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dc.contributor.author Rodriguez, J.
dc.contributor.author Soria, Francisco Fernando
dc.contributor.author Geronazzo, Hugo Isidoro
dc.contributor.author Destefanis, Hugo Alberto
dc.date.available 2018-08-15T19:33:28Z
dc.date.issued 2016-05
dc.identifier.citation Rodriguez, J.; Soria, Francisco Fernando; Geronazzo, Hugo Isidoro; Destefanis, Hugo Alberto; Modification and characterization of natural aluminosilicates, expanded perlite, and its application to immobilise α – amylase from A. oryzae; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 133; 5-2016; S259-S270
dc.identifier.issn 1381-1177
dc.identifier.uri http://hdl.handle.net/11336/55729
dc.description.abstract The aim of this study was to modify natural silicoaluminates as expanded perlite (EP) through simple and inexpensive treatments in order to get a greater reactivity of surface and immobilise α-amylase from A. oryzae by adsorption and covalent binding. The materials obtained (expanded perlite treated with HCl, rehydroxylated expanded perlite, zeolite, and the incorporation of polystyrene in expanded perlite) were analysed by infrared spectroscopy, thermal analysis, zeta potential, adsorption of N2, and Scanning Electron Microscopy. The analysis allowed us to confirm that the modifications on the materials studied were effective. This is perceived by an increase in bands corresponding to OH groups, which is beneficial when considering functional groups that interact directly with the enzyme. It also allowed us to determine that the materials tested exhibit good thermal stability at the temperature range in which enzymatic studies are conducted. The conditions for immobilisation (pH, concentration of glutaraldehyde, time of contact between the enzyme and the substrate, enzyme concentration) and some properties of the immobilised derivatives (optimum pH, temperature of maximum activity, and reuse) were analysed. The suitable range for the immobilisation of α-amylase from A. oryzae by covalent binding was pH between 5 and 6, and for immobilisation by adsorption the suitable pH range was between 5 and 5.5. These values ​​are consistent with the zeta potential values ​​previously determined for the different media studied. The reuse of the immobilised enzyme by covalent binding resulted in a residual activity of 90% up to the sixth reuse. Immobilisation by covalent binding was more effective than immobilisation by adsorption.
dc.format application/pdf
dc.language.iso eng
dc.publisher Elsevier Science
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject ALPHA AMYLASE
dc.subject IMMOBILISED ENZYME
dc.subject PERLITES
dc.subject.classification Otras Ingeniería Química
dc.subject.classification Ingeniería Química
dc.subject.classification INGENIERÍAS Y TECNOLOGÍAS
dc.title Modification and characterization of natural aluminosilicates, expanded perlite, and its application to immobilise α – amylase from A. oryzae
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2018-08-15T13:59:05Z
dc.journal.volume 133
dc.journal.pagination S259-S270
dc.journal.pais Países Bajos
dc.journal.ciudad Amsterdam
dc.description.fil Fil: Rodriguez, J.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; Argentina
dc.description.fil Fil: Soria, Francisco Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; Argentina
dc.description.fil Fil: Geronazzo, Hugo Isidoro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; Argentina
dc.description.fil Fil: Destefanis, Hugo Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Investigaciones para la Industria Química. Universidad Nacional de Salta. Facultad de Ingeniería. Instituto de Investigaciones para la Industria Química; Argentina
dc.journal.title Journal of Molecular Catalysis B: Enzymatic
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1016/j.molcatb.2017.01.012
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1381117717300127
dc.conicet.fuente Elsevier


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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)