New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins

Bread melanoidins are melanoproteins classically extracted with the proteolytic enzyme pronase E (S. griserus). In this study, the structure and functionality of melanoidins extracted with the proteolytic enzymes papain (PE) and enzymes from B. subtillus (SP) and a mixture from B. subtillus and A. o...

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Detalhes bibliográficos
Autores: Cavia Saiz, Mónica, Gerardi, Gisela, Muñiz Rodríguez, Pilar, García Tojal, Javier, Salazar Mardones, Gonzalo
Tipo de documento: artigo
Estado:Versión aceptada para publicación
Data de publicação:2025
País:España
Recursos:Universidad de Burgos (UBU)
Repositório:Repositorio Institucional de la Universidad de Burgos (RIUBU)
OAI Identifier:oai:riubu.ubu.es:10259/11151
Acesso em linha:https://hdl.handle.net/10259/11151
Access Level:Acceso aberto
Palavra-chave:Melanoidins
Proteolytic-enzyme
Structure
Antioxidant
Neurotoxicity
Pan (Alimento)
Alimentos-Análisis
Bread
Food-Analysis
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spelling New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidinsCavia Saiz, MónicaGerardi, GiselaMuñiz Rodríguez, PilarGarcía Tojal, JavierSalazar Mardones, GonzaloMelanoidinsProteolytic-enzymeStructureAntioxidantNeurotoxicityPan (Alimento)Alimentos-AnálisisBreadFood-AnalysisBread melanoidins are melanoproteins classically extracted with the proteolytic enzyme pronase E (S. griserus). In this study, the structure and functionality of melanoidins extracted with the proteolytic enzymes papain (PE) and enzymes from B. subtillus (SP) and a mixture from B. subtillus and A. oryzae (MP) were evaluated. PE extracted melanoidins have the highest nitrogen (4.3 %) and protein (29 %) content. FTIR showed that PE had a higher protein content and pronase had higher in carbohydrates. The K420 and K345 values and antioxidant capacities of the PE extract were similar to pronase and higher than the other microbial enzymes. After in vitro digestion, the increased in the antioxidant capacity was most pronounced in the PE extract. No neurotoxicity was observed, as evidenced by no neuronal cell death or changes in neuronal ROS levels. These results indicate that the PE enzyme may be a good alternative to pronase for extraction of melanoidins.This research was funded by the Ministry of Science and Innovation, Spanish State Research Agency and European Regional Development Fund (TED201-132195B-I00).Elsevier202520252025info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttps://hdl.handle.net/10259/11151reponame:Repositorio Institucional de la Universidad de Burgos (RIUBU)instname:Universidad de Burgos (UBU)InglésFood Chemistry. 2025, V. 478, 143699https://doi.org/10.1016/j.foodchem.2025.143699info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica, Técnica y de Innovación 2021-2023/TED2021-132195B-I00Attribution-NonCommercial-NoDerivatives 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:riubu.ubu.es:10259/111512026-05-28T07:56:11Z
dc.title.none.fl_str_mv New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins
title New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins
spellingShingle New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins
Cavia Saiz, Mónica
Melanoidins
Proteolytic-enzyme
Structure
Antioxidant
Neurotoxicity
Pan (Alimento)
Alimentos-Análisis
Bread
Food-Analysis
title_short New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins
title_full New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins
title_fullStr New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins
title_full_unstemmed New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins
title_sort New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins
dc.creator.none.fl_str_mv Cavia Saiz, Mónica
Gerardi, Gisela
Muñiz Rodríguez, Pilar
García Tojal, Javier
Salazar Mardones, Gonzalo
author Cavia Saiz, Mónica
author_facet Cavia Saiz, Mónica
Gerardi, Gisela
Muñiz Rodríguez, Pilar
García Tojal, Javier
Salazar Mardones, Gonzalo
author_role author
author2 Gerardi, Gisela
Muñiz Rodríguez, Pilar
García Tojal, Javier
Salazar Mardones, Gonzalo
author2_role author
author
author
author
dc.subject.none.fl_str_mv Melanoidins
Proteolytic-enzyme
Structure
Antioxidant
Neurotoxicity
Pan (Alimento)
Alimentos-Análisis
Bread
Food-Analysis
topic Melanoidins
Proteolytic-enzyme
Structure
Antioxidant
Neurotoxicity
Pan (Alimento)
Alimentos-Análisis
Bread
Food-Analysis
description Bread melanoidins are melanoproteins classically extracted with the proteolytic enzyme pronase E (S. griserus). In this study, the structure and functionality of melanoidins extracted with the proteolytic enzymes papain (PE) and enzymes from B. subtillus (SP) and a mixture from B. subtillus and A. oryzae (MP) were evaluated. PE extracted melanoidins have the highest nitrogen (4.3 %) and protein (29 %) content. FTIR showed that PE had a higher protein content and pronase had higher in carbohydrates. The K420 and K345 values and antioxidant capacities of the PE extract were similar to pronase and higher than the other microbial enzymes. After in vitro digestion, the increased in the antioxidant capacity was most pronounced in the PE extract. No neurotoxicity was observed, as evidenced by no neuronal cell death or changes in neuronal ROS levels. These results indicate that the PE enzyme may be a good alternative to pronase for extraction of melanoidins.
publishDate 2025
dc.date.none.fl_str_mv 2025
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/10259/11151
url https://hdl.handle.net/10259/11151
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Food Chemistry. 2025, V. 478, 143699
https://doi.org/10.1016/j.foodchem.2025.143699
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica, Técnica y de Innovación 2021-2023/TED2021-132195B-I00
dc.rights.none.fl_str_mv Attribution-NonCommercial-NoDerivatives 4.0 Internacional
http://creativecommons.org/licenses/by-nc-nd/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv 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.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositorio Institucional de la Universidad de Burgos (RIUBU)
instname:Universidad de Burgos (UBU)
instname_str Universidad de Burgos (UBU)
reponame_str Repositorio Institucional de la Universidad de Burgos (RIUBU)
collection Repositorio Institucional de la Universidad de Burgos (RIUBU)
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.811543

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