Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/355534
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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.contributor.authorunicampMercaldi, Gustavo Fernando-
dc.typeArtigopt_BR
dc.titleEst16, a new esterase isolated from a metagenomic library of a microbial consortium specializing in diesel oil degradationpt_BR
dc.contributor.authorPereira, Mariana Rangel-
dc.contributor.authorMercaldi, Gustavo Fernando-
dc.contributor.authorMaester, Thaís Carvalho-
dc.contributor.authorBalan, Andrea-
dc.contributor.authorMacedo Lemos, Eliana Gertrudes de-
dc.subjectMetagenômicapt_BR
dc.subjectEsterasespt_BR
dc.subject.otherlanguageMetagenomicspt_BR
dc.subject.otherlanguageEsterasespt_BR
dc.description.abstractLipolytic enzymes have attracted attention from a global market because they show enormous biotechnological potential for applications such as detergent production, leather processing, cosmetics production, and use in perfumes and biodiesel. Due to the intense demand for biocatalysts, a metagenomic approach provides methods of identifying new enzymes. In this study, an esterase designated as Est16 was selected from 4224 clones of a fosmid metagenomic library, revealing an 87% amino acid identity with an esterase/lipase (accession number ADM63076.1) from an uncultured bacterium. Phylogenetic studies showed that the enzyme belongs to family V of bacterial lipolytic enzymes and has sequence and structural similarities with an aryl-esterase from Pseudomonas fluorescens and a patented Anti-Kazlauskas lipase (patent number US20050153404). The protein was expressed and purified as a highly soluble, thermally stable enzyme that showed a preference for basic pH. Est16 exhibited activity toward a wide range of substrates and the highest catalytic efficiency against p-nitrophenyl butyrate and p-nitrophenyl valerate. Est16 also showed tolerance to the presence of organic solvents, detergents and metals. Based on molecular modeling, we showed that the large alpha-beta domain is conserved in the patented enzymes but not the substrate pocket. Here, it was demonstrated that a metagenomic approach is suitable for discovering the lipolytic enzyme diversity and that Est16 has the biotechnological potential for use in industrial processespt_BR
dc.relation.ispartofPLoS onept_BR
dc.publisher.citySan Francisco, CApt_BR
dc.publisher.countryEstados Unidospt_BR
dc.publisherPublic Library of Sciencept_BR
dc.date.issued2015-
dc.date.monthofcirculationJulypt_BR
dc.language.isoengpt_BR
dc.description.volume10pt_BR
dc.description.issuenumber7pt_BR
dc.rightsAbertopt_BR
dc.sourceWOSpt_BR
dc.identifier.eissn1932-6203pt_BR
dc.identifier.doi10.1371/journal.pone.0133723pt_BR
dc.identifier.urlhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0133723pt_BR
dc.description.sponsorshipFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESPpt_BR
dc.description.sponsordocumentnumber2011/ 09136-7pt_BR
dc.date.available2021-02-10T18:34:44Z-
dc.date.accessioned2021-02-10T18:34:44Z-
dc.description.provenanceSubmitted by Mariana Aparecida Azevedo (mary1@unicamp.br) on 2021-02-10T18:34:44Z No. of bitstreams: 0en
dc.description.provenanceMade available in DSpace on 2021-02-10T18:34:44Z (GMT). No. of bitstreams: 0 Previous issue date: 2015en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/355534-
dc.contributor.departmentsem informaçãopt_BR
dc.contributor.unidadeInstituto de Biologiapt_BR
dc.subject.keywordLipasespt_BR
dc.subject.keywordEnzyme structurept_BR
dc.subject.keywordDNA cloningpt_BR
dc.subject.keywordPhylogenetic analysispt_BR
dc.subject.keywordPseudomonas fluorescenspt_BR
dc.subject.keywordEnzymespt_BR
dc.identifier.source000358594300026pt_BR
dc.creator.orcidsem informaçãopt_BR
dc.type.formArtigo de pesquisapt_BR
dc.identifier.articleide0133723pt_BR
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