ArticleFoods (Basel, Switzerland)2022
Effect of Malondialdehyde on the Digestibility of Beef Myofibrillar Protein: Potential Mechanisms from Structure to Modification Site.
Article in Foods (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 25 citations in OpenAlex.
- Mechanism of Malondialdehyde-Induced Deterioration in Water-Holding Capacity of Bovine Myofibrillar Proteins: Insights from Structural Modifications and Molecular Docking.Foods (Basel, Switzerland) · 2026Article
- Proteomics unveils chemical modifications on protein side chains in raw breast meat of broilers (Gallus gallus) affected with growth-related myopathies.Animal bioscience · 2025Article
- Rapid Kinetic Fluorogenic Quantification of Malondialdehyde in Ground Beef.Foods (Basel, Switzerland) · 2025Article
- Molecular mechanism of Golden Pomfret myofibrillar protein digestion inhibition by malondialdehyde-mediated oxidation based on peptidomics analysis.Food chemistry: X · 2025Article
- Improving the Edible and Nutritional Quality of Roasted Duck Breasts through Variable Pressure Salting: Implications for Protein Anabolism and Digestion in Rats.Foods (Basel, Switzerland) · 2024Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Lipid oxidation and protein oxidation occur side by side in meat. Here, the effect of malondialdehyde (MDA), the major product of lipid oxidation, on the digestibility of beef myofibrillar proteins (MP) was studied. MP samples were incubated with 0, 0.1, 0.3, 0.5, and 0.7 mM MDA at 4 °C for 12 h and then subjected to in vitro gastrointestinal digestion. The result showed that MDA remarkably reduced the digestibility of MP (p < 0.05). MDA treatments significantly increased carbonyl and Schiff base contents in MP (p < 0.05). The microstructure observed by atomic force microscopy showed that MDA treatments resulted in the aggregation of MP. Non-reducing and reducing electrophoresis suggested the aggregation was mainly caused by covalent bonds including disulfide bond and carbonyl−amine bond. Proteomics analysis proved that the myosin tail was the main target of MDA attack, meanwhile, lysine residues were the major modification sites. Taken together, the above results imply that MDA induces protein oxidation, aggregation, and blockage of hydrolysis sites, consequently leading to the decrease in both gastric and gastrointestinal digestibility of MP.
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