The antioxidant activities of nitrite and nitrosylmyoglobin in cooked meats

Low concentrations of nitrite (20 mg/kg) caused significant (p < 0·001) inhibition of lipid oxidation, measured by the TBA test, in a cooked muscle system and 50 mg/kg nitrite resulted in a highly significant (p < 0·001) reduction in TBA values. Similar antioxidant effects of nitrite were observed in heated water-extracted pork muscle systems catalysed by 5 mg/g metmyoglobin (Mb) or 5 mg/kg Fe(2+), Cu(2+) or Co(2+). The cured meat pigment, nitrosylmyoglobin per se exhibited significant (p < 0·05) antioxidant effects in pork muscle systems catalysed by Mb or metal ions. Progressive depletion of nitrite occurred during refrigerated storage of heated and unheated nitrite-treated pork muscle, muscle aqueous extract and in systems containing Mb, Cu(2+) ot Co(2+). Nitrite depletion occurred much more rapidly in Fe(2+)-containing systems and nitrite concentration had decreased to 5% of the original concentration immediately after heating. In addition, nitrite caused a significant (p < 0·05) reduction in the concentration of non-haem iron in heated aqueous-extracts of beef muscle, whereas, in nitrite-free extracts, a highly significant (p < 0·001) increase in the concentration of non-haem iron, probably due to heat denaturation of the haem structure with release of iron, was observed. Based on the results of this study, three co-operative mechanisms for the antioxidative activities in meat are proposed: (a) by the formation of MbNO which has antioxidant properties per se, (b) on heating, MbNO forms a stable complex, nitrosylhaemochrome, which blocks the catalytic activity of haem iron and also prevents release of haem iron as non-haem iron, which is a highly effective catalyst and (c) nitrite appears to 'chelate' non-haem iron-and possibly copper and cobalt-forming a stable complex, thus inhibiting catalytic activity.