 5.5. The optimal temperature and pH value for laccase activity toward 2,6-DMP were 60 °C and 3.0, respectively. It was stable at temperatures below 50 °C and at alkaline conditions. Kinetic study showed that this laccase showed higher affinity on ABTS than on 2,6-DMP. Its activity was enhanced by the presence of several metal ions such as Mg2+, Ca2+ and Zn2+, while it was strongly inhibited by Fe2+, Ag+ and Hg2+. The novel laccase also showed high, remarkable sodium chloride tolerance. Its ability to decolorize different dyes, with or without HBT (1-hydroxy-benzotriazole), as redox mediator, suggests that this protein may be useful for different industrial applications and/or bioremediation processes. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Springer Nature | es_ES |
dc.relation.isversionof | Publisher's version | es_ES |
dc.rights | openAccess | es_ES |
dc.subject | Chaetomium | es_ES |
dc.subject | Screening | es_ES |
dc.subject | Fungi | es_ES |
dc.subject | Laccase | es_ES |
dc.subject | Oxidoreductase | es_ES |
dc.title | A halotolerant laccase from Chaetomium strain isolated from desert soil and its ability for dye decolourization | es_ES |
dc.type | artículo | es_ES |
dc.identifier.doi | 10.1007/s13205-017-0973-5 | - |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | http://dx.doi.org/10.1007/s13205-017-0973-5 | es_ES |
dc.identifier.e-issn | 2190-5738 | - |
dc.relation.csic | Sí | es_ES |
oprm.item.hasRevision | no ko 0 false | * |
dc.identifier.pmid | 28955626 | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.grantfulltext | open | - |
item.openairetype | artículo | - |
item.fulltext | With Fulltext | - |
item.languageiso639-1 | en | - |
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3 Biotech_de Eugenio L. 2017.pdf | Artículo principal | 602,83 kB | Adobe PDF | Visualizar/Abrir |
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