Maillard reaction products inhibit lipid oxidation by regulating myoglobin stability in washed muscle model

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 Mb-mediated 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. PRACTICAL APPLICATION: 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.

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Publication Details

Journal
Journal of Food Science
Published
2024-09-30
DOI
https://doi.org/10.1111/1750-3841.17378
Citations
6
Primary Topic
Meat and Animal Product Quality
Type
article
Field-Weighted Citation Impact
2.05
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article

Maillard reaction products inhibit lipid oxidation by regulating myoglobin stability in washed muscle model

Yixiao Shen, Haixia Yan, Ling Liu, Bing Bai et al.
6 citations
Journal of Food Science
Meat and Animal Product Quality
2.05
article

Maillard reaction products inhibit lipid oxidation by regulating myoglobin stability in washed muscle model

Yixiao Shen, Haixia Yan, Ling Liu, Bing Bai, Jiarong Cao, Yingbo Zhao
article en
6 citations

Abstract

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 Mb-mediated 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. PRACTICAL APPLICATION: 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.

Journal of Food ScienceVol. 89(11)
Shenyang Agricultural University (CN)
Life below water
Openalex Percentile: Top 15%
Meat and Animal Product Quality
2.05
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Maillard reaction products inhibit lipid oxidation by regulating myoglobin stability in washed muscle model — Yixiao Shen, Haixia Yan, et al. · Journal of Food Science (2024) | TGRS Research Map | TGRS