ArticleFood chemistry: X2025
Elucidating the degradation mechanism of beef myofibrillar proteins under hydroxyl radical oxidation through the lens of cysteine oxidation modifications.
Article in Food chemistry: X, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Analysis of lipid-protein interactive oxidation and underlying pathways in aquatic products via multi-omics and machine learning: a case study of air-dried hairtail.Food chemistry: X · 2026Article
- Interaction Mechanism of Bovine Myosin Oxidation Inhibition by Epicatechin Gallate: Insights from Molecular Docking and Thermodynamic Analysis.Foods (Basel, Switzerland) · 2026Article
- Mechanism of Malondialdehyde-Induced Deterioration in Water-Holding Capacity of Bovine Myofibrillar Proteins: Insights from Structural Modifications and Molecular Docking.Foods (Basel, Switzerland) · 2026Article
- Effects of supercooling, sub-freezing, and deep-freezing pre-cooling on color, pH, shear force, sensory quality, and myofibrillar protein properties of beef during expanded polystyrene-based distribution.Food science of animal resources · 2026Article
- Effect of protein oxidation on the quality of abalone (Food chemistry: X · 2025Article
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Authors and funding
9 authors.
Funding
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Abstract
The study aimed to assess the oxidative modification behavior of bovine myofibrillar proteins (MPs) cysteines (Cys) by hydroxyl radical (·OH) through the construction of an in vitr Fenton reaction system. The ·OH generated by the Fenton reaction induced large-scale oxidative modification of Cys, and redox proteomics identified a total of 1192 differential oxidation sites (Dos), 59 Dos were located in the MPs structure. The Cys of actin (17 Dos), myosin/myomesin (16 Dos), tenascin (12 Dos) and sarcomere (10 Dos) in the MPs structure showed active oxidative modification behavior towards ·OH, especially with the "-C-X-X-X-X-W-" structure amino acid sequence showed high sensitivity. Notably, the oxidative modification of Cys by ·OH was an irreversible process, as evidenced mainly by a significant decrease (
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