β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions

Autores
Santagapita, Patricio Roman; Gómez Brizuela, Leissy; Mazzobre, Maria Florencia; Ramirez, Héctor L.; Corti, Horacio Roberto; Villalonga Santana, Reynaldo; Buera, Maria del Pilar
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The effect of β-cyclodextrin modifications (polymerization (PCD) and later carboxymethylation (CMPCD)) on their action as enzyme stabilizers was analyzed during freeze-drying and thermal treatment. Combined polymer-trehalose matrices were also employed. Due to their higher Tg values, PCD and CMPCD provided better structural stability to the freeze-dried formulations than β-CD. However, only PCD was a good excipient to protect invertase both in amorphous and supercooled systems. FT-IR revealed increased protein denaturation in the presence of CMPCD, but not in the presence of PCD. Even though all polymers inhibited/delayed trehalose crystallization, only trehalose (T) combined with PCD (PCD + T) and with β-cyclodextrin (β-CD + T) offered the best stability to the enzyme. In β-CD + T system, trehalose was the main responsible for the protection. In PCD + T system, both additives contributed to improve the enzyme stability. FT-IR and DSC were useful to analyze the combined role of molecular and supramolecular interactions on enzyme stability in dehydrated model systems.
Fil: Santagapita, Patricio Roman. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; Argentina
Fil: Gómez Brizuela, Leissy. Universidad de Matanzas Camilo Cienfuegos; Cuba
Fil: Mazzobre, Maria Florencia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; Argentina
Fil: Ramirez, Héctor L.. Universidad de Matanzas “Camilo Cienfuegos”; Cuba
Fil: Corti, Horacio Roberto. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Comisión Nacional de Energía Atómica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; Argentina
Fil: Villalonga Santana, Reynaldo. Universidad de Matanzas “Camilo Cienfuegos”; Cuba
Fil: Buera, Maria del Pilar. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; Argentina
Materia
ADDITIVES
ENZYME STABILITY
FREEZE-DRIED ENZYME FORMULATIONS
MODIFIED CYCLODEXTRINS
POLYCYCLODEXTRIN
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:11336/113194
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/113194
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactionsSantagapita, Patricio RomanGómez Brizuela, LeissyMazzobre, Maria FlorenciaRamirez, Héctor L.Corti, Horacio RobertoVillalonga Santana, ReynaldoBuera, Maria del PilarADDITIVESENZYME STABILITYFREEZE-DRIED ENZYME FORMULATIONSMODIFIED CYCLODEXTRINSPOLYCYCLODEXTRINhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The effect of β-cyclodextrin modifications (polymerization (PCD) and later carboxymethylation (CMPCD)) on their action as enzyme stabilizers was analyzed during freeze-drying and thermal treatment. Combined polymer-trehalose matrices were also employed. Due to their higher Tg values, PCD and CMPCD provided better structural stability to the freeze-dried formulations than β-CD. However, only PCD was a good excipient to protect invertase both in amorphous and supercooled systems. FT-IR revealed increased protein denaturation in the presence of CMPCD, but not in the presence of PCD. Even though all polymers inhibited/delayed trehalose crystallization, only trehalose (T) combined with PCD (PCD + T) and with β-cyclodextrin (β-CD + T) offered the best stability to the enzyme. In β-CD + T system, trehalose was the main responsible for the protection. In PCD + T system, both additives contributed to improve the enzyme stability. FT-IR and DSC were useful to analyze the combined role of molecular and supramolecular interactions on enzyme stability in dehydrated model systems.Fil: Santagapita, Patricio Roman. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; ArgentinaFil: Gómez Brizuela, Leissy. Universidad de Matanzas Camilo Cienfuegos; CubaFil: Mazzobre, Maria Florencia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; ArgentinaFil: Ramirez, Héctor L.. Universidad de Matanzas “Camilo Cienfuegos”; CubaFil: Corti, Horacio Roberto. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Comisión Nacional de Energía Atómica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; ArgentinaFil: Villalonga Santana, Reynaldo. Universidad de Matanzas “Camilo Cienfuegos”; CubaFil: Buera, Maria del Pilar. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; ArgentinaElsevier2011-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/113194Santagapita, Patricio Roman; Gómez Brizuela, Leissy; Mazzobre, Maria Florencia; Ramirez, Héctor L.; Corti, Horacio Roberto; et al.; β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions; Elsevier; Carbohydrate Polymers; 83; 1; 1-2011; 203-2090144-8617CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.carbpol.2010.07.041info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0144861710005849info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:41:43Zoai:ri.conicet.gov.ar:11336/113194instacron: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:34982025-10-22 11:41:43.798CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions
title β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions
spellingShingle β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions
Santagapita, Patricio Roman
ADDITIVES
ENZYME STABILITY
FREEZE-DRIED ENZYME FORMULATIONS
MODIFIED CYCLODEXTRINS
POLYCYCLODEXTRIN
title_short β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions
title_full β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions
title_fullStr β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions
title_full_unstemmed β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions
title_sort β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions
dc.creator.none.fl_str_mv Santagapita, Patricio Roman
Gómez Brizuela, Leissy
Mazzobre, Maria Florencia
Ramirez, Héctor L.
Corti, Horacio Roberto
Villalonga Santana, Reynaldo
Buera, Maria del Pilar
author Santagapita, Patricio Roman
author_facet Santagapita, Patricio Roman
Gómez Brizuela, Leissy
Mazzobre, Maria Florencia
Ramirez, Héctor L.
Corti, Horacio Roberto
Villalonga Santana, Reynaldo
Buera, Maria del Pilar
author_role author
author2 Gómez Brizuela, Leissy
Mazzobre, Maria Florencia
Ramirez, Héctor L.
Corti, Horacio Roberto
Villalonga Santana, Reynaldo
Buera, Maria del Pilar
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv ADDITIVES
ENZYME STABILITY
FREEZE-DRIED ENZYME FORMULATIONS
MODIFIED CYCLODEXTRINS
POLYCYCLODEXTRIN
topic ADDITIVES
ENZYME STABILITY
FREEZE-DRIED ENZYME FORMULATIONS
MODIFIED CYCLODEXTRINS
POLYCYCLODEXTRIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The effect of β-cyclodextrin modifications (polymerization (PCD) and later carboxymethylation (CMPCD)) on their action as enzyme stabilizers was analyzed during freeze-drying and thermal treatment. Combined polymer-trehalose matrices were also employed. Due to their higher Tg values, PCD and CMPCD provided better structural stability to the freeze-dried formulations than β-CD. However, only PCD was a good excipient to protect invertase both in amorphous and supercooled systems. FT-IR revealed increased protein denaturation in the presence of CMPCD, but not in the presence of PCD. Even though all polymers inhibited/delayed trehalose crystallization, only trehalose (T) combined with PCD (PCD + T) and with β-cyclodextrin (β-CD + T) offered the best stability to the enzyme. In β-CD + T system, trehalose was the main responsible for the protection. In PCD + T system, both additives contributed to improve the enzyme stability. FT-IR and DSC were useful to analyze the combined role of molecular and supramolecular interactions on enzyme stability in dehydrated model systems.
Fil: Santagapita, Patricio Roman. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; Argentina
Fil: Gómez Brizuela, Leissy. Universidad de Matanzas Camilo Cienfuegos; Cuba
Fil: Mazzobre, Maria Florencia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; Argentina
Fil: Ramirez, Héctor L.. Universidad de Matanzas “Camilo Cienfuegos”; Cuba
Fil: Corti, Horacio Roberto. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Comisión Nacional de Energía Atómica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; Argentina
Fil: Villalonga Santana, Reynaldo. Universidad de Matanzas “Camilo Cienfuegos”; Cuba
Fil: Buera, Maria del Pilar. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; Argentina
description The effect of β-cyclodextrin modifications (polymerization (PCD) and later carboxymethylation (CMPCD)) on their action as enzyme stabilizers was analyzed during freeze-drying and thermal treatment. Combined polymer-trehalose matrices were also employed. Due to their higher Tg values, PCD and CMPCD provided better structural stability to the freeze-dried formulations than β-CD. However, only PCD was a good excipient to protect invertase both in amorphous and supercooled systems. FT-IR revealed increased protein denaturation in the presence of CMPCD, but not in the presence of PCD. Even though all polymers inhibited/delayed trehalose crystallization, only trehalose (T) combined with PCD (PCD + T) and with β-cyclodextrin (β-CD + T) offered the best stability to the enzyme. In β-CD + T system, trehalose was the main responsible for the protection. In PCD + T system, both additives contributed to improve the enzyme stability. FT-IR and DSC were useful to analyze the combined role of molecular and supramolecular interactions on enzyme stability in dehydrated model systems.
publishDate 2011
dc.date.none.fl_str_mv 2011-01
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/11336/113194
Santagapita, Patricio Roman; Gómez Brizuela, Leissy; Mazzobre, Maria Florencia; Ramirez, Héctor L.; Corti, Horacio Roberto; et al.; β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions; Elsevier; Carbohydrate Polymers; 83; 1; 1-2011; 203-209
0144-8617
CONICET Digital
CONICET
url http://hdl.handle.net/11336/113194
identifier_str_mv Santagapita, Patricio Roman; Gómez Brizuela, Leissy; Mazzobre, Maria Florencia; Ramirez, Héctor L.; Corti, Horacio Roberto; et al.; β-cyclodextrin modifications as related to enzyme stability in dehydrated systems: Supramolecular transitions and molecular interactions; Elsevier; Carbohydrate Polymers; 83; 1; 1-2011; 203-209
0144-8617
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.carbpol.2010.07.041
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0144861710005849
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
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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
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score 12.982451

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