2026-07-29T14:16:12Zhttps://riubu.ubu.es/oai/requestoai:riubu.ubu.es:10259/111512026-03-08T23:42:11Zcom_10259_4244com_10259_5086com_10259_2604com_10259_3596com_10259_5827col_10259_4245col_10259_3597col_10259_5828
Repositorio Institucional de la Universidad de Burgos
author
Cavia Saiz, Mónica
author
Gerardi, Gisela
author
Muñiz Rodríguez, Pilar
author
García Tojal, Javier
author
Salazar Mardones, Gonzalo
2025-12-16T14:03:20Z
2025-12-16T14:03:20Z
2025-06
0308-8146
https://hdl.handle.net/10259/11151
10.1016/j.foodchem.2025.143699
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.
eng
Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Melanoidins
Proteolytic-enzyme
Structure
Antioxidant
Neurotoxicity
New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins
info:eu-repo/semantics/article
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URL
https://riubu.ubu.es/bitstream/10259/11151/1/Cavia-fc_2025.pdf
File
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1139402
application/pdf
Cavia-fc_2025.pdf