Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability

This report describes an efficient procedure for enzyme encapsulation and its application for the hydrolysis of lactose. The enzymatic material that has been developed consists of hydrogel particles (ca. 3–4 mm of diameter) composed of either alginate or an alginate-agarose combination, in which bac...

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Detalles Bibliográficos
Autores: Fabra, María José, Pérez Bassart, Zaida, Talens Perales, David, Martínez Sanz, Marta, López Rubio, Amparo, Marín Navarro, Julia, Polaina, Julio
Tipo de recurso: artículo
Fecha de publicación:2019
País:España
Institución:Universidad Católica de Valencia San Vicente Mártir
Repositorio:RIUCV. Repositorio de la Universidad Católica de Valencia San Vicente Mártir
Idioma:inglés
OAI Identifier:oai:riucv.ucv.es:20.500.12466/3787
Acceso en línea:http://hdl.handle.net/20.500.12466/3787
Access Level:acceso abierto
Palabra clave:Galactosidase
Cell permeabilization
Enzyme immobilization
Lactose
Thermostable enzyme
2302 Bioquímica
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spelling Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capabilityFabra, María JoséPérez Bassart, ZaidaTalens Perales, DavidMartínez Sanz, MartaLópez Rubio, AmparoMarín Navarro, JuliaPolaina, JulioGalactosidaseCell permeabilizationEnzyme immobilizationLactoseThermostable enzyme2302 BioquímicaThis report describes an efficient procedure for enzyme encapsulation and its application for the hydrolysis of lactose. The enzymatic material that has been developed consists of hydrogel particles (ca. 3–4 mm of diameter) composed of either alginate or an alginate-agarose combination, in which bacterial cells loaded with a thermostable β-galactosidase are embedded. The cells were rendered fully permeable to the substrate, either chromogenic p-nitrophenyl galactose or lactose, by thermal treatment at 75 °C. Hydrogel particles made of a mixture of alginate and agarose displayed high catalytic activity (i.e. 1 g of beads hydrolyze the lactose equivalent of 100 mL of milk in 15 min) and thermal stability: they could be reused at 75 °C for complete hydrolysis of 5% (w/v) lactose solution at least six consecutive times without significant loss of activity.20242024-01-2320192019-11-0120192019-11-01journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/20.500.12466/3787reponame:RIUCV. Repositorio de la Universidad Católica de Valencia San Vicente Mártirinstname:Universidad Católica de Valencia San Vicente MártirInglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:riucv.ucv.es:20.500.12466/37872026-06-19T08:32:07Z
dc.title.none.fl_str_mv Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability
title Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability
spellingShingle Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability
Fabra, María José
Galactosidase
Cell permeabilization
Enzyme immobilization
Lactose
Thermostable enzyme
2302 Bioquímica
title_short Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability
title_full Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability
title_fullStr Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability
title_full_unstemmed Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability
title_sort Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability
dc.creator.none.fl_str_mv Fabra, María José
Pérez Bassart, Zaida
Talens Perales, David
Martínez Sanz, Marta
López Rubio, Amparo
Marín Navarro, Julia
Polaina, Julio
author Fabra, María José
author_facet Fabra, María José
Pérez Bassart, Zaida
Talens Perales, David
Martínez Sanz, Marta
López Rubio, Amparo
Marín Navarro, Julia
Polaina, Julio
author_role author
author2 Pérez Bassart, Zaida
Talens Perales, David
Martínez Sanz, Marta
López Rubio, Amparo
Marín Navarro, Julia
Polaina, Julio
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv
dc.subject.none.fl_str_mv Galactosidase
Cell permeabilization
Enzyme immobilization
Lactose
Thermostable enzyme
2302 Bioquímica
topic Galactosidase
Cell permeabilization
Enzyme immobilization
Lactose
Thermostable enzyme
2302 Bioquímica
description This report describes an efficient procedure for enzyme encapsulation and its application for the hydrolysis of lactose. The enzymatic material that has been developed consists of hydrogel particles (ca. 3–4 mm of diameter) composed of either alginate or an alginate-agarose combination, in which bacterial cells loaded with a thermostable β-galactosidase are embedded. The cells were rendered fully permeable to the substrate, either chromogenic p-nitrophenyl galactose or lactose, by thermal treatment at 75 °C. Hydrogel particles made of a mixture of alginate and agarose displayed high catalytic activity (i.e. 1 g of beads hydrolyze the lactose equivalent of 100 mL of milk in 15 min) and thermal stability: they could be reused at 75 °C for complete hydrolysis of 5% (w/v) lactose solution at least six consecutive times without significant loss of activity.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-11-01
2019
2019-11-01
2024
2024-01-23
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12466/3787
url http://hdl.handle.net/20.500.12466/3787
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 Internacional
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 Internacional
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:RIUCV. Repositorio de la Universidad Católica de Valencia San Vicente Mártir
instname:Universidad Católica de Valencia San Vicente Mártir
instname_str Universidad Católica de Valencia San Vicente Mártir
reponame_str RIUCV. Repositorio de la Universidad Católica de Valencia San Vicente Mártir
collection RIUCV. Repositorio de la Universidad Católica de Valencia San Vicente Mártir
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869407646209015808
score 15,300724

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