Comparative Analysis of Different Hemoglobins:  Autoxidation, Reaction with Peroxide, and Lipid Oxidation

Beef hemoglobin (Hb) had lower levels of deoxyHb and autoxidized much slower as compared to trout Hb at pH 6.3. Chicken Hb autoxidized at a rate intermediate between beef and trout Hb. In the presence of hydrogen peroxide, metHb formed rapidly from trout Hb whereas beef Hb was essentially nonreactive with hydrogen peroxide. The autoxidation rate of perch Hb was more rapid than trout Hb despite the low deoxyHb content of perch Hb. Perch Hb was a better catalyst of lipid oxidation than trout Hb when added to washed cod muscle based on formation of lipid hydroperoxides and thiobarbituric acid reactive substances. These studies indicate that autoxidation rate does not always increase with increasing deoxyHb content. The role of heme crevice volume in heme protein autoxidation is discussed. Among other factors, these studies suggest that rates of lipid oxidation in various muscle foods may depend on the relative ability of hemoglobins from different animal species to promote lipid oxidation. Keywords: Trout; perch; chicken; beef; rancidity; blood; oxygen affinity; quality deterioration; muscle foods; Bohr effect; hydrogen peroxide; deoxyhemoglobin