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resumen

Resumen
Cyclodextrin glycosyltransferases (CGTases) are important enzymes in the biotechnology field because they catalyze starch conversion into cyclodextrins and linear oligosaccharides, which are used in food, pharmaceutical and cosmetic industries. The CGTases are classified according to their product specificity in α-, β-, α/β- and γ-CGTases. As molecular markers are the preferred tool for bacterial identification, we employed six molecular markers (16S [ver mas...]
dc.contributor.authorCaminata Landriel, Soledad
dc.contributor.authorCastillo, Julieta D. L. M.
dc.contributor.authorTaboga, Oscar Alberto
dc.contributor.authorFerrarotti, Susana Alicia
dc.contributor.authorGottlieb, Alexandra Marina
dc.contributor.authorCosta, Hernán
dc.date.accessioned2020-01-14T13:30:43Z
dc.date.available2020-01-14T13:30:43Z
dc.date.issued2019-10
dc.identifier.issn1678-2690
dc.identifier.otherhttp://dx.doi.org/10.1590/0001-3765201920180568
dc.identifier.urihttp://hdl.handle.net/20.500.12123/6671
dc.identifier.urihttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652019000500620&lng=en&nrm=iso&tlng=en
dc.description.abstractCyclodextrin glycosyltransferases (CGTases) are important enzymes in the biotechnology field because they catalyze starch conversion into cyclodextrins and linear oligosaccharides, which are used in food, pharmaceutical and cosmetic industries. The CGTases are classified according to their product specificity in α-, β-, α/β- and γ-CGTases. As molecular markers are the preferred tool for bacterial identification, we employed six molecular markers (16S rRNA, dnaK, gyrB, recA, rpoB and tufA) to test the identification of a CGTase-producing bacterial strain (DF 9R) in a phylogenetic context. In addition, we assessed the phylogenetic relationship of CGTases along bacterial evolution. The results obtained here allowed us to identify the strain DF 9R as Paenibacillus barengoltzii, and to unveil a complex origin for CGTase types during archaeal and bacterial evolution. We postulate that the α-CGTase activity represents the ancestral type, and that the γ-activity may have derived from β-CGTases.eng
dc.formatapplication/pdfeng
dc.language.isoeng
dc.publisherAcademia Brasileira de Ciênciases_AR
dc.rightsinfo:eu-repo/semantics/openAccesseng
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.sourceAnais da Academia Brasileira de Ciências 91 (3) : e20180568. (Octubre 2019)por
dc.subjectPaenibacilluses_AR
dc.subjectGlycosidaseseng
dc.subjectGlicosidasases_AR
dc.subjectGenetic Markerseng
dc.subjectMarcadores Genéticoses_AR
dc.subjectEnzyme Activityeng
dc.subjectActividad Enzimáticaes_AR
dc.subjectPhylogenyeng
dc.subjectFilogeniaes_AR
dc.titleMolecular identification of a cyclodextrin glycosyltransferase-producing microorganism and phylogenetic assessment of enzymatic activitieseng
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articleeng
dc.typeinfo:eu-repo/semantics/publishedVersioneng
dc.rights.licenseCreative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.description.origenInstituto de Biotecnologíaes_AR
dc.description.filFil: Caminata Landriel, Soledad. Universidad Nacional de Luján. Departamento de Ciencias Básicas. Laboratorio de Química Biológica; Argentinaes_AR
dc.description.filFil: Castillo, Julieta D. L. M. Universidad Nacional de Luján. Departamento de Ciencias Básicas. Laboratorio de Química Biológica; Argentinaes_AR
dc.description.filFil: Taboga, Oscar Alberto. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Ferrarotti, Susana Alicia. Universidad Nacional de Luján. Departamento de Ciencias Básicas. Laboratorio de Química Biológica; Argentina.es_AR
dc.description.filFil: Gottlieb, Alexandra Marina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Ecología, Genética y Evolución; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Costa, Hernán. Universidad Nacional de Luján. Departamento de Ciencias Básicas.Laboratorio de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.subtypecientifico


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