Influence of the nature of the support on the catalytic performance of CALB: Experimental and theoretical evidence

The immobilization of the lipase B of Candida antarctica (CALB) was carried out on various hydrophilic and hydrophobic supports through adsorption and covalent bond interactions. The catalytic performance of the biocatalysts was evaluated in the enantioselective esterification of R/S-ibuprofen with...

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Detalles Bibliográficos
Autores principales: José, Carla, Toledo, María Victoria, Nicolás, Paula, Lasalle, Verónica, Ferreira, María Luján, Briand, Laura Estefanía
Formato: Articulo Preprint
Lenguaje:Inglés
Publicado: 2018
Materias:
Ingeniería Química
CALB
Immobilized enzymes
Hydrophobic support
Hydrophilic support
R/s-ibuprofen
Esterification
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/99652
https://ri.conicet.gov.ar/11336/83396
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-99652
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ingeniería Química
CALB
Immobilized enzymes
Hydrophobic support
Hydrophilic support
R/s-ibuprofen
Esterification
spellingShingle Ingeniería Química
CALB
Immobilized enzymes
Hydrophobic support
Hydrophilic support
R/s-ibuprofen
Esterification
José, Carla
Toledo, María Victoria
Nicolás, Paula
Lasalle, Verónica
Ferreira, María Luján
Briand, Laura Estefanía
Influence of the nature of the support on the catalytic performance of CALB: Experimental and theoretical evidence
topic_facet Ingeniería Química
CALB
Immobilized enzymes
Hydrophobic support
Hydrophilic support
R/s-ibuprofen
Esterification
description The immobilization of the lipase B of Candida antarctica (CALB) was carried out on various hydrophilic and hydrophobic supports through adsorption and covalent bond interactions. The catalytic performance of the biocatalysts was evaluated in the enantioselective esterification of R/S-ibuprofen with ethanol without co-solvents added. The present investigation demonstrates that the biocatalysts based on CALB immobilized by adsorption on hydrophobic supports (acrylic resin, polymethylmethacrylate, polystyrene, epoxy resin and polypropylene) exhibit higher conversion of ibuprofen and enantiomeric excess towards the S-enantiomer than CALB immobilized on hydrophilic materials. Additionally, the enzyme loading is a key factor influencing the conversion of the substrate regardless of the nature of the support material. A high enzyme loading is detrimental to the specific activity of the biocatalysts. Experimental and molecular modeling investigations provided evidence for the influence of water activity in the stereospecificity of the lipase.
format Articulo
Preprint
author José, Carla
Toledo, María Victoria
Nicolás, Paula
Lasalle, Verónica
Ferreira, María Luján
Briand, Laura Estefanía
author_facet José, Carla
Toledo, María Victoria
Nicolás, Paula
Lasalle, Verónica
Ferreira, María Luján
Briand, Laura Estefanía
author_sort José, Carla
title Influence of the nature of the support on the catalytic performance of CALB: Experimental and theoretical evidence
title_short Influence of the nature of the support on the catalytic performance of CALB: Experimental and theoretical evidence
title_full Influence of the nature of the support on the catalytic performance of CALB: Experimental and theoretical evidence
title_fullStr Influence of the nature of the support on the catalytic performance of CALB: Experimental and theoretical evidence
title_full_unstemmed Influence of the nature of the support on the catalytic performance of CALB: Experimental and theoretical evidence
title_sort influence of the nature of the support on the catalytic performance of calb: experimental and theoretical evidence
publishDate 2018
url http://sedici.unlp.edu.ar/handle/10915/99652
https://ri.conicet.gov.ar/11336/83396
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