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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleSubstrate cleavage pattern, biophysical characterization and low-resolution structure of a novel hyperthermostable arabinanase from Thermotoga petrophilapt_BR
dc.contributor.authorSquina, FMpt_BR
dc.contributor.authorSantos, CRpt_BR
dc.contributor.authorRibeiro, DApt_BR
dc.contributor.authorCota, Jpt_BR
dc.contributor.authorde Oliveira, RRpt_BR
dc.contributor.authorRuller, Rpt_BR
dc.contributor.authorMort, Apt_BR
dc.contributor.authorMurakami, MTpt_BR
dc.contributor.authorPrade, RApt_BR
unicamp.author.emailfabio.squina@bioetanol.org.brpt_BR
unicamp.authorSquina, Fabio M. Ribeiro, Daniela A. Cota, Junio Ruller, Roberto CNPEM, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, Campinas, SP, Brazilpt_BR
unicamp.authorSantos, Camila R. de Oliveira, Renata R. Murakami, Mario T. CNPEM, Lab Nacl Biociencias LNBio, Campinas, SP, Brazilpt_BR
unicamp.authorCota, Junio Univ Estadual Campinas, Dept Ciencias Alimentos, BR-13081970 Campinas, SP, Brazilpt_BR
unicamp.authorMort, Andrew Oklahoma State Univ, Dept Biochem, Stillwater, OK 74078 USApt_BR
unicamp.authorPrade, Rolf A. Oklahoma State Univ, Dept Microbiol & Mol Genet, Stillwater, OK 74078 USApt_BR
dc.subjectArabinanasept_BR
dc.subjectCapillary zone electrophoresispt_BR
dc.subjectSmall angle X-ray scattering (SAXS)pt_BR
dc.subjectHyperthermostable enzymept_BR
dc.subjectArabinanpt_BR
dc.subject.wosGlycosyl Hydrolasespt_BR
dc.subject.wosCrystal-structurept_BR
dc.subject.wosArabinofuranosidasept_BR
dc.subject.wosPurificationpt_BR
dc.subject.wosDegradationpt_BR
dc.subject.wosClassificationpt_BR
dc.subject.wosExpressionpt_BR
dc.subject.wosSucrosept_BR
dc.subject.wosEnzymespt_BR
dc.subject.wosBindingpt_BR
dc.description.abstractArabinan is a plant structural polysaccharide degraded by two enzymes: alpha-L-arabinofuranosidase and endo-1,5-alpha-L-arabinanase. These enzymes are highly diversified in nature, however, little is known about their biochemical and biophysical properties. We have characterized a novel arabinanase (AbnA) isolated from Thermotoga petrophila with unique thermostable properties such as the insignificant decrease of residual activity after incubation up to 90 degrees C. We determined the AbnA mode of operation through capillary zone electrophoresis, which accumulates arabinotriose and arabinobiose as end products after hydrolysis of arabinan-containing polysaccharides. Spectroscopic analyses by Far-UV circular dichroism and intrinsic tryptophan fluorescence emission demonstrated that AbnA is folded and formed mainly by beta-sheet structural elements. In silico molecular modeling showed that the AbnA structure encompasses a five-bladed beta-propeller catalytic core juxtaposed by distorted up-and-down beta-barrel domain. The low-resolution structure determined by small angle X-ray scattering indicated that AbnA is monomeric in solution and its molecular shape is in full agreement with the model. (C) 2010 Elsevier Inc. All rights reserved.pt
dc.relation.ispartofBiochemical And Biophysical Research Communicationspt_BR
dc.relation.ispartofabbreviationBiochem. Biophys. Res. Commun.pt_BR
dc.publisher.citySan Diegopt_BR
dc.publisher.countryEUApt_BR
dc.publisherAcademic Press Inc Elsevier Sciencept_BR
dc.date.issued2010pt_BR
dc.date.monthofcirculationSEP 3pt_BR
dc.identifier.citationBiochemical And Biophysical Research Communications. Academic Press Inc Elsevier Science, v. 399, n. 4, n. 505, n. 511, 2010.pt_BR
dc.language.isoenpt_BR
dc.description.volume399pt_BR
dc.description.issuenumber4pt_BR
dc.description.firstpage505pt_BR
dc.description.lastpage511pt_BR
dc.rightsfechadopt_BR
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policypt_BR
dc.sourceWeb of Sciencept_BR
dc.identifier.issn0006-291Xpt_BR
dc.identifier.wosidWOS:000281840200008pt_BR
dc.identifier.doi10.1016/j.bbrc.2010.07.097pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipDepartment of Energy [06103-OKL, ZDJ-7-77608-01]pt_BR
dc.description.sponsorship1Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsordocumentnumberFAPESP [08/58037-9]pt
dc.description.sponsordocumentnumberCNPq [478059/2009-4]pt
dc.description.sponsordocumentnumberDepartment of Energy [06103-OKL, ZDJ-7-77608-01]pt
dc.date.available2014-11-14T10:09:04Z
dc.date.available2015-11-26T17:14:23Z-
dc.date.accessioned2014-11-14T10:09:04Z
dc.date.accessioned2015-11-26T17:14:23Z-
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dc.description.provenanceMade available in DSpace on 2015-11-26T17:14:23Z (GMT). No. of bitstreams: 2 WOS000281840200008.pdf: 609954 bytes, checksum: bc5ed9b631d430fb6dab2f3bf6cff035 (MD5) WOS000281840200008.pdf.txt: 32219 bytes, checksum: a4d93b8a3d1d42ef107c4e23ed0ed680 (MD5) Previous issue date: 2010en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/74685pt_BR
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/74685
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/74685-
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