The valuable antioxidant activity of superoxide dismutase (SOD) involved in protective mechanisms against ROS (reactive oxygen species) was monitored. SOD activity was evaluated in two crude meat extracts by measuring the ability of SOD to inhibit the autoxidation of pyrogallol, with the aim to further understand its thermal and athermal stability.
The activity of superoxide dismutase extracted from Longissimus dorsi muscle of pork and pork kidney extracts was measured in the presence of phosphate buffer with 1 mM EDTA, pH 8.2, using 0,15 mM pyrogallol and 10 mM HCl as substrate. SOD activity in kidney and Longissimus dorsi muscle extracts was spectrophotometrically assessed.
SOD extracted from pork kidney displayed higher activity values than the one from Longissimus dorsi muscle, thus it was further selected for the inactivation studies. This preliminary study of SOD activity demonstrated that kidney extracts are richer in SOD and could represent a better choice for performing thermal and athermal inactivation.
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