Effect of magnetic field modification on oxidative stability of myoglobin in sarcoplasm systems.
Hydroxyl radical
Magnetic field
Myoglobin
Oxidation stability
Sarcoplasmic protein
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
15 Mar 2024
15 Mar 2024
Historique:
received:
16
06
2023
revised:
04
10
2023
accepted:
05
10
2023
medline:
3
11
2023
pubmed:
15
10
2023
entrez:
14
10
2023
Statut:
ppublish
Résumé
This study aimed to investigate the effect of magnetic fields (0, 3, 6, 12 mT) on the oxidation characteristics of myoglobin (Mb) in the sarcoplasmic protein (SP) system and to understander the underlying mechanism. The metmyoglobin content, Soret band of heme iron porphyrin, protein conformation and molecular weight distribution were measured in different Mb and SP samples. The results showed that the primary oxidation site of hydroxyl radical on Mb was likely to be the porphyrin ring structure and the side chain group of protein rather than the central iron atoms, what's more, 12 mT magnetic field treatment had an inhibitory effect on the oxidative damage induced by hydroxyl radical.
Identifiants
pubmed: 37837684
pii: S0308-8146(23)02309-9
doi: 10.1016/j.foodchem.2023.137691
pii:
doi:
Substances chimiques
Myoglobin
0
Hydroxyl Radical
3352-57-6
Metmyoglobin
12772-23-5
Iron
E1UOL152H7
Porphyrins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
137691Informations de copyright
Copyright © 2023 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.