Related Experiment Video
Updated: Sep 3, 2025

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
Published on: April 26, 2024
Effect of Malondialdehyde on the Digestibility of Beef Myofibrillar Protein: Potential Mechanisms from Structure to
Yantao Yin1, Lei Zhou1, Jiaming Cai1
1Key Laboratory of Meat Processing and Quality Control, Ministry of Education China, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
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.
Insights
Malondialdehyde (MDA), a lipid oxidation product, significantly reduces beef myofibrillar protein (MP) digestibility. MDA causes protein oxidation and aggregation, blocking hydrolysis sites and decreasing digestibility.
Area of Science:
- Food Science
- Protein Chemistry
- Oxidative Stress
Background:
- Lipid oxidation and protein oxidation are concurrent processes in meat.
- Malondialdehyde (MDA) is a primary biomarker and product of lipid oxidation.
Purpose of the Study:
- To investigate the impact of malondialdehyde (MDA) on the in vitro digestibility of beef myofibrillar proteins (MP).
Main Methods:
- Incubation of MP with varying concentrations of MDA.
- In vitro gastrointestinal digestion assays.
- Analysis of protein carbonyl and Schiff base content.
- Atomic force microscopy for microstructure analysis.
- Electrophoresis (reducing and non-reducing) and proteomics for structural and modification analysis.
Main Results:
- MDA significantly decreased MP digestibility (p < 0.05).
- MDA treatment increased protein carbonyl and Schiff base content.
- MDA induced MP aggregation via covalent bonds (disulfide, carbonyl-amine).
- Myosin tail was identified as a primary MDA target, with lysine residues being major modification sites.
Conclusions:
- MDA induces oxidative damage and aggregation in beef MP.
- Protein aggregation and modification by MDA block enzymatic hydrolysis sites.
- This leads to reduced gastric and gastrointestinal digestibility of beef proteins.
More Related Videos
07:46Author Spotlight: Improving Beef Cattle Nutrition and Production with a Focus on Feed Efficiency and Meat Quality Traits Through Advanced Biochemical and Molecular Assays
Published on: July 12, 2024
06:19Evaluation of Oxidative Stress in Biological Samples Using the Thiobarbituric Acid Reactive Substances Assay
Published on: May 12, 2020
Related Concept Videos
Protein Digestion
Protein Denaturation
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Bacterial Protein Maturation
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...