Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability

Autores
Chong Cerda, Rocío; Levin, Laura Noemí; Castro Ríos, Rocío; Hernández Luna, Carlos Eduardo; González Horta, Azucena; Gutiérrez Soto, Guadalupe; Chávez Montes, Abelardo
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
One primary drawback of enzyme catalysis at industrial scale is the short-term service life of the enzymes, they lose their activity due to oxidation or other processes which results in less stability and a shorter lifetime thereby rendering them less efficient. An effective way to increase the stability of the enzymes is to attach them to nanoparticles. In this work, the polymer Eudragit® L 100-55 sensitive to pH was used to prepare laccase polymeric nanoparticles by the double-emulsion solvent evaporation approach. The size and morphology of the nanoparticles obtained were evaluated—as well as the encapsulation efficiency and zeta potential. pH effect on activity and stability was compared between free and immobilized laccase. Their stability was also determined in a sequential assay involving acidic pHs up to alkaline ones. The nanoparticles had a spherical shape with a mean size of 147 nm, zeta potential of −22.7 mV at pH 7.0 and load efficiency of 87%. The optimum pH of both free and immobilized laccases was 3.0, being the nanoparticles more stable at acidic pHs. Thus, this would be the first report of obtaining laccase nanoparticles with potential application in animal feed due to the stability conferred to enzymatic activity at pHs similar to those present in the gastrointestinal tract of rabbits, which would allow their potential use in animal feed.
Fil: Chong Cerda, Rocío. Universidad Autonoma de Nuevo Leon.; México
Fil: Levin, Laura Noemí. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Micología y Botánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Micología y Botánica; Argentina
Fil: Castro Ríos, Rocío. Universidad Autonoma de Nuevo Leon.; México
Fil: Hernández Luna, Carlos Eduardo. Universidad Autonoma de Nuevo Leon.; México
Fil: González Horta, Azucena. Universidad Autonoma de Nuevo Leon.; México
Fil: Gutiérrez Soto, Guadalupe. Universidad Autonoma de Nuevo Leon.; México
Fil: Chávez Montes, Abelardo. Universidad Autonoma de Nuevo Leon.; México
Materia
ANIMAL FEED
ENZYME IMMOBILIZATION
LACCASE
TRAMETES MAXIMA CU1
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:11336/211386
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/211386
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stabilityChong Cerda, RocíoLevin, Laura NoemíCastro Ríos, RocíoHernández Luna, Carlos EduardoGonzález Horta, AzucenaGutiérrez Soto, GuadalupeChávez Montes, AbelardoANIMAL FEEDENZYME IMMOBILIZATIONLACCASETRAMETES MAXIMA CU1https://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2One primary drawback of enzyme catalysis at industrial scale is the short-term service life of the enzymes, they lose their activity due to oxidation or other processes which results in less stability and a shorter lifetime thereby rendering them less efficient. An effective way to increase the stability of the enzymes is to attach them to nanoparticles. In this work, the polymer Eudragit® L 100-55 sensitive to pH was used to prepare laccase polymeric nanoparticles by the double-emulsion solvent evaporation approach. The size and morphology of the nanoparticles obtained were evaluated—as well as the encapsulation efficiency and zeta potential. pH effect on activity and stability was compared between free and immobilized laccase. Their stability was also determined in a sequential assay involving acidic pHs up to alkaline ones. The nanoparticles had a spherical shape with a mean size of 147 nm, zeta potential of −22.7 mV at pH 7.0 and load efficiency of 87%. The optimum pH of both free and immobilized laccases was 3.0, being the nanoparticles more stable at acidic pHs. Thus, this would be the first report of obtaining laccase nanoparticles with potential application in animal feed due to the stability conferred to enzymatic activity at pHs similar to those present in the gastrointestinal tract of rabbits, which would allow their potential use in animal feed.Fil: Chong Cerda, Rocío. Universidad Autonoma de Nuevo Leon.; MéxicoFil: Levin, Laura Noemí. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Micología y Botánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Micología y Botánica; ArgentinaFil: Castro Ríos, Rocío. Universidad Autonoma de Nuevo Leon.; MéxicoFil: Hernández Luna, Carlos Eduardo. Universidad Autonoma de Nuevo Leon.; MéxicoFil: González Horta, Azucena. Universidad Autonoma de Nuevo Leon.; MéxicoFil: Gutiérrez Soto, Guadalupe. Universidad Autonoma de Nuevo Leon.; MéxicoFil: Chávez Montes, Abelardo. Universidad Autonoma de Nuevo Leon.; MéxicoMDPI2020-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/211386Chong Cerda, Rocío; Levin, Laura Noemí; Castro Ríos, Rocío; Hernández Luna, Carlos Eduardo; González Horta, Azucena; et al.; Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability; MDPI; Catalysts; 10; 9; 8-2020; 1-112073-4344CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2073-4344/10/9/1085info:eu-repo/semantics/altIdentifier/doi/10.3390/catal10091085info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:05:16Zoai:ri.conicet.gov.ar:11336/211386instacron: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:34982025-10-15 15:05:17.0CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability
title Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability
spellingShingle Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability
Chong Cerda, Rocío
ANIMAL FEED
ENZYME IMMOBILIZATION
LACCASE
TRAMETES MAXIMA CU1
title_short Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability
title_full Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability
title_fullStr Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability
title_full_unstemmed Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability
title_sort Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability
dc.creator.none.fl_str_mv Chong Cerda, Rocío
Levin, Laura Noemí
Castro Ríos, Rocío
Hernández Luna, Carlos Eduardo
González Horta, Azucena
Gutiérrez Soto, Guadalupe
Chávez Montes, Abelardo
author Chong Cerda, Rocío
author_facet Chong Cerda, Rocío
Levin, Laura Noemí
Castro Ríos, Rocío
Hernández Luna, Carlos Eduardo
González Horta, Azucena
Gutiérrez Soto, Guadalupe
Chávez Montes, Abelardo
author_role author
author2 Levin, Laura Noemí
Castro Ríos, Rocío
Hernández Luna, Carlos Eduardo
González Horta, Azucena
Gutiérrez Soto, Guadalupe
Chávez Montes, Abelardo
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv ANIMAL FEED
ENZYME IMMOBILIZATION
LACCASE
TRAMETES MAXIMA CU1
topic ANIMAL FEED
ENZYME IMMOBILIZATION
LACCASE
TRAMETES MAXIMA CU1
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv One primary drawback of enzyme catalysis at industrial scale is the short-term service life of the enzymes, they lose their activity due to oxidation or other processes which results in less stability and a shorter lifetime thereby rendering them less efficient. An effective way to increase the stability of the enzymes is to attach them to nanoparticles. In this work, the polymer Eudragit® L 100-55 sensitive to pH was used to prepare laccase polymeric nanoparticles by the double-emulsion solvent evaporation approach. The size and morphology of the nanoparticles obtained were evaluated—as well as the encapsulation efficiency and zeta potential. pH effect on activity and stability was compared between free and immobilized laccase. Their stability was also determined in a sequential assay involving acidic pHs up to alkaline ones. The nanoparticles had a spherical shape with a mean size of 147 nm, zeta potential of −22.7 mV at pH 7.0 and load efficiency of 87%. The optimum pH of both free and immobilized laccases was 3.0, being the nanoparticles more stable at acidic pHs. Thus, this would be the first report of obtaining laccase nanoparticles with potential application in animal feed due to the stability conferred to enzymatic activity at pHs similar to those present in the gastrointestinal tract of rabbits, which would allow their potential use in animal feed.
Fil: Chong Cerda, Rocío. Universidad Autonoma de Nuevo Leon.; México
Fil: Levin, Laura Noemí. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Micología y Botánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Micología y Botánica; Argentina
Fil: Castro Ríos, Rocío. Universidad Autonoma de Nuevo Leon.; México
Fil: Hernández Luna, Carlos Eduardo. Universidad Autonoma de Nuevo Leon.; México
Fil: González Horta, Azucena. Universidad Autonoma de Nuevo Leon.; México
Fil: Gutiérrez Soto, Guadalupe. Universidad Autonoma de Nuevo Leon.; México
Fil: Chávez Montes, Abelardo. Universidad Autonoma de Nuevo Leon.; México
description One primary drawback of enzyme catalysis at industrial scale is the short-term service life of the enzymes, they lose their activity due to oxidation or other processes which results in less stability and a shorter lifetime thereby rendering them less efficient. An effective way to increase the stability of the enzymes is to attach them to nanoparticles. In this work, the polymer Eudragit® L 100-55 sensitive to pH was used to prepare laccase polymeric nanoparticles by the double-emulsion solvent evaporation approach. The size and morphology of the nanoparticles obtained were evaluated—as well as the encapsulation efficiency and zeta potential. pH effect on activity and stability was compared between free and immobilized laccase. Their stability was also determined in a sequential assay involving acidic pHs up to alkaline ones. The nanoparticles had a spherical shape with a mean size of 147 nm, zeta potential of −22.7 mV at pH 7.0 and load efficiency of 87%. The optimum pH of both free and immobilized laccases was 3.0, being the nanoparticles more stable at acidic pHs. Thus, this would be the first report of obtaining laccase nanoparticles with potential application in animal feed due to the stability conferred to enzymatic activity at pHs similar to those present in the gastrointestinal tract of rabbits, which would allow their potential use in animal feed.
publishDate 2020
dc.date.none.fl_str_mv 2020-08
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/11336/211386
Chong Cerda, Rocío; Levin, Laura Noemí; Castro Ríos, Rocío; Hernández Luna, Carlos Eduardo; González Horta, Azucena; et al.; Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability; MDPI; Catalysts; 10; 9; 8-2020; 1-11
2073-4344
CONICET Digital
CONICET
url http://hdl.handle.net/11336/211386
identifier_str_mv Chong Cerda, Rocío; Levin, Laura Noemí; Castro Ríos, Rocío; Hernández Luna, Carlos Eduardo; González Horta, Azucena; et al.; Nanoencapsulated laccases obtained by double-emulsion technique. Effects on enzyme activity ph-dependence and stability; MDPI; Catalysts; 10; 9; 8-2020; 1-11
2073-4344
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2073-4344/10/9/1085
info:eu-repo/semantics/altIdentifier/doi/10.3390/catal10091085
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
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
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
_version_ 1846083195385151488
score 13.22299

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