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dc.contributor.authorCota, Junio-
dc.contributor.authorOliveira, Leandro C.-
dc.contributor.authorDamásio, André R.L.-
dc.contributor.authorCitadini, Ana P.-
dc.contributor.authorHoffmam, Zaira B.-
dc.contributor.authorAlvarez, Thabata M.-
dc.contributor.authorCodima, Carla A.-
dc.contributor.authorLeite, Vitor Barbanti Pereira-
dc.contributor.authorPastore, Glaucia-
dc.contributor.authorDe Oliveira-Neto, Mario-
dc.contributor.authorMurakami, Mario T.-
dc.contributor.authorRuller, Roberto-
dc.contributor.authorSquina, Fabio M.-
dc.identifier.citationBiochimica et Biophysica Acta - Proteins and Proteomics, v. 1834, n. 8, p. 1492-1500, 2013.-
dc.description.abstractMultifunctional enzyme engineering can improve enzyme cocktails for emerging biofuel technology. Molecular dynamics through structure-based models (SB) is an effective tool for assessing the tridimensional arrangement of chimeric enzymes as well as for inferring the functional practicability before experimental validation. This study describes the computational design of a bifunctional xylanase-lichenase chimera (XylLich) using the xynA and bglS genes from Bacillus subtilis. In silico analysis of the average solvent accessible surface area (SAS) and the root mean square fluctuation (RMSF) predicted a fully functional chimera, with minor fluctuations and variations along the polypeptide chains. Afterwards, the chimeric enzyme was built by fusing the xynA and bglS genes. XylLich was evaluated through small-angle X-ray scattering (SAXS) experiments, resulting in scattering curves with a very accurate fit to the theoretical protein model. The chimera preserved the biochemical characteristics of the parental enzymes, with the exception of a slight variation in the temperature of operation and the catalytic efficiency (k cat/Km). The absence of substantial shifts in the catalytic mode of operation was also verified. Furthermore, the production of chimeric enzymes could be more profitable than producing a single enzyme separately, based on comparing the recombinant protein production yield and the hydrolytic activity achieved for XylLich with that of the parental enzymes. © 2013 Elsevier B.V. All rights reserved.en
dc.subjectComputational characterization-
dc.subjectExperimental validation-
dc.subjectMolecular dynamics-
dc.subjectMultifunctional enzyme-
dc.subjectSmall-angle X-ray scattering-
dc.subjectendo 1,4 beta xylanase-
dc.subjecthybrid protein-
dc.subjectBacillus subtilis-
dc.subjectchemical structure-
dc.subjectcomputer simulation-
dc.subjectmolecular dynamics-
dc.subjectsmall angle scattering-
dc.subjectComputer Simulation-
dc.subjectEndo-1,4-beta Xylanases-
dc.subjectGlycoside Hydrolases-
dc.subjectModels, Molecular-
dc.subjectMolecular Dynamics Simulation-
dc.subjectRecombinant Fusion Proteins-
dc.subjectScattering, Small Angle-
dc.titleAssembling a xylanase-lichenase chimera through all-atom molecular dynamics simulationsen
dc.contributor.institutionLaboratório Nacional de Ciência e Tecnologia do Bioetanol - CTBE/CNPEM-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)-
dc.contributor.institutionLaboratório Nacional de Biociências - LNBio/CNPEM-
dc.description.affiliationLaboratório Nacional de Ciência e Tecnologia do Bioetanol - CTBE/CNPEM, Caixa Postal 6170, 13083-970 Campinas, São Paulo-
dc.description.affiliationDepartamento de Física IBILCE Universidade Estadual Paulista - UNESP, São José do Rio Preto, SP-
dc.description.affiliationFaculdade de Engenharia de Alimentos Universidade Estadual de Campinas, Campinas, SP-
dc.description.affiliationDepartamento de Física e Biofísica Instituto de Biociências UNESP, Botucatu, São Paulo-
dc.description.affiliationLaboratório Nacional de Biociências - LNBio/CNPEM, Campinas, SP-
dc.description.affiliationUnespDepartamento de Física IBILCE Universidade Estadual Paulista - UNESP, São José do Rio Preto, SP-
dc.description.affiliationUnespDepartamento de Física e Biofísica Instituto de Biociências UNESP, Botucatu, São Paulo-
dc.rights.accessRightsAcesso aberto-
dc.relation.ispartofBiochimica et Biophysica Acta: Proteins and Proteomics-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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