Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste

Autores
Llerena Suster, Carlos Rafael; Fuentes, Cynthia Analía; Sambeth, Jorge Enrique; José, Carla
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The adsorption of the lipase B from Candida antarctica (CALB) over polyethylene terephthalate (PET), polypropylene (PP), and derivatives, abundant components of urban solid waste (USW),was investigated. The characterization of the supports and biocatalysts synthesized by SEM-EDS and FTIR is presented. Two immobilization strategies were evaluated, conventional and total adsorption. The adsorbed protein was determined by Bradford and through high-resolution inductively coupled plasma atomic emission spectroscopy (ICP-AES). In this sense, the adsorption of CALB in all the proposed supports was evidenced, obtaining the highest protein loads in bis-(2-hydroxyethyl) terephthalate (BHET). Subsequently, the biocatalysts were applied to the esterification of rac-ibuprofen with ethanol. CALB immobilized in BHET showed remarkable activity, achieving conversions of 30%. In this context, immobilization on this support was optimized, studying the addition of sorbitol-glycerol. Thus, in the presence of 0.91 g of polyols, a catalyst with a protein load of 33.3 mg·g−1 was obtained, achieving productivity of 0.298 mmol min−1 mg−1 . Additionally, no differences were found when using BHET from USW bottles of various colors. This research shows the potential of materials derived from PET as enzymatic supports, unreported materials, that we can use as tools to achieve sustainable biotechnological applications.
Centro de Investigación y Desarrollo en Ciencias Aplicadas
Centro de Investigación de Proteínas Vegetales
Materia
Química
Biocatálisis
Enzimas
Polietilentereftalato
Polipropileno
Bis(2-hidroxietil)tereftalato
Química verde
Profenos
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/159933

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oai_identifier_str oai:sedici.unlp.edu.ar:10915/159933
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Immobilization of the Lipase B from Candida antarctica on Urban Solid WasteLlerena Suster, Carlos RafaelFuentes, Cynthia AnalíaSambeth, Jorge EnriqueJosé, CarlaQuímicaBiocatálisisEnzimasPolietilentereftalatoPolipropilenoBis(2-hidroxietil)tereftalatoQuímica verdeProfenosThe adsorption of the lipase B from Candida antarctica (CALB) over polyethylene terephthalate (PET), polypropylene (PP), and derivatives, abundant components of urban solid waste (USW),was investigated. The characterization of the supports and biocatalysts synthesized by SEM-EDS and FTIR is presented. Two immobilization strategies were evaluated, conventional and total adsorption. The adsorbed protein was determined by Bradford and through high-resolution inductively coupled plasma atomic emission spectroscopy (ICP-AES). In this sense, the adsorption of CALB in all the proposed supports was evidenced, obtaining the highest protein loads in bis-(2-hydroxyethyl) terephthalate (BHET). Subsequently, the biocatalysts were applied to the esterification of rac-ibuprofen with ethanol. CALB immobilized in BHET showed remarkable activity, achieving conversions of 30%. In this context, immobilization on this support was optimized, studying the addition of sorbitol-glycerol. Thus, in the presence of 0.91 g of polyols, a catalyst with a protein load of 33.3 mg·g−1 was obtained, achieving productivity of 0.298 mmol min−1 mg−1 . Additionally, no differences were found when using BHET from USW bottles of various colors. This research shows the potential of materials derived from PET as enzymatic supports, unreported materials, that we can use as tools to achieve sustainable biotechnological applications.Centro de Investigación y Desarrollo en Ciencias AplicadasCentro de Investigación de Proteínas Vegetales2023-09-26info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/159933enginfo:eu-repo/semantics/altIdentifier/issn/2073-4344info:eu-repo/semantics/altIdentifier/doi/10.3390/catal13101324info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-17T10:24:31Zoai:sedici.unlp.edu.ar:10915/159933Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-17 10:24:32.089SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste
title Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste
spellingShingle Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste
Llerena Suster, Carlos Rafael
Química
Biocatálisis
Enzimas
Polietilentereftalato
Polipropileno
Bis(2-hidroxietil)tereftalato
Química verde
Profenos
title_short Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste
title_full Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste
title_fullStr Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste
title_full_unstemmed Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste
title_sort Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste
dc.creator.none.fl_str_mv Llerena Suster, Carlos Rafael
Fuentes, Cynthia Analía
Sambeth, Jorge Enrique
José, Carla
author Llerena Suster, Carlos Rafael
author_facet Llerena Suster, Carlos Rafael
Fuentes, Cynthia Analía
Sambeth, Jorge Enrique
José, Carla
author_role author
author2 Fuentes, Cynthia Analía
Sambeth, Jorge Enrique
José, Carla
author2_role author
author
author
dc.subject.none.fl_str_mv Química
Biocatálisis
Enzimas
Polietilentereftalato
Polipropileno
Bis(2-hidroxietil)tereftalato
Química verde
Profenos
topic Química
Biocatálisis
Enzimas
Polietilentereftalato
Polipropileno
Bis(2-hidroxietil)tereftalato
Química verde
Profenos
dc.description.none.fl_txt_mv The adsorption of the lipase B from Candida antarctica (CALB) over polyethylene terephthalate (PET), polypropylene (PP), and derivatives, abundant components of urban solid waste (USW),was investigated. The characterization of the supports and biocatalysts synthesized by SEM-EDS and FTIR is presented. Two immobilization strategies were evaluated, conventional and total adsorption. The adsorbed protein was determined by Bradford and through high-resolution inductively coupled plasma atomic emission spectroscopy (ICP-AES). In this sense, the adsorption of CALB in all the proposed supports was evidenced, obtaining the highest protein loads in bis-(2-hydroxyethyl) terephthalate (BHET). Subsequently, the biocatalysts were applied to the esterification of rac-ibuprofen with ethanol. CALB immobilized in BHET showed remarkable activity, achieving conversions of 30%. In this context, immobilization on this support was optimized, studying the addition of sorbitol-glycerol. Thus, in the presence of 0.91 g of polyols, a catalyst with a protein load of 33.3 mg·g−1 was obtained, achieving productivity of 0.298 mmol min−1 mg−1 . Additionally, no differences were found when using BHET from USW bottles of various colors. This research shows the potential of materials derived from PET as enzymatic supports, unreported materials, that we can use as tools to achieve sustainable biotechnological applications.
Centro de Investigación y Desarrollo en Ciencias Aplicadas
Centro de Investigación de Proteínas Vegetales
description The adsorption of the lipase B from Candida antarctica (CALB) over polyethylene terephthalate (PET), polypropylene (PP), and derivatives, abundant components of urban solid waste (USW),was investigated. The characterization of the supports and biocatalysts synthesized by SEM-EDS and FTIR is presented. Two immobilization strategies were evaluated, conventional and total adsorption. The adsorbed protein was determined by Bradford and through high-resolution inductively coupled plasma atomic emission spectroscopy (ICP-AES). In this sense, the adsorption of CALB in all the proposed supports was evidenced, obtaining the highest protein loads in bis-(2-hydroxyethyl) terephthalate (BHET). Subsequently, the biocatalysts were applied to the esterification of rac-ibuprofen with ethanol. CALB immobilized in BHET showed remarkable activity, achieving conversions of 30%. In this context, immobilization on this support was optimized, studying the addition of sorbitol-glycerol. Thus, in the presence of 0.91 g of polyols, a catalyst with a protein load of 33.3 mg·g−1 was obtained, achieving productivity of 0.298 mmol min−1 mg−1 . Additionally, no differences were found when using BHET from USW bottles of various colors. This research shows the potential of materials derived from PET as enzymatic supports, unreported materials, that we can use as tools to achieve sustainable biotechnological applications.
publishDate 2023
dc.date.none.fl_str_mv 2023-09-26
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
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format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/159933
url http://sedici.unlp.edu.ar/handle/10915/159933
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/2073-4344
info:eu-repo/semantics/altIdentifier/doi/10.3390/catal13101324
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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