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...
| Main Authors: | , , |
|---|---|
| Format: | Online |
| Language: | spa |
| Published: |
Universidad Pedagógica y Tecnológica de Colombia
2021
|
| Subjects: | |
| Online Access: | https://revistas.uptc.edu.co/index.php/ciencia_en_desarrollo/article/view/12818 |
| _version_ | 1801706350103756800 |
|---|---|
| author | Vargas, Annie Y. Romanelli, Gustavo P. Martinez, Jose J. |
| author_facet | Vargas, Annie Y. Romanelli, Gustavo P. Martinez, Jose J. |
| author_sort | Vargas, Annie Y. |
| collection | OJS |
| 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. |
| format | Online |
| id | oai:oai.revistas.uptc.edu.co:article-12818 |
| institution | Revista Ciencia en Desarrollo |
| language | spa |
| publishDate | 2021 |
| publisher | Universidad Pedagógica y Tecnológica de Colombia |
| record_format | ojs |
| spelling | oai:oai.revistas.uptc.edu.co:article-128182021-12-14T02:35:17Z Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization Nanopartículas magnéticas funcionalizadas y modificadas con entrecruzamiento para mejorar la inmovilización de la invertasa Vargas, Annie Y. Romanelli, Gustavo P. Martinez, Jose J. invertasa Fe3O4 Inmobilizacion compuestos invertase, Fe3O4, immobilization, composites. 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. 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. Universidad Pedagógica y Tecnológica de Colombia 2021-01-08 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion application/pdf https://revistas.uptc.edu.co/index.php/ciencia_en_desarrollo/article/view/12818 10.19053/01217488.v12.n1.2021.12818 Ciencia En Desarrollo; Vol. 12 No. 1 (2021): Vol 12, Núm.1 (2021): Enero-Junio; 69-77 Ciencia en Desarrollo; Vol. 12 Núm. 1 (2021): Vol 12, Núm.1 (2021): Enero-Junio; 69-77 2462-7658 0121-7488 spa https://revistas.uptc.edu.co/index.php/ciencia_en_desarrollo/article/view/12818/10694 Derechos de autor 2021 CIENCIA EN DESARROLLO |
| spellingShingle | invertasa Fe3O4 Inmobilizacion compuestos invertase, Fe3O4, immobilization, composites. Vargas, Annie Y. Romanelli, Gustavo P. Martinez, Jose J. Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization |
| title | Magnetic Nanoparticles Functionalized And Modified With Cross-Linking To Improve The Invertase Immobilization |
| title_alt | Nanopartículas magnéticas funcionalizadas y modificadas con entrecruzamiento para mejorar la inmovilización de la invertasa |
| 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_short | 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 |
| topic | invertasa Fe3O4 Inmobilizacion compuestos invertase, Fe3O4, immobilization, composites. |
| topic_facet | invertasa Fe3O4 Inmobilizacion compuestos invertase, Fe3O4, immobilization, composites. |
| url | https://revistas.uptc.edu.co/index.php/ciencia_en_desarrollo/article/view/12818 |
| work_keys_str_mv | AT vargasanniey magneticnanoparticlesfunctionalizedandmodifiedwithcrosslinkingtoimprovetheinvertaseimmobilization AT romanelligustavop magneticnanoparticlesfunctionalizedandmodifiedwithcrosslinkingtoimprovetheinvertaseimmobilization AT martinezjosej magneticnanoparticlesfunctionalizedandmodifiedwithcrosslinkingtoimprovetheinvertaseimmobilization AT vargasanniey nanoparticulasmagneticasfuncionalizadasymodificadasconentrecruzamientoparamejorarlainmovilizaciondelainvertasa AT romanelligustavop nanoparticulasmagneticasfuncionalizadasymodificadasconentrecruzamientoparamejorarlainmovilizaciondelainvertasa AT martinezjosej nanoparticulasmagneticasfuncionalizadasymodificadasconentrecruzamientoparamejorarlainmovilizaciondelainvertasa |
