ArticleFoods (Basel, Switzerland)2023
Identification of Protein-Phenol Adducts in Meat Proteins: A Molecular Probe Technology Study.
Article in Foods (Basel, Switzerland), 2023. 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, 5 citations in OpenAlex.
- Fermented Radish and Beetroot Powder as Natural Sources of Nitrite in Beef Burger.Foods (Basel, Switzerland) · 2026Article
- Effects of Whey and Plant-Based Additives on Technological and Microbiological Characterization of Fermented Raw-Dried Pork Meat Snacks of Human Grade Standard.Foods (Basel, Switzerland) · 2025Article
- Incorporation of Pork Meat and Blood Plasma Proteins into a Cocoa Cream Matrix: Characterization, Comparison of Functional Properties, and In Vitro Simulated Digestion.Foods (Basel, Switzerland) · 2025Article
- The Heat-Induced Gel-Sol Transition in Coated Tofu: A Study on Protein Conformation and Microstructural Changes.Gels (Basel, Switzerland) · 2025Article
- Recent Advances, Challenges, and Functional Applications of Natural Phenolic Compounds in the Meat Products Industry.Antioxidants (Basel, Switzerland) · 2025Review
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Plant polyphenols with a catechol structure can form covalent adducts with meat proteins, which affects the quality and processing of meat products. However, there is a lack of fast and effective methods of characterizing these adducts and understanding their mechanisms. This study aimed to investigate the covalent interaction between myofibrillar protein (MP) and caffeic acid (CA), a plant polyphenol with a catechol structure, using molecular probe technology. The CA-MP adducts were separated via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and detected via Western blot and LC-MS/MS analyses. The Western blot analysis revealed that various specific adducts were successfully enriched and identified as bands around 220 kDa, 45 kDa, and two distinct bands between 95 and 130 kDa. Combined with the LC-MS/MS analysis, a total of 51 peptides were identified to be CA-adducted, corresponding to 31 proteins. More than 80% of the adducted peptides carried one adducted site, and the rest carried two adducted sites. The adducted sites were located on cysteine (C/Cys), histidine (H/His), arginine (R/Arg), lysine (K/Lys), proline (P/Pro), and N-terminal (N-Term) residues. Results showed that the covalent interaction of CA and MP was highly selective for the R side chain of amino acids. Moreover, the adducts were more likely to form via C-N bonding than C-S bonding. This study provides new insights into the covalent interaction of plant polyphenols and meat proteins, which has important implications for the rational use of plant polyphenols in the meat processing industry.
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