Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/340370
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampCastro, Victoria Ramos Sodré de-
dc.contributor.authorunicampGonçalves, Thiago Augusto-
dc.contributor.authorunicampFranco, Telma Teixeira-
dc.contributor.authorunicampDamásio, André Ricardo de Lima-
dc.contributor.authorunicampSquina, Fabio Marcio-
dc.typeArtigopt_BR
dc.titleAn alkaline active feruloyl-CoA synthetase from soil metagenome as a potential key enzyme for lignin valorization strategiespt_BR
dc.contributor.authorSodre, Victoria-
dc.contributor.authorAraujo, Juscemacia Nascimento-
dc.contributor.authorGoncalves, Thiago Augusto-
dc.contributor.authorVilela, Nathalia-
dc.contributor.authorKimus Braz, Antonio Sergio-
dc.contributor.authorFranco, Telma Teixeira-
dc.contributor.authorNeto, Mario de Oliveira-
dc.contributor.authorde Lima Damasio, Andre Ricardo-
dc.contributor.authorGarcia, Wanius-
dc.contributor.authorSquina, Fabio Marcio-
dc.subjectLigninapt_BR
dc.subject.otherlanguageLigninpt_BR
dc.description.abstractFerulic acid (FA), a low-molecular weight aromatic compound derived from lignin, represents a high-value molecule, used for applications in the cosmetic and pharmaceutical industries. FA can be further enzymatically converted in other commercially interesting molecules, such as vanillin and bioplastics. In several organisms, these transformations often start with a common step of FA activation via CoA-thioesterification, catalyzed by feruloyl-CoA synthetases (Fcs). In this context, these enzymes are of biotechnological interest for conversion of lignin-derived FA into high value chemicals. In this study, we describe the first structural characterization of a prokaryotic Fcs, named FCS1, isolated from a lignin-degrading microbial consortium. The FCS1 optimum pH and temperature were 9 and 37 degrees C, respectively, with Km of 0.12 mM and Vmax of 36.82 U/mg. The circular dichroism spectra indicated a notable secondary structure stability at alkaline pH values and high temperatures. This secondary structure stability corroborates the activity data, which remains high until pH 9. The Small Angle X-Ray Scattering analyses resulted on the tertiary/quaternary structure and the low-resolution envelope in solution of FCS1, which was modeled as a homodimer using the hyperthermophilic nucleoside diphosphate-forming acetyl-CoA synthetase from Candidatus Korachaeum cryptofilum. This study contributes to the field of research by establishing the first biophysical and structural characterization for Fcs, and our data may be used for comparison against novel enzymes of this class that to be studied in the futurept_BR
dc.relation.ispartofPLoS onept_BR
dc.relation.ispartofabbreviationPLoS onept_BR
dc.publisher.citySan Francisco, CApt_BR
dc.publisher.countryEstados Unidospt_BR
dc.publisherPublic Library of Sciencept_BR
dc.date.issued2019-
dc.date.monthofcirculationFeb.pt_BR
dc.language.isoengpt_BR
dc.description.volume14pt_BR
dc.description.issuenumber2pt_BR
dc.rightsAbertopt_BR
dc.sourceWOSpt_BR
dc.identifier.eissn1932-6203pt_BR
dc.identifier.doi10.1371/journal.pone.0212629pt_BR
dc.identifier.urlhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0212629pt_BR
dc.description.sponsorshipCONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQpt_BR
dc.description.sponsorshipCOORDENAÇÃO DE APERFEIÇOAMENTO DE PESSOAL DE NÍVEL SUPERIOR - CAPESpt_BR
dc.description.sponsorshipFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESPpt_BR
dc.description.sponsordocumentnumber305748/2017-3; 305740/2017-2; 304816/2017-5pt_BR
dc.description.sponsordocumentnumbersem informaçãopt_BR
dc.description.sponsordocumentnumber15/50590-4; 15/50612-8; 17/17275-3; 17/22669-0; 2018/18101-1; 2017/05901-7; 17/16089-1; 2017/16976-8; 17/08166-6pt_BR
dc.date.available2020-05-07T19:16:03Z-
dc.date.accessioned2020-05-07T19:16:03Z-
dc.description.provenanceSubmitted by Cintia Oliveira de Moura (cintiaom@unicamp.br) on 2020-05-07T19:16:03Z No. of bitstreams: 0. Added 1 bitstream(s) on 2020-08-27T19:17:57Z : No. of bitstreams: 1 000459710700015.pdf: 3651789 bytes, checksum: 55251b36d27f010f5bf69fdf3c223e68 (MD5)en
dc.description.provenanceMade available in DSpace on 2020-05-07T19:16:03Z (GMT). No. of bitstreams: 0 Previous issue date: 2019en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/340370-
dc.contributor.departmentsem informaçãopt_BR
dc.contributor.departmentsem informaçãopt_BR
dc.contributor.departmentDepartamento de Engenharia de Processospt_BR
dc.contributor.departmentDepartamento de Bioquímica e Biologia Tecidualpt_BR
dc.contributor.departmentsem informaçãopt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeFaculdade de Engenharia Químicapt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.identifier.source000459710700015pt_BR
dc.creator.orcidsem informaçãopt_BR
dc.creator.orcid0000-0001-6526-905Xpt_BR
dc.creator.orcidsem informaçãopt_BR
dc.creator.orcid0000-0001-9304-3998pt_BR
dc.creator.orcidsem informaçãopt_BR
dc.type.formArtigo de pesquisapt_BR
dc.identifier.articleide0212629pt_BR
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