RT info:eu-repo/semantics/article
T1 New approach using alternative proteolytic enzymes to the conventional enzyme pronase for the isolation of bread melanoidins
A1 Cavia Saiz, Mónica
A1 Gerardi, Gisela
A1 Muñiz Rodríguez, Pilar
A1 García Tojal, Javier
A1 Salazar Mardones, Gonzalo
K1 Melanoidins
K1 Proteolytic-enzyme
K1 Structure
K1 Antioxidant
K1 Neurotoxicity
K1 Pan (Alimento)
K1 Bread
K1 Alimentos-Análisis
K1 Food-Analysis
AB 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.
PB Elsevier
SN 0308-8146
YR 2025
FD 2025-06
LK https://hdl.handle.net/10259/11151
UL https://hdl.handle.net/10259/11151
LA eng
NO This research was funded by the Ministry of Science and Innovation, Spanish State Research Agency and European Regional Development Fund (TED201-132195B-I00).
DS Repositorio Institucional de la Universidad de Burgos
RD 22-abr-2026