Effect of pH on lipid oxidation mediated by hemoglobin in washed chicken muscle

Abstract To investigate the effect of pH on lipid oxidation of chicken muscle, chicken hemolysates were added to washed chicken muscles to analyze lipid oxidation at pH 5.7, 6.3, and 7.2. The results showed that with a blue shift of the Soret peak, oxyhemoglobin gradually transformed to methemoglobin during storage, the shape of porphyrin rings of heme in fluorescence electron microscopy changed from round to trail-like structure. These changes were more significant at low pH. Comparing hemoglobin (Hb) structure, the distance of amino acids between the E10 of lysine and metHb-7-propionate groups is longer at pH 5.7 than other pHs, which makes solvent easily enter the heme cavity, leading to the severe destruction of Hb. The linear correlation between color and lipid oxidation also further confirmed that the increased oxidation of chicken Hb causes more rapid lipid oxidation in pH 5.7 than the other 2 pHs (p