Effect of magnetic field modification on oxidative stability of myoglobin in sarcoplasm systems

Jingjiao Jiang; Minquan Xia; Honghong Gong; Jing Ma; Weiqing Sun

doi:10.1016/j.foodchem.2023.137691

Effect of magnetic field modification on oxidative stability of myoglobin in sarcoplasm systems

Food Chem. 2024 Mar 15:436:137691. doi: 10.1016/j.foodchem.2023.137691. Epub 2023 Oct 10.

Authors

Jingjiao Jiang¹, Minquan Xia², Honghong Gong¹, Jing Ma¹, Weiqing Sun³

Affiliations

¹ College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China.
² National Research and Development Centre for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, PR China.
³ College of Life Science, Yangtze University, Jingzhou, Hubei 434023, PR China. Electronic address: sunweiqing@yangtzeu.edu.cn.

PMID: 37837684
DOI: 10.1016/j.foodchem.2023.137691

Abstract

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.

Keywords: Hydroxyl radical; Magnetic field; Myoglobin; Oxidation stability; Sarcoplasmic protein.

MeSH terms

Hydroxyl Radical
Iron
Magnetic Fields
Metmyoglobin / chemistry
Myoglobin* / chemistry
Oxidation-Reduction
Oxidative Stress
Porphyrins*

Substances

Myoglobin
Hydroxyl Radical
Metmyoglobin
Iron
Porphyrins