About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite

Autores
Nicolás, Paula; Lassalle, Verónica Leticia; Ferreira, María Luján
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The immobilization of Candida antarctica lipase B (CALB) was carried out using glutaraldehyde (GLUT) and/or 3-aminopropyl-triethoxisilane (APTS). The aim of this work was to elucidate the role of these crosslinkers/functionalizers on the efficiency of the prepared nanosized catalysts in solvent-free oleic acid esterification.A series of biocatalysts were prepared in presence or absence of GLUT and APTS. The impact of the amount of initial CALB was also explored. An experimental design was utilized to study the variables that maximize biocatalyst activity.A strong dependence of enzymatic activity with the nominal amount of GLUT as well as the final protein/CALB loading was found. Nominal quantity of APTS did not affect catalyst́s activity when used in combination with GLUT. Additional studies demonstrated that stability during storage was mainly dependent on the enzyme loading. The optimum biocatalyst was reused 6 cycles without mass loss. Biocatalyst́s performance decreased with reuse. Mechanisms justifying these results were proposed.The role of GLUT and APTS on stability during storage and on differences between initial enzymatic activity and the performance in the reaction after two months was discussed. The problem of mixed interaction of CALB (covalent bonding plus simple adsorption) was carefully addressed to explain leaching of the lipaseLeaching and stability on storage should be included in the analysis of modifiers impact when support́s modifiers are used. The fresh and stored biocatalyst enzymatic activity has to be addressed looking at the practical aspects of implementation in technological settings.
Fil: Nicolás, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Lassalle, Verónica Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Materia
Enzyme Immobilization
Calb
Magnetic Support
Biocatalysis
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:11336/24790
Acceder
id CONICETDig_05603d7fa9010195853494e17d3a62a7
oai_identifier_str oai:ri.conicet.gov.ar:11336/24790
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetiteNicolás, PaulaLassalle, Verónica LeticiaFerreira, María LujánEnzyme ImmobilizationCalbMagnetic SupportBiocatalysishttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2The immobilization of Candida antarctica lipase B (CALB) was carried out using glutaraldehyde (GLUT) and/or 3-aminopropyl-triethoxisilane (APTS). The aim of this work was to elucidate the role of these crosslinkers/functionalizers on the efficiency of the prepared nanosized catalysts in solvent-free oleic acid esterification.A series of biocatalysts were prepared in presence or absence of GLUT and APTS. The impact of the amount of initial CALB was also explored. An experimental design was utilized to study the variables that maximize biocatalyst activity.A strong dependence of enzymatic activity with the nominal amount of GLUT as well as the final protein/CALB loading was found. Nominal quantity of APTS did not affect catalyst́s activity when used in combination with GLUT. Additional studies demonstrated that stability during storage was mainly dependent on the enzyme loading. The optimum biocatalyst was reused 6 cycles without mass loss. Biocatalyst́s performance decreased with reuse. Mechanisms justifying these results were proposed.The role of GLUT and APTS on stability during storage and on differences between initial enzymatic activity and the performance in the reaction after two months was discussed. The problem of mixed interaction of CALB (covalent bonding plus simple adsorption) was carefully addressed to explain leaching of the lipaseLeaching and stability on storage should be included in the analysis of modifiers impact when support́s modifiers are used. The fresh and stored biocatalyst enzymatic activity has to be addressed looking at the practical aspects of implementation in technological settings.Fil: Nicolás, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaFil: Lassalle, Verónica Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; ArgentinaFil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaElsevier Science2015-10-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/24790Nicolás, Paula; Lassalle, Verónica Leticia; Ferreira, María Luján; About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite; Elsevier Science; Journal Of Molecular Catalysis B: Enzymatic; 122; 8-10-2015; 296-3041381-1177CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1381117715300746info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2015.09.013info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:11:33Zoai:ri.conicet.gov.ar:11336/24790instacron: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:34982025-09-10 13:11:33.628CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite
title About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite
spellingShingle About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite
Nicolás, Paula
Enzyme Immobilization
Calb
Magnetic Support
Biocatalysis
title_short About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite
title_full About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite
title_fullStr About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite
title_full_unstemmed About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite
title_sort About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite
dc.creator.none.fl_str_mv Nicolás, Paula
Lassalle, Verónica Leticia
Ferreira, María Luján
author Nicolás, Paula
author_facet Nicolás, Paula
Lassalle, Verónica Leticia
Ferreira, María Luján
author_role author
author2 Lassalle, Verónica Leticia
Ferreira, María Luján
author2_role author
author
dc.subject.none.fl_str_mv Enzyme Immobilization
Calb
Magnetic Support
Biocatalysis
topic Enzyme Immobilization
Calb
Magnetic Support
Biocatalysis
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The immobilization of Candida antarctica lipase B (CALB) was carried out using glutaraldehyde (GLUT) and/or 3-aminopropyl-triethoxisilane (APTS). The aim of this work was to elucidate the role of these crosslinkers/functionalizers on the efficiency of the prepared nanosized catalysts in solvent-free oleic acid esterification.A series of biocatalysts were prepared in presence or absence of GLUT and APTS. The impact of the amount of initial CALB was also explored. An experimental design was utilized to study the variables that maximize biocatalyst activity.A strong dependence of enzymatic activity with the nominal amount of GLUT as well as the final protein/CALB loading was found. Nominal quantity of APTS did not affect catalyst́s activity when used in combination with GLUT. Additional studies demonstrated that stability during storage was mainly dependent on the enzyme loading. The optimum biocatalyst was reused 6 cycles without mass loss. Biocatalyst́s performance decreased with reuse. Mechanisms justifying these results were proposed.The role of GLUT and APTS on stability during storage and on differences between initial enzymatic activity and the performance in the reaction after two months was discussed. The problem of mixed interaction of CALB (covalent bonding plus simple adsorption) was carefully addressed to explain leaching of the lipaseLeaching and stability on storage should be included in the analysis of modifiers impact when support́s modifiers are used. The fresh and stored biocatalyst enzymatic activity has to be addressed looking at the practical aspects of implementation in technological settings.
Fil: Nicolás, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Lassalle, Verónica Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
description The immobilization of Candida antarctica lipase B (CALB) was carried out using glutaraldehyde (GLUT) and/or 3-aminopropyl-triethoxisilane (APTS). The aim of this work was to elucidate the role of these crosslinkers/functionalizers on the efficiency of the prepared nanosized catalysts in solvent-free oleic acid esterification.A series of biocatalysts were prepared in presence or absence of GLUT and APTS. The impact of the amount of initial CALB was also explored. An experimental design was utilized to study the variables that maximize biocatalyst activity.A strong dependence of enzymatic activity with the nominal amount of GLUT as well as the final protein/CALB loading was found. Nominal quantity of APTS did not affect catalyst́s activity when used in combination with GLUT. Additional studies demonstrated that stability during storage was mainly dependent on the enzyme loading. The optimum biocatalyst was reused 6 cycles without mass loss. Biocatalyst́s performance decreased with reuse. Mechanisms justifying these results were proposed.The role of GLUT and APTS on stability during storage and on differences between initial enzymatic activity and the performance in the reaction after two months was discussed. The problem of mixed interaction of CALB (covalent bonding plus simple adsorption) was carefully addressed to explain leaching of the lipaseLeaching and stability on storage should be included in the analysis of modifiers impact when support́s modifiers are used. The fresh and stored biocatalyst enzymatic activity has to be addressed looking at the practical aspects of implementation in technological settings.
publishDate 2015
dc.date.none.fl_str_mv 2015-10-08
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/11336/24790
Nicolás, Paula; Lassalle, Verónica Leticia; Ferreira, María Luján; About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite; Elsevier Science; Journal Of Molecular Catalysis B: Enzymatic; 122; 8-10-2015; 296-304
1381-1177
CONICET Digital
CONICET
url http://hdl.handle.net/11336/24790
identifier_str_mv Nicolás, Paula; Lassalle, Verónica Leticia; Ferreira, María Luján; About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite; Elsevier Science; Journal Of Molecular Catalysis B: Enzymatic; 122; 8-10-2015; 296-304
1381-1177
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1381117715300746
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2015.09.013
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
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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 12.993085

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