Journal
FOOD CHEMISTRY
Volume 416, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2023.135818
Keywords
Biotinylated caffeic acid; Myofibrillar proteins; Covalent interaction; Gel properties; Correlation analysis
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The study investigated the effects of covalent interactions between myofibrillar proteins (MP) and caffeic acid (CA). Protein-phenol adducts were identified using biotinylated caffeic acid (BioC) as a substitute for CA. The total sulfhydryls and free amines content decreased, while the alpha-helix structure of MP increased. MP gel properties slightly enhanced at low CA dosages, but significantly impaired at high CA dosages. Myosin heavy chain (MHC)-BioC and Actin-BioC adducts were identified and their concentrations showed a negative correlation with gel properties.
In this study, the effects of covalent interactions between myofibrillar proteins (MP) and caffeic acid (CA) were investigated. Protein-phenol adducts were identified by biotinylated caffeic acid (BioC) used as a substitution of CA. The total sulfhydryls and free amines content were decreased (p < 0.05). The alpha-helix structure of MP increased (p < 0.05) and MP gel properties enhanced slightly at low dosages of CA (10 and 50 mu M), and both were impaired significantly (p < 0.05) at high dosages of CA (250 and 1250 mu M). Two prominent adducts of myosin heavy chain (MHC)-BioC and Actin-BioC were identified by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), which gradually increased at low concentrations of BioC (10 and 50 mu M), and raised significantly at the concentration of 1250 mu M. According to the correlation analysis, MHC-BioC and Actin-BioC adducts showed a significant negative correlation with gel properties, such as G', hardness, and water holding capacity (WHC) (p < 0.01), which indicated that the covalent interactions between MP and CA significantly affected the quality of meat products.
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