期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 58, 期 7, 页码 4448-4455出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf903757h
关键词
Oxidation; myofibrillar proteins; semialdehydes; DNPH-method; LC-ESI-MS; phenolic compounds
资金
- Marie Curie Intra-European Fellowship
The effect of selected phenolic compounds, namely, gallic acid, chlorogenic acid, genistein, catechin, cyanidin-3-glucoside and rutin, on the formation of specific protein carbonyls, alpha-aminoadipic and gamma-glutamic semialdehydes (AAS and GGS, respectively), from oxidized nnyofibrillar proteins, was studied in the present article. Suspensions containing myofibrillar proteins (20 mg/mL) and the aforementioned phenolic compounds (1 mM) were oxidized (37 degrees C for 20 days) in the presence of copper acetate, iron (FeCl3), or myoglobin (10 mu M) in combination with 1 mM H2O2 and analyzed for AAS and GGS using liquid chromatography-electrospray ionization mass spectrometry (LC-ESI-MS). Suspensions with added alpha-tocopherol (1 mM) and a control group (with no phenolic compound) were also considered. In the presence of copper, the alpha-tocopherol and most phenolic compounds significantly inhibited the formation of AAS and GGS. In iron- and myoglobin-oxidized suspensions, however, some of those phenolic compounds (i.e., chlorogenic acid and genistein) promoted the formation of the semialdehydes. Besides the influence of the oxidation promoters, the overall effect of plant phenolics on protein oxidation is likely affected by the chemical structure of the phenolics and the result of the interactions between these compounds and myofibrillar proteins. Plausible mechanisms for the antioxidant and pro-oxidant effects of plant phenolics on myofibrillar proteins are proposed in the present article. This study highlights the complexity of redox reactions between plant phenolics and oxidizing myofibrillar proteins.
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