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Maillard reaction products inhibit lipid oxidation by regulating myoglobin stability in washed muscle model.
- Source :
-
Journal of Food Science (John Wiley & Sons, Inc.) . Sep2024, p1. 14p. 8 Illustrations. - Publication Year :
- 2024
-
Abstract
- Practical Application Lipid oxidation significantly contributes to muscle deterioration, with heme protein oxidation playing a crucial role in this process. This study investigated the inhibition of heme protein oxidation by Maillard reaction products (MRPs) using a washed muscle model combining washed carp with myoglobin (Mb). Protein oxidation products, protein texture, and lipid oxidation levels were assessed. Results showed that metmyoglobin (MetMb) is a primary driver of lipid oxidation in meat, likely due to Mb oxidation, exposing hydrophobic groups that bind to lipids. MRPs at concentrations of 0.5% and 1% effectively inhibited Mb oxidation. Specifically, treatment with 1% MRPs reduced MetMb formation by 15.38%, protein carbonyl content by 6.53%, hydroxyl radical content by 20.37%, protein aggregation by 40.81%, and particle size by 36.95% during later storage stages, thereby preserving Mb stability. In the Mbāmediated oxidation model, 1% MRPs inhibited the formation of primary and secondary oxidative metabolites by 59.47% and 68.19%, respectively, while maintaining muscle tissue texture integrity.The antioxidation of Maillard reaction products (MRPs) improves the stability of common carp. By inhibiting the autoxidation of myoglobin and lipid, MRPs help preserve the texture and color of fish muscle while extending its shelf life. This study provides a valuable reference for effectively controlling lipid oxidation in refrigerated fish products and enhancing their overall quality. [ABSTRACT FROM AUTHOR]
- Subjects :
- *COLOR of fish
*MAILLARD reaction
*HEMOPROTEINS
*METABOLITES
*CARP
*MYOGLOBIN
Subjects
Details
- Language :
- English
- ISSN :
- 00221147
- Database :
- Academic Search Index
- Journal :
- Journal of Food Science (John Wiley & Sons, Inc.)
- Publication Type :
- Academic Journal
- Accession number :
- 180067851
- Full Text :
- https://doi.org/10.1111/1750-3841.17378