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

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...

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Published in:Journal of Molecular Catalysis B: Enzymatic
Main Authors: Nicolás, Paula, Lassalle, Verónica Leticia, Ferreira, María Luján
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier Science
Subjects:
Online Access:http://hdl.handle.net/11336/24790
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author Nicolás, Paula
Lassalle, Verónica Leticia
Ferreira, María Luján
author_facet Nicolás, Paula
Lassalle, Verónica Leticia
Ferreira, María Luján
author_sort Nicolás, Paula
collection CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas)
container_start_page 296
container_title Journal of Molecular Catalysis B: Enzymatic
container_volume 122
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. 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. ...
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op_doi https://doi.org/10.1016/j.molcatb.2015.09.013
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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
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spelling ftconicet:oai:ri.conicet.gov.ar:11336/24790 2025-01-16T19:13:13+00:00 About the role of typical spacer/crosslinker on the design of efficient magnetic biocatalysts based on nanosized magnetite Nicolás, Paula Lassalle, Verónica Leticia Ferreira, María Luján application/pdf http://hdl.handle.net/11336/24790 eng eng Elsevier Science 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 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 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ Enzyme Immobilization Calb Magnetic Support Biocatalysis https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1016/j.molcatb.2015.09.013 2023-09-24T19:18:36Z 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. ... Article in Journal/Newspaper Antarc* Antarctica CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Journal of Molecular Catalysis B: Enzymatic 122 296 304
spellingShingle Enzyme Immobilization
Calb
Magnetic Support
Biocatalysis
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
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
title 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_short 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
topic Enzyme Immobilization
Calb
Magnetic Support
Biocatalysis
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
topic_facet Enzyme Immobilization
Calb
Magnetic Support
Biocatalysis
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
url http://hdl.handle.net/11336/24790