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dc.contributor.authorHoffmam, Zaira B.
dc.contributor.authorOliveira, Leandro C. [UNESP]
dc.contributor.authorCota, Junio
dc.contributor.authorAlvarez, Thabata M.
dc.contributor.authorDiogo, Jos A.
dc.contributor.authorNeto, Mario de Oliveira [UNESP]
dc.contributor.authorCitadini, Ana Paula S.
dc.contributor.authorLeite, Vitor Barbanti Pereira [UNESP]
dc.contributor.authorSquina, Fabio M.
dc.contributor.authorMurakami, Mario T.
dc.contributor.authorRuller, Roberto
dc.date.accessioned2014-12-03T13:11:09Z
dc.date.available2014-12-03T13:11:09Z
dc.date.issued2013-11-01
dc.identifierhttp://dx.doi.org/10.1007/s12033-013-9677-1
dc.identifier.citationMolecular Biotechnology. Totowa: Humana Press Inc, v. 55, n. 3, p. 260-267, 2013.
dc.identifier.issn1073-6085
dc.identifier.urihttp://hdl.handle.net/11449/112907
dc.description.abstractalpha-l-Arabinofuranosidases (alpha-l-Abfases, EC 3.2.1.55) display a broad specificity against distinct glycosyl moieties in branched hemicellulose and recent studies have demonstrated their synergistic use with cellulases and xylanases for biotechnological processes involving plant biomass degradation. In this study, we examined the structural organization of the arabinofuranosidase (GH51 family) from the mesophilic Bacillus subtilis (AbfA) and its implications on function and stability. The recombinant AbfA showed to be active over a broad temperature range with the maximum activity between 35 and 50 A degrees C, which is desirable for industrial applications. Functional studies demonstrated that AbfA preferentially cleaves debranched or linear arabinan and is an exo-acting enzyme producing arabinose from arabinoheptaose. The enzyme has a canonical circular dichroism spectrum of alpha/beta proteins and exhibits a hexameric quaternary structure in solution, as expected for GH51 members. Thermal denaturation experiments indicated a melting temperature of 53.5 A degrees C, which is in agreement with the temperature-activity curves. The mechanisms associated with the unfolding process were investigated through molecular dynamics simulations evidencing an important contribution of the quaternary arrangement in the stabilization of the beta-sandwich accessory domain and other regions involved in the formation of the catalytic interface of hexameric Abfases belonging to GH51 family.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent260-267
dc.language.isoeng
dc.publisherHumana Press Inc
dc.relation.ispartofMolecular Biotechnology
dc.sourceWeb of Science
dc.subjectArabinofuranosidaseen
dc.subjectGlycosyl hydrolase family 51en
dc.subjectBacillus subtilisen
dc.subjectQuaternary structureen
dc.titleCharacterization of a Hexameric Exo-Acting GH51 alpha-l-Arabinofuranosidase from the Mesophilic Bacillus subtilisen
dc.typeArtigo
dcterms.rightsHolderHumana Press Inc
dc.contributor.institutionCtr Nacl Pesquisa Energia & Mat
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionLab Nacl Biociencias LNBio CNPEM
dc.description.affiliationCtr Nacl Pesquisa Energia & Mat, Lab Nacl Ciencia & Tecnol Bioetanol, BR-13083970 Campinas, SP, Brazil
dc.description.affiliationUniv Estadual Campinas UNICAMP, Campinas, SP, Brazil
dc.description.affiliationUniv Estadual Paulista IBILCE UNESP, Inst Biociencias Letras & Ciencias Exatas, Dept Fis, Sao Jose Do Rio Preto, SP, Brazil
dc.description.affiliationUNESP Botucatu, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP, Brazil
dc.description.affiliationLab Nacl Biociencias LNBio CNPEM, Campinas, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista IBILCE UNESP, Inst Biociencias Letras & Ciencias Exatas, Dept Fis, Sao Jose Do Rio Preto, SP, Brazil
dc.description.affiliationUnespUNESP Botucatu, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP, Brazil
dc.identifier.doi10.1007/s12033-013-9677-1
dc.identifier.wosWOS:000328208600007
dc.rights.accessRightsAcesso restrito
dc.description.sponsorshipIdFAPESP: 08/58037-9
dc.description.sponsorshipIdFAPESP: 10/51890-8
dc.description.sponsorshipIdFAPESP: 11/14200-6
dc.description.sponsorshipIdFAPESP: 11/13242-7
dc.description.sponsorshipIdFAPESP: 10/11499-1
dc.description.sponsorshipIdCNPq: 133394/2011-5
dc.description.sponsorshipIdCNPq: 475022/2011-4
dc.description.sponsorshipIdCNPq: 310177/2011-1
dc.description.sponsorshipIdCNPq: 2011/17658-3
dc.description.sponsorshipIdCNPq: 140420/2009-6
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Botucatupt
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt
dc.identifier.lattes0500034174785796
dc.identifier.lattes8213371495151651
unesp.author.lattes0500034174785796
unesp.advisor.lattes8213371495151651
unesp.author.orcid0000-0001-7501-5176[11]
unesp.author.orcid0000-0002-0405-8010[10]
unesp.author.orcid0000-0002-5087-9493[11]
unesp.author.orcid0000-0002-6932-6792[2]
dc.relation.ispartofjcr1.815
dc.relation.ispartofsjr0,643
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