期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 62, 期 10, 页码 2158-2164出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf405705t
关键词
nitrite; ascorbate; tryptophan oxidation; carbonylation; nitrosation; 3-nitrotyrosine
资金
- Spanish Ministry of Economics and Competitiveness (SMEC) [RYC-2009-03901, AGL2010-15134]
- Executive Research Agency from the European Community through the Marie Curie Reintegration Fellowship, Pox-MEAT [PERG05-GA-2009-248959,]
- predoctoral Formacion de Personal Investigador (FPI) from SMEC
Understanding the chemistry behind the redox properties of nitrite and ascorbate is essential to identify the impact of curing agents on food quality and optimize the formulation of cured meat products. This study was designed to gain insight into the interactions between curing agents and myofibrillar proteins (MPs) during in vitro oxidation by a hydroxylradical-generating system. MPs (4 mg/mL) were oxidized for 4 days at 37 degrees C under constant stirring with 25 mu M iron(III) and 2.5 mM hydrogen peroxide. Dependent upon the addition of nitrite (0, 75, and 150 mg/L) and ascorbate (0, 250, and 500 mg/L), nine different reaction units were prepared in triplicate (n = 3) according to a total factorial design. Upon completion of the oxidation assay, samples were analyzed for the concentration of tryptophan (TRP), a-aminoadipic semialdehyde (AAS), Schiff bases (SBs), and 3-nitrotyrosine (3NT). Ascorbate at 250 mg/L significantly inhibited the depletion of TRP (similar to 20% inhibition) and the formation of AAS and SBs (>90% inhibition) in MP suspensions. Nitrite, alone, had a negligible effect on protein oxidation but induced the formation of a specific marker of nitrosative stress, namely, 3NT. Ascorbate was also efficient at inhibiting the formation of 3NT by a dose-dependent anti-nitrosative effect and enabled the antioxidant action of nitrite.
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