Lignin degradation by a novel thermophilic and alkaline yellow laccase from Chitinophaga sp.

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorInstitute for Research in Bioenergy (IPBEN)-
Autor(es): dc.creatorBuzzo, Bárbara Bonfá-
Autor(es): dc.creatorLima, Natália Sarmanho Monteiro-
Autor(es): dc.creatorPereira, Pâmela Aparecida Maldaner-
Autor(es): dc.creatorGomes-Pepe, Elisângela Soares-
Autor(es): dc.creatorSartini, Camila Cesario Fernandes-
Autor(es): dc.creatorde Macedo Lemos, Eliana Gertrudes-
Data de aceite: dc.date.accessioned2025-08-21T17:40:44Z-
Data de disponibilização: dc.date.available2025-08-21T17:40:44Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2024-06-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1128/spectrum.04013-23-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/309527-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/309527-
Descrição: dc.descriptionLaccases (EC 1.10.3.2) are oxidoreductases that belong to the multicopper oxidase subfamily and are classifiedas yellow/white or blue according to their absorption spectrum. Yellow laccases are more useful for industrial processes since they oxidize nonphenolic compounds in the absence of a redox mediator and stand out for being more stable and functional under extreme conditions. This study aimed to characterize a new laccase that was predicted to be present in the genome of Chitinophaga sp. CB10 - Lac_CB10. Lac_CB10, with a molecular mass of 100.06 kDa, was purifiedand characterized via biochemical assays using guaiacol as a substrate. The enzyme demonstrated extremophilic characteristics, exhibiting relative activity under alkaline conditions (CAPS bufferpH 10.5) and thermophilic conditions (80-90°C), as well as maintaining its activity above 50% for 5 h at 80°C and 90°C. Furthermore, Lac_CB10 presented a spectral profiletypical of yellow laccases, exhibiting only one absorbance peak at 300 nm (at the T2/T3 site) and no peak at 600 nm (at the T1 site). When lignin was degraded using copper as an inducer, 52.27% of the material was degraded within 32 h. These results highlight the potential of this enzyme, which is a novel yellow laccase with thermophilic and alkaline activity and the ability to act on lignin. This enzyme could be a valuable addition to the biorefineryprocess. In addition, this approach has high potential for industrial application and in the bioremediation of contaminated environments since these processes often occur at extreme temperatures and pH values.-
Descrição: dc.descriptionDepartment of Agricultural Livestock and Environmental Biotechnology São Paulo State University Júlio de Mesquita Filho, São Paulo-
Descrição: dc.descriptionMolecular Biology Laboratory Institute for Research in Bioenergy (IPBEN), Jaboticabal-
Descrição: dc.descriptionAgricultural Microbiology Graduate Program UNESP, São Paulo-
Descrição: dc.descriptionDepartment of Agricultural Livestock and Environmental Biotechnology São Paulo State University Júlio de Mesquita Filho, São Paulo-
Descrição: dc.descriptionAgricultural Microbiology Graduate Program UNESP, São Paulo-
Idioma: dc.languageen-
Relação: dc.relationMicrobiology Spectrum-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectextremophile-
Palavras-chave: dc.subjectlignin-
Palavras-chave: dc.subjectyellow laccase-
Título: dc.titleLignin degradation by a novel thermophilic and alkaline yellow laccase from Chitinophaga sp.-
Tipo de arquivo: dc.typelivro digital-
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