Synthesis of 1,4-dihydropyrimidines with immobilized urease: Effect of method immobilization on magnetic supports

Autores
Vargas, Annie Y.; Rojas, Hugo A.; Romanelli, Gustavo Pablo; Martínez Zambrano, José Jobanny
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The effect of the urease immobilization method was studied on magnetic supports for the Biginelli/Hantzsch reaction. For this purpose, Fe3O4/SiO2 was modified with 3-Aminopropyl-Triethoxysilane and then activated with glutaraldehyde. A ratio of 500 mg of enzyme per gram of support at 4°C and 18 h were sufficient for the physical adsorption, while 24 h were required for covalent bonding. The Biginelli and Hantzsch reactions were used to evaluate urease application in multicomponent reactions (MCRs). The synthesis of 1,4-dihydropyrimidines was successfully performed using immobilized urease favoring the Hantzsch product. The magnetic properties of the supports allow easy separation, and the urease immobilized by both methods improved the enzymatic activity compared to that of free urease.
Centro de Investigación y Desarrollo en Ciencias Aplicadas
Materia
Química
Biginelli/Hantzsch reaction
magnetic supports
urease immobilized
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/87296
Acceder
id SEDICI_96239f4633e5a8791c434fcafe1a26e8
oai_identifier_str oai:sedici.unlp.edu.ar:10915/87296
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Synthesis of 1,4-dihydropyrimidines with immobilized urease: Effect of method immobilization on magnetic supportsVargas, Annie Y.Rojas, Hugo A.Romanelli, Gustavo PabloMartínez Zambrano, José JobannyQuímicaBiginelli/Hantzsch reactionmagnetic supportsurease immobilizedThe effect of the urease immobilization method was studied on magnetic supports for the Biginelli/Hantzsch reaction. For this purpose, Fe3O4/SiO2 was modified with 3-Aminopropyl-Triethoxysilane and then activated with glutaraldehyde. A ratio of 500 mg of enzyme per gram of support at 4°C and 18 h were sufficient for the physical adsorption, while 24 h were required for covalent bonding. The Biginelli and Hantzsch reactions were used to evaluate urease application in multicomponent reactions (MCRs). The synthesis of 1,4-dihydropyrimidines was successfully performed using immobilized urease favoring the Hantzsch product. The magnetic properties of the supports allow easy separation, and the urease immobilized by both methods improved the enzymatic activity compared to that of free urease.Centro de Investigación y Desarrollo en Ciencias Aplicadas2017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf377-384http://sedici.unlp.edu.ar/handle/10915/87296enginfo:eu-repo/semantics/altIdentifier/issn/2191-9542info:eu-repo/semantics/altIdentifier/doi/10.1515/gps-2016-0143info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-15T11:09:06Zoai:sedici.unlp.edu.ar:10915/87296Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:09:07.132SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Synthesis of 1,4-dihydropyrimidines with immobilized urease: Effect of method immobilization on magnetic supports
title Synthesis of 1,4-dihydropyrimidines with immobilized urease: Effect of method immobilization on magnetic supports
spellingShingle Synthesis of 1,4-dihydropyrimidines with immobilized urease: Effect of method immobilization on magnetic supports
Vargas, Annie Y.
Química
Biginelli/Hantzsch reaction
magnetic supports
urease immobilized
title_short Synthesis of 1,4-dihydropyrimidines with immobilized urease: Effect of method immobilization on magnetic supports
title_full Synthesis of 1,4-dihydropyrimidines with immobilized urease: Effect of method immobilization on magnetic supports
title_fullStr Synthesis of 1,4-dihydropyrimidines with immobilized urease: Effect of method immobilization on magnetic supports
title_full_unstemmed Synthesis of 1,4-dihydropyrimidines with immobilized urease: Effect of method immobilization on magnetic supports
title_sort Synthesis of 1,4-dihydropyrimidines with immobilized urease: Effect of method immobilization on magnetic supports
dc.creator.none.fl_str_mv Vargas, Annie Y.
Rojas, Hugo A.
Romanelli, Gustavo Pablo
Martínez Zambrano, José Jobanny
author Vargas, Annie Y.
author_facet Vargas, Annie Y.
Rojas, Hugo A.
Romanelli, Gustavo Pablo
Martínez Zambrano, José Jobanny
author_role author
author2 Rojas, Hugo A.
Romanelli, Gustavo Pablo
Martínez Zambrano, José Jobanny
author2_role author
author
author
dc.subject.none.fl_str_mv Química
Biginelli/Hantzsch reaction
magnetic supports
urease immobilized
topic Química
Biginelli/Hantzsch reaction
magnetic supports
urease immobilized
dc.description.none.fl_txt_mv The effect of the urease immobilization method was studied on magnetic supports for the Biginelli/Hantzsch reaction. For this purpose, Fe3O4/SiO2 was modified with 3-Aminopropyl-Triethoxysilane and then activated with glutaraldehyde. A ratio of 500 mg of enzyme per gram of support at 4°C and 18 h were sufficient for the physical adsorption, while 24 h were required for covalent bonding. The Biginelli and Hantzsch reactions were used to evaluate urease application in multicomponent reactions (MCRs). The synthesis of 1,4-dihydropyrimidines was successfully performed using immobilized urease favoring the Hantzsch product. The magnetic properties of the supports allow easy separation, and the urease immobilized by both methods improved the enzymatic activity compared to that of free urease.
Centro de Investigación y Desarrollo en Ciencias Aplicadas
description The effect of the urease immobilization method was studied on magnetic supports for the Biginelli/Hantzsch reaction. For this purpose, Fe3O4/SiO2 was modified with 3-Aminopropyl-Triethoxysilane and then activated with glutaraldehyde. A ratio of 500 mg of enzyme per gram of support at 4°C and 18 h were sufficient for the physical adsorption, while 24 h were required for covalent bonding. The Biginelli and Hantzsch reactions were used to evaluate urease application in multicomponent reactions (MCRs). The synthesis of 1,4-dihydropyrimidines was successfully performed using immobilized urease favoring the Hantzsch product. The magnetic properties of the supports allow easy separation, and the urease immobilized by both methods improved the enzymatic activity compared to that of free urease.
publishDate 2017
dc.date.none.fl_str_mv 2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/87296
url http://sedici.unlp.edu.ar/handle/10915/87296
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/2191-9542
info:eu-repo/semantics/altIdentifier/doi/10.1515/gps-2016-0143
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
377-384
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.22299

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