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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/55171
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dc.creatorRita Terezinha de Oliveira Carneiropt_BR
dc.creatorMaíza Alves Lopespt_BR
dc.creatorMarília Lôrdelo Cardoso Silvapt_BR
dc.creatorVerônica da Silva Santospt_BR
dc.creatorVolnei Brito de Souzapt_BR
dc.creatorAurizângela Oliveira de Sousapt_BR
dc.creatorCarlos Priminho Pirovanipt_BR
dc.creatorMaria Gabriela Bello Koblitzpt_BR
dc.creatorRaquel Guimarães Benevidespt_BR
dc.creatorAristóteles Góes Netopt_BR
dc.date.accessioned2023-06-20T19:27:43Z-
dc.date.available2023-06-20T19:27:43Z-
dc.date.issued2017-
dc.citation.volume27pt_BR
dc.citation.issue1pt_BR
dc.citation.spage179pt_BR
dc.citation.epage188pt_BR
dc.identifier.doihttp://dx.doi.org/10.4014/jmb.1606.06055pt_BR
dc.identifier.issn1738-8872pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/55171-
dc.description.resumoWhite-rot basidiomycetes are the organisms that decompose lignin most efficiently, and Trametes villosa is a promising species for ligninolytic enzyme production. There are several publications on T. villosa applications for lignin degradation regarding the expression and secretion of laccase and manganese peroxidase (MnP) but no reports on the identification and characterization of lignin peroxidase (LiP), a relevant enzyme for the efficient breakdown of lignin. The object of this study was to identify and partially characterize, for the first time, gDNA, mRNA, and the corresponding lignin peroxidase (TvLiP) protein from T. villosa strain CCMB561 from the Brazilian semiarid region. The presence of ligninolytic enzymes produced by this strain grown in inducer media was qualitatively and quantitatively analyzed by spectrophotometry, qPCR, and dye fading using Remazol Brilliant Blue R. The spectrophotometric analysis showed that LiP activity was higher than that of MnP. The greatest LiP expression as measured by qPCR occurred on the 7th day, and the ABSA medium (agar, sugarcane bagasse, and ammonium sulfate) was the best that favored LiP expression. The amplification of the TvLiP gene median region covering approximately 50% of the T. versicolor LPGIV gene (87% identity); the presence of Trp199, Leu115, Asp193, Trp199, and Ala203 in the translated amplicon of the T. villosa mRNA; and the close phylogenetic relationship between TvLiP and T. versicolor LiP all indicate that the target enzyme is a lignin peroxidase. Therefore, T. villosa CCMB561 has great potential for use as a LiP, MnP, and Lac producer for industrial applications.pt_BR
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
dc.description.sponsorshipOutra Agênciapt_BR
dc.format.mimetypepdfpt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentICB - DEPARTAMENTO DE MICROBIOLOGIApt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofJournal of microbiology and biotechnologypt_BR
dc.rightsAcesso Abertopt_BR
dc.subjectLigninpt_BR
dc.subjectLigninolytic enzymespt_BR
dc.subjectWhite-rot basidiomycetespt_BR
dc.subject.otherLigninapt_BR
dc.subject.otherEnzimaspt_BR
dc.subject.otherBasidiomycota - enzimologiapt_BR
dc.titleTrametes villosa Lignin Peroxidase (TvLiP): genetic and molecular characterizationpt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://www.jmb.or.kr/journal/view.html?doi=10.4014/jmb.1606.06055pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-7568-6487pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-5963-314Xpt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-9669-7890pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-6176-4069pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-5558-570Xpt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-5410-6973pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-7692-6243pt_BR
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