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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/openAccess  
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