The antioxidant effect of porcine pancreatic phospholipase A2 (PLA2) was previously demonstrated. Understanding how PLA2 inhibits lipid oxidation promoted by hemoglobin (Hb) is important for its applications in muscle foods. Effects of enzyme dose, pH, and calcium ion on the ability of PLA2 to inhibit trout hemoglobin-mediated lipid oxidation were investigated in washed cod muscle (WCM). Results indicated that PLA2 required calcium ion for both the hydrolyzing activity and the antioxidant effect. The abilities of PLA2 to inhibit lipid oxidation and suppress oxidation of Hb to form methemoglobin and ferryl hemoglobin were pH-dependent. The lag phase before lipid oxidation enters the exponential phase reciprocally shortened as more hemin was bound to the insoluble matrix of WCM. However, PLA2 was able to inhibit lipid oxidation without preventing the interaction between hemin and the insoluble matrix of the washed muscle.
Keywords: Antioxidant; Calcium ion; Hemin; Hemoglobin; Lipid oxidation; Phospholipase A2.
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