Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization

Procedures of immobilization invertase have been developed using different supports. However, disadvantages such as use of small particles for invertase immobilizations in packed-bed reactors are being solved using magnetic particles. In this study, composites containing Fe3O4 were prepared by incor...

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Autores:
Tipo de recurso:
Fecha de publicación:
2021
Institución:
Universidad Pedagógica y Tecnológica de Colombia
Repositorio:
RiUPTC: Repositorio Institucional UPTC
Idioma:
spa
OAI Identifier:
oai:repositorio.uptc.edu.co:001/15320
Acceso en línea:
https://revistas.uptc.edu.co/index.php/ciencia_en_desarrollo/article/view/12818
https://repositorio.uptc.edu.co/handle/001/15320
Palabra clave:
invertasa
Fe3O4
Inmobilizacion
compuestos
invertase, Fe3O4, immobilization, composites.
Rights
License
Derechos de autor 2021 CIENCIA EN DESARROLLO
id REPOUPTC2_8ce49e6c074f4ce027809150dfab3bf7
oai_identifier_str oai:repositorio.uptc.edu.co:001/15320
network_acronym_str REPOUPTC2
network_name_str RiUPTC: Repositorio Institucional UPTC
repository_id_str
dc.title.en-US.fl_str_mv Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization
dc.title.es-ES.fl_str_mv Nanopartículas magnéticas funcionalizadas y modificadas con entrecruzamiento para mejorar la inmovilización de la invertasa
title Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization
spellingShingle Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization
invertasa
Fe3O4
Inmobilizacion
compuestos
invertase, Fe3O4, immobilization, composites.
title_short Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization
title_full Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization
title_fullStr Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization
title_full_unstemmed Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization
title_sort Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization
dc.subject.es-ES.fl_str_mv invertasa
Fe3O4
Inmobilizacion
compuestos
topic invertasa
Fe3O4
Inmobilizacion
compuestos
invertase, Fe3O4, immobilization, composites.
dc.subject.en-US.fl_str_mv invertase, Fe3O4, immobilization, composites.
description Procedures of immobilization invertase have been developed using different supports. However, disadvantages such as use of small particles for invertase immobilizations in packed-bed reactors are being solved using magnetic particles. In this study, composites containing Fe3O4 were prepared by incorporation of a polysiloxane layer required for the physical adsorption of the invertase. Besides, the functionalized magnetite was activated with glutaraldehyde and polyethylenimine (PEI) with the aim of performing a covalent immobilization. The effect of different conditions such as enzyme:support ratio, pH, and temperature were analyzed in the preservation of invertase. The results demonstrated that the optimum enzyme:support ratio is higher for covalent bonding than for physical adsorption. The ideal pH for the immobilized enzyme is 5.0, and the enzymatic activity is retained until 70°C. The values of km are similar in both immobilization methods. The analysis of the effect of pH and thermostability showed that the catalytic activity of invertase is not affected in comparison with the free enzyme. The covalent immobilization displays higher efficiency in the immobilization process (Fε), less inhibition and twice as much stability. The enzymes immobilized by physical and covalent methods can be reused for up to four cycles and can be removed from the reaction medium by applying an external magnetic field.
publishDate 2021
dc.date.accessioned.none.fl_str_mv 2024-07-08T14:24:03Z
dc.date.available.none.fl_str_mv 2024-07-08T14:24:03Z
dc.date.none.fl_str_mv 2021-01-08
dc.type.none.fl_str_mv info:eu-repo/semantics/article
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_2df8fbb1
dc.identifier.none.fl_str_mv https://revistas.uptc.edu.co/index.php/ciencia_en_desarrollo/article/view/12818
10.19053/01217488.v12.n1.2021.12818
dc.identifier.uri.none.fl_str_mv https://repositorio.uptc.edu.co/handle/001/15320
url https://revistas.uptc.edu.co/index.php/ciencia_en_desarrollo/article/view/12818
https://repositorio.uptc.edu.co/handle/001/15320
identifier_str_mv 10.19053/01217488.v12.n1.2021.12818
dc.language.none.fl_str_mv spa
dc.language.iso.none.fl_str_mv spa
language spa
dc.relation.none.fl_str_mv https://revistas.uptc.edu.co/index.php/ciencia_en_desarrollo/article/view/12818/10694
dc.rights.es-ES.fl_str_mv Derechos de autor 2021 CIENCIA EN DESARROLLO
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
rights_invalid_str_mv Derechos de autor 2021 CIENCIA EN DESARROLLO
http://purl.org/coar/access_right/c_abf2
dc.format.none.fl_str_mv application/pdf
dc.publisher.es-ES.fl_str_mv Universidad Pedagógica y Tecnológica de Colombia
dc.source.en-US.fl_str_mv Ciencia En Desarrollo; Vol. 12 No. 1 (2021): Vol 12, Núm.1 (2021): Enero-Junio; 69-77
dc.source.es-ES.fl_str_mv Ciencia en Desarrollo; Vol. 12 Núm. 1 (2021): Vol 12, Núm.1 (2021): Enero-Junio; 69-77
dc.source.none.fl_str_mv 2462-7658
0121-7488
institution Universidad Pedagógica y Tecnológica de Colombia
repository.name.fl_str_mv Repositorio Institucional UPTC
repository.mail.fl_str_mv repositorio.uptc@uptc.edu.co
_version_ 1839633857242988544
spelling 2021-01-082024-07-08T14:24:03Z2024-07-08T14:24:03Zhttps://revistas.uptc.edu.co/index.php/ciencia_en_desarrollo/article/view/1281810.19053/01217488.v12.n1.2021.12818https://repositorio.uptc.edu.co/handle/001/15320Procedures of immobilization invertase have been developed using different supports. However, disadvantages such as use of small particles for invertase immobilizations in packed-bed reactors are being solved using magnetic particles. In this study, composites containing Fe3O4 were prepared by incorporation of a polysiloxane layer required for the physical adsorption of the invertase. Besides, the functionalized magnetite was activated with glutaraldehyde and polyethylenimine (PEI) with the aim of performing a covalent immobilization. The effect of different conditions such as enzyme:support ratio, pH, and temperature were analyzed in the preservation of invertase. The results demonstrated that the optimum enzyme:support ratio is higher for covalent bonding than for physical adsorption. The ideal pH for the immobilized enzyme is 5.0, and the enzymatic activity is retained until 70°C. The values of km are similar in both immobilization methods. The analysis of the effect of pH and thermostability showed that the catalytic activity of invertase is not affected in comparison with the free enzyme. The covalent immobilization displays higher efficiency in the immobilization process (Fε), less inhibition and twice as much stability. The enzymes immobilized by physical and covalent methods can be reused for up to four cycles and can be removed from the reaction medium by applying an external magnetic field.Se han desarrollado procedimientos de inmovilización con invertasa utilizando diferentes soportes. Sin embargo, las desventajas como el uso de partículas pequeñas para inmovilizaciones de invertasa en reactores de lecho compacto se están resolviendo utilizando partículas magnéticas. En este estudio, los compuestos que contienen Fe3O4 se prepararon mediante la incorporación de una capa de polisiloxano necesaria para la adsorción física de la invertasa. Además, la magnetita funcionalizada se activó con glutaraldehído y polietilenimina (PEI) con el objetivo de realizar una inmovilización covalente. Se analizó el efecto de diferentes condiciones como la relación enzima: soporte, pH y temperatura en la conservación de la invertasa. Los resultados demostraron que la relación enzima: soporte óptima es mayor para la unión covalente que para la adsorción física. El pH ideal para la enzima inmovilizada es 5,0 y la actividad enzimática se mantiene hasta 70 ° C. Los valores de km son similares en ambos métodos de inmovilización. El análisis del efecto del pH y la termoestabilidad mostró que la actividad catalítica de la invertasa no se ve afectada en comparación con la enzima libre. La inmovilización covalente muestra una mayor eficacia en el proceso de inmovilización (Fε), menos inhibición y el doble de estabilidad. Las enzimas inmovilizadas por métodos físicos y covalentes se pueden reutilizar hasta por cuatro ciclos y se pueden eliminar del medio de reacción aplicando un campo magnético externo.application/pdfspaspaUniversidad Pedagógica y Tecnológica de Colombiahttps://revistas.uptc.edu.co/index.php/ciencia_en_desarrollo/article/view/12818/10694Derechos de autor 2021 CIENCIA EN DESARROLLOhttp://purl.org/coar/access_right/c_abf2Ciencia En Desarrollo; Vol. 12 No. 1 (2021): Vol 12, Núm.1 (2021): Enero-Junio; 69-77Ciencia en Desarrollo; Vol. 12 Núm. 1 (2021): Vol 12, Núm.1 (2021): Enero-Junio; 69-772462-76580121-7488invertasaFe3O4Inmobilizacioncompuestosinvertase, Fe3O4, immobilization, composites.Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase ImmobilizationNanopartículas magnéticas funcionalizadas y modificadas con entrecruzamiento para mejorar la inmovilización de la invertasainfo:eu-repo/semantics/articlehttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_2df8fbb1Vargas, Annie Y.Romanelli, Gustavo P.Martinez, Jose J.001/15320oai:repositorio.uptc.edu.co:001/153202025-07-18 10:56:40.243metadata.onlyhttps://repositorio.uptc.edu.coRepositorio Institucional UPTCrepositorio.uptc@uptc.edu.co