SAXS Studies of the Endoglucanase Cel12A from Gloeophyllum trabeum Show Its Monomeric Structure and Reveal the Influence of Temperature on the Structural Stability of the Enzyme

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dc.contributor.authorMiotto, Lis S.
dc.contributor.authorReis, Caio V. dos
dc.contributor.authorNeto, Mario de Oliveira [UNESP]
dc.contributor.authorPolikarpov, Igor
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2015-03-18T15:56:21Z
dc.date.available2015-03-18T15:56:21Z
dc.date.issued2014-07-01
dc.description.abstractEndoglucanases are key enzymes applied to the conversion of biomass aiming for second generation biofuel production. In the present study we obtained the small angle X-ray scattering (SAXS) structure of the G. trabeum endo-1,4-beta-glucanase Cel12A and investigated the influence of an important parameter, temperature, on both secondary and tertiary structure of the enzyme and its activity. The CD analysis for GtCel12A revealed that changes in the CD spectra starts at 55 degrees C and the T-m calculated from the experimental CD sigmoid curve using the Boltzmann function was 60.2 +/- 0.6 degrees C. SAXS data showed that GtCel12A forms monomers in solution and has an elongated form with a maximum diameter of 60 +/- 5 angstrom and a gyration radius of 19.4 +/- 0.1 angstrom as calculated from the distance distribution function. Kratky analysis revealed that 60 degrees C is the critical temperature above which we observed clear indications of denaturation. Our results showed the influence of temperature on the stability and activity of enzymes and revealed novel structural features of GtCel12A.en
dc.description.affiliationUniv Sao Paulo, Inst Fis Sao Carlos, Grp Biotecnol Mol, BR-13566590 Sao Carlos, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Inst Biociencias Botucatu, Dept Fis & Biofis, BR-18618970 Botucatu, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Biociencias Botucatu, Dept Fis & Biofis, BR-18618970 Botucatu, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdFAPESP: 09/08233-9
dc.format.extent5202-5211
dc.identifierhttp://dx.doi.org/10.3390/ma7075202
dc.identifier.citationMaterials. Basel: Mdpi Ag, v. 7, n. 7, p. 5202-5211, 2014.
dc.identifier.doi10.3390/ma7075202
dc.identifier.fileWOS000339989700015.pdf
dc.identifier.issn1996-1944
dc.identifier.lattes8213371495151651
dc.identifier.urihttp://hdl.handle.net/11449/117516
dc.identifier.wosWOS:000339989700015
dc.language.isoeng
dc.publisherMdpi Ag
dc.relation.ispartofMaterials
dc.relation.ispartofjcr2.467
dc.relation.ispartofsjr0,732
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectendoglucanaseen
dc.subjectGloeophyllum trabeumen
dc.subjectbiophysicsen
dc.subjectcircular dichroismen
dc.subjectsmall angle X-ray scattering (SAXS)en
dc.subjectKratky analysisen
dc.titleSAXS Studies of the Endoglucanase Cel12A from Gloeophyllum trabeum Show Its Monomeric Structure and Reveal the Influence of Temperature on the Structural Stability of the Enzymeen
dc.typeArtigo
dcterms.rightsHolderMdpi Ag
unesp.author.lattes8213371495151651
unesp.author.orcid0000-0001-9496-4174[4]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Botucatupt

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Artigos - Física e Biofísica - IBB