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Published on: June 21, 2021
4-methylcatechol inhibits protein oxidation in meat but not disulfide formation
Sisse Jongberg1, Marianne N Lund, Andrew L Waterhouse
1Food Chemistry, Department of Food Science, Faculty of Life Sciences, University of Copenhagen, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark.
Abstract:
The interaction between phenolic compounds and protein thiols was investigated in minced beef with or without 500 ppm 4-methylcatechol (4-MC) that had been stored under oxygen or argon for 7 days (4 °C). Myofibrillar protein isolates were extracted, and the oxidative stability evaluated by the protein radical intensity measured by ESR spectroscopy was found to be improved by 4-MC as well as by storage without oxygen. Significant loss of thiols was found in samples stored under oxygen compared to argon, whereas an additional loss was found in samples with added 4-MC stored under oxygen. In beef with added 4-MC, LC-MS analysis showed formation of thiol-quinone adducts, which may explain the observed additional loss of thiols. Although storage without oxygen inhibited protein cross-link formation as evaluated by SDS-PAGE, both in presence and in the absence of 4-MC, no inhibitory effect of 4-MC was found on the formation of protein disulfide cross-links in beef stored under oxygen.
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