Effect of high hydrostatic pressure on the oxidation of washed muscle with added chicken hemoglobin

•Chicken hemoglobin is relatively stable at high hydrostatic pressures.•Oxidation in washed chicken is promoted by high pressure processing and hemoglobin.•Oxidation is related to the appearance of methemoglobin and insoluble heme forms.•The release of hemin seems to play a crucial role in the progression of oxidation. The role of chicken hemoglobin in lipid oxidation of washed chicken muscle exposed to high hydrostatic pressure (0, 200, 400 and 600 MPa) was examined. The observed decrease in redness was higher with elevated pressures (5.0 vs 3.7). During storage, redness decreased in samples exposed to 400 and 600 MPa. This decrease was concomitant with the progression of oxidation and the 2.5 fold decrease of soluble heme. An additional experiment was conducted to examine the effect of the hemoglobin mode of addition into pressurized muscle. The exposure at 600 MPa led to washed muscle oxidation even in the absence of hemoglobin, thus indicating that pressure treatments triggered lipid oxidation. However, the presence of native or pressurized hemoglobin into pressurized washed muscle caused more hexanal than the pressurized control without hemoglobin. Overall, results suggest that membrane disruption and the release of hemin are crucial for the onset of oxidation.