Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interfa...

Autores
Monti, Gustavo Antonio; Falcone, Ruben Dario; Moyano, Fernando; Correa, Nestor Mariano
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this work, we present an investigation of the influence of water encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate/methyl laurate and 1,4-bis-2-ethylhexylsulfosuccinate/isopropyl myristate reverse micelles on the enzymatic hydrolysis of 1-naphthyl phosphate by alkaline phosphatase. Our results show that the enzyme is active in the biocompatible reverse micelles studied and that the Michaelis–Menten kinetic model is valid in all systems. We found that both micellar systems studied have a particular behavior toward pH and that the penetration of external solvents into the interfaces is crucial to understanding the effect. Methyl laurate does not disrupt the interface and is not necessary to control the pH value since alkaline phosphatase in the center of the micelles is always solvated similarly. In contrast, isopropyl myristate disrupts the interfaces so that the water and 1-naphthol molecules cannot form hydrogen bond interactions with the polar head of the surfactant. Then, when the water is at pH = 7, the 1-naphthol moves away to the interfaces inhibiting alkaline phosphatase which is not observable when the water is at pH = 10. Our study shows that the concept of pH cannot be used directly in a confined environment. In addition, our research is of great importance in the field of reactions that occur in reverse micelles, catalyzed by enzymes.
Fil: Monti, Gustavo Antonio. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Instituto de Investigaciones en Tecnologías Energéticas y Materiales Avanzados. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Tecnologías Energéticas y Materiales Avanzados; Argentina. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; Argentina
Fil: Falcone, Ruben Dario. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; Argentina
Fil: Moyano, Fernando. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; Argentina
Fil: Correa, Nestor Mariano. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; Argentina
Materia
Alkaline Phosphatase
Reverse Micelles
Isopropyl myristate
Methyl laurate
Hydrogen bond
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/218995
Acceder
id CONICETDig_58e413a7d6a298489dbd388bc2481871
oai_identifier_str oai:ri.conicet.gov.ar:11336/218995
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interfaceMonti, Gustavo AntonioFalcone, Ruben DarioMoyano, FernandoCorrea, Nestor MarianoAlkaline PhosphataseReverse MicellesIsopropyl myristateMethyl laurateHydrogen bondhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1In this work, we present an investigation of the influence of water encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate/methyl laurate and 1,4-bis-2-ethylhexylsulfosuccinate/isopropyl myristate reverse micelles on the enzymatic hydrolysis of 1-naphthyl phosphate by alkaline phosphatase. Our results show that the enzyme is active in the biocompatible reverse micelles studied and that the Michaelis–Menten kinetic model is valid in all systems. We found that both micellar systems studied have a particular behavior toward pH and that the penetration of external solvents into the interfaces is crucial to understanding the effect. Methyl laurate does not disrupt the interface and is not necessary to control the pH value since alkaline phosphatase in the center of the micelles is always solvated similarly. In contrast, isopropyl myristate disrupts the interfaces so that the water and 1-naphthol molecules cannot form hydrogen bond interactions with the polar head of the surfactant. Then, when the water is at pH = 7, the 1-naphthol moves away to the interfaces inhibiting alkaline phosphatase which is not observable when the water is at pH = 10. Our study shows that the concept of pH cannot be used directly in a confined environment. In addition, our research is of great importance in the field of reactions that occur in reverse micelles, catalyzed by enzymes.Fil: Monti, Gustavo Antonio. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Instituto de Investigaciones en Tecnologías Energéticas y Materiales Avanzados. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Tecnologías Energéticas y Materiales Avanzados; Argentina. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; ArgentinaFil: Falcone, Ruben Dario. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; ArgentinaFil: Moyano, Fernando. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; ArgentinaFil: Correa, Nestor Mariano. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; ArgentinaRoyal Society of Chemistry2023-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/218995Monti, Gustavo Antonio; Falcone, Ruben Dario; Moyano, Fernando; Correa, Nestor Mariano; Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface; Royal Society of Chemistry; RSC Advances; 13; 2; 1-2023; 1194-12022046-2069CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1039/d2ra06296hinfo:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2023/RA/D2RA06296Hinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:29:56Zoai:ri.conicet.gov.ar:11336/218995instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:29:56.938CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface
title Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface
spellingShingle Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface
Monti, Gustavo Antonio
Alkaline Phosphatase
Reverse Micelles
Isopropyl myristate
Methyl laurate
Hydrogen bond
title_short Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface
title_full Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface
title_fullStr Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface
title_full_unstemmed Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface
title_sort Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface
dc.creator.none.fl_str_mv Monti, Gustavo Antonio
Falcone, Ruben Dario
Moyano, Fernando
Correa, Nestor Mariano
author Monti, Gustavo Antonio
author_facet Monti, Gustavo Antonio
Falcone, Ruben Dario
Moyano, Fernando
Correa, Nestor Mariano
author_role author
author2 Falcone, Ruben Dario
Moyano, Fernando
Correa, Nestor Mariano
author2_role author
author
author
dc.subject.none.fl_str_mv Alkaline Phosphatase
Reverse Micelles
Isopropyl myristate
Methyl laurate
Hydrogen bond
topic Alkaline Phosphatase
Reverse Micelles
Isopropyl myristate
Methyl laurate
Hydrogen bond
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In this work, we present an investigation of the influence of water encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate/methyl laurate and 1,4-bis-2-ethylhexylsulfosuccinate/isopropyl myristate reverse micelles on the enzymatic hydrolysis of 1-naphthyl phosphate by alkaline phosphatase. Our results show that the enzyme is active in the biocompatible reverse micelles studied and that the Michaelis–Menten kinetic model is valid in all systems. We found that both micellar systems studied have a particular behavior toward pH and that the penetration of external solvents into the interfaces is crucial to understanding the effect. Methyl laurate does not disrupt the interface and is not necessary to control the pH value since alkaline phosphatase in the center of the micelles is always solvated similarly. In contrast, isopropyl myristate disrupts the interfaces so that the water and 1-naphthol molecules cannot form hydrogen bond interactions with the polar head of the surfactant. Then, when the water is at pH = 7, the 1-naphthol moves away to the interfaces inhibiting alkaline phosphatase which is not observable when the water is at pH = 10. Our study shows that the concept of pH cannot be used directly in a confined environment. In addition, our research is of great importance in the field of reactions that occur in reverse micelles, catalyzed by enzymes.
Fil: Monti, Gustavo Antonio. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Instituto de Investigaciones en Tecnologías Energéticas y Materiales Avanzados. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Tecnologías Energéticas y Materiales Avanzados; Argentina. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; Argentina
Fil: Falcone, Ruben Dario. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; Argentina
Fil: Moyano, Fernando. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; Argentina
Fil: Correa, Nestor Mariano. Universidad Nacional de Río Cuarto. Instituto para el Desarrollo Agroindustrial y de la Salud. - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto para el Desarrollo Agroindustrial y de la Salud; Argentina
description In this work, we present an investigation of the influence of water encapsulated in 1,4-bis-2-ethylhexylsulfosuccinate/methyl laurate and 1,4-bis-2-ethylhexylsulfosuccinate/isopropyl myristate reverse micelles on the enzymatic hydrolysis of 1-naphthyl phosphate by alkaline phosphatase. Our results show that the enzyme is active in the biocompatible reverse micelles studied and that the Michaelis–Menten kinetic model is valid in all systems. We found that both micellar systems studied have a particular behavior toward pH and that the penetration of external solvents into the interfaces is crucial to understanding the effect. Methyl laurate does not disrupt the interface and is not necessary to control the pH value since alkaline phosphatase in the center of the micelles is always solvated similarly. In contrast, isopropyl myristate disrupts the interfaces so that the water and 1-naphthol molecules cannot form hydrogen bond interactions with the polar head of the surfactant. Then, when the water is at pH = 7, the 1-naphthol moves away to the interfaces inhibiting alkaline phosphatase which is not observable when the water is at pH = 10. Our study shows that the concept of pH cannot be used directly in a confined environment. In addition, our research is of great importance in the field of reactions that occur in reverse micelles, catalyzed by enzymes.
publishDate 2023
dc.date.none.fl_str_mv 2023-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/218995
Monti, Gustavo Antonio; Falcone, Ruben Dario; Moyano, Fernando; Correa, Nestor Mariano; Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface; Royal Society of Chemistry; RSC Advances; 13; 2; 1-2023; 1194-1202
2046-2069
CONICET Digital
CONICET
url http://hdl.handle.net/11336/218995
identifier_str_mv Monti, Gustavo Antonio; Falcone, Ruben Dario; Moyano, Fernando; Correa, Nestor Mariano; Green AOT reverse micelles as nanoreactors for alkaline phosphatase. The hydrogen bond “dances” between water and the enzyme, the reaction product, and the reverse micelles interface; Royal Society of Chemistry; RSC Advances; 13; 2; 1-2023; 1194-1202
2046-2069
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1039/d2ra06296h
info:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2023/RA/D2RA06296H
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846083438326579200
score 13.22299

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