Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactose

Thermostable β-galactosidase (TmLac) has been immobilized as hybrid inorganic-protein nanoflowers using salts of Cu2+, Mn2+, Zn2+, Co2+ and Ca2+ as the inorganic component. The incorporation efficiency of enzyme into the nanoflowers was higher than 95% for a protein concentration of 0.05 mg/mL. The...

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Detalhes bibliográficos
Autores: Talens Perales, David, Fabra, María José, Martínez Argente, Luis, Marín Navarro, Julia, Polaina, Julio
Tipo de documento: artigo
Data de publicação:2020
País:España
Recursos:Universidad Católica de Valencia San Vicente Mártir
Repositório:RIUCV. Repositorio de la Universidad Católica de Valencia San Vicente Mártir
Idioma:inglês
OAI Identifier:oai:riucv.ucv.es:20.500.12466/3778
Acesso em linha:http://hdl.handle.net/20.500.12466/3778
Access Level:Acceso aberto
Palavra-chave:β-Galactosidase
Enzyme immobilization
Lactose intolerance
Milk products
2302 Bioquímica
2302.90 Bioquímica de Alimentos
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oai_identifier_str oai:riucv.ucv.es:20.500.12466/3778
network_acronym_str ES
network_name_str España
repository_id_str
spelling Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactoseTalens Perales, DavidFabra, María JoséMartínez Argente, LuisMarín Navarro, JuliaPolaina, Julioβ-GalactosidaseEnzyme immobilizationLactose intoleranceMilk products2302 Bioquímica2302.90 Bioquímica de AlimentosThermostable β-galactosidase (TmLac) has been immobilized as hybrid inorganic-protein nanoflowers using salts of Cu2+, Mn2+, Zn2+, Co2+ and Ca2+ as the inorganic component. The incorporation efficiency of enzyme into the nanoflowers was higher than 95% for a protein concentration of 0.05 mg/mL. The structure, activity and recyclability of the nanoflowers with different chemical composition were analyzed. Ca2+, Mn2+ and Co2+ nanoflowers showed a level of lactase activity equivalent to their same content of free enzyme. Cu2+nanoflowers showed only marginal enzyme activity in agreement with the inhibitory effect of this cation on the enzyme. TmLac nanoflowers provide an efficient methodology for enzyme immobilization and recyclability. TmLac-Ca2+ nanoflowers presented the best properties for lactose hydrolysis both in buffered and in milk, and could be reused in five consecutive cycles.20242024-01-2320202020-05-1520202020-05-15journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/20.500.12466/3778reponame: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:20.500.12466/37782026-06-19T08:32:07Z
dc.title.none.fl_str_mv Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactose
title Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactose
spellingShingle Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactose
Talens Perales, David
β-Galactosidase
Enzyme immobilization
Lactose intolerance
Milk products
2302 Bioquímica
2302.90 Bioquímica de Alimentos
title_short Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactose
title_full Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactose
title_fullStr Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactose
title_full_unstemmed Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactose
title_sort Recyclable thermophilic hybrid protein-inorganic nanoflowers for the hydrolysis of milk lactose
dc.creator.none.fl_str_mv Talens Perales, David
Fabra, María José
Martínez Argente, Luis
Marín Navarro, Julia
Polaina, Julio
author Talens Perales, David
author_facet Talens Perales, David
Fabra, María José
Martínez Argente, Luis
Marín Navarro, Julia
Polaina, Julio
author_role author
author2 Fabra, María José
Martínez Argente, Luis
Marín Navarro, Julia
Polaina, Julio
author2_role author
author
author
author
dc.contributor.none.fl_str_mv
dc.subject.none.fl_str_mv β-Galactosidase
Enzyme immobilization
Lactose intolerance
Milk products
2302 Bioquímica
2302.90 Bioquímica de Alimentos
topic β-Galactosidase
Enzyme immobilization
Lactose intolerance
Milk products
2302 Bioquímica
2302.90 Bioquímica de Alimentos
description Thermostable β-galactosidase (TmLac) has been immobilized as hybrid inorganic-protein nanoflowers using salts of Cu2+, Mn2+, Zn2+, Co2+ and Ca2+ as the inorganic component. The incorporation efficiency of enzyme into the nanoflowers was higher than 95% for a protein concentration of 0.05 mg/mL. The structure, activity and recyclability of the nanoflowers with different chemical composition were analyzed. Ca2+, Mn2+ and Co2+ nanoflowers showed a level of lactase activity equivalent to their same content of free enzyme. Cu2+nanoflowers showed only marginal enzyme activity in agreement with the inhibitory effect of this cation on the enzyme. TmLac nanoflowers provide an efficient methodology for enzyme immobilization and recyclability. TmLac-Ca2+ nanoflowers presented the best properties for lactose hydrolysis both in buffered and in milk, and could be reused in five consecutive cycles.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020-05-15
2020
2020-05-15
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/20.500.12466/3778
url http://hdl.handle.net/20.500.12466/3778
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
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score 15,300724

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