Effects of fish heme protein structure and lipid substrate composition on hemoglobin-mediated lipid oxidation.

Hemoglobin (Hb) promoted lipid oxidation more effectively in washed tilapia as compared to washed cod in spite of a 2.8-fold higher polyenoic index in the washed cod. This suggested that increasing the fatty acid unsaturation of the substrate did not accelerate the onset of lipid oxidation. Substantial phospholipid hydrolysis in the washed cod was observed, which has the potential to inhibit lipid oxidation. MetHb formation and lipid oxidation occurred more rapidly at pH 6.3 as compared to pH 7.4. Trout Hb autoxidized faster and was a better promoter of lipid oxidation as compared to tilapia Hb. The greater ability of trout Hb to promote lipid oxidation was attributed in part to its lower conformational and structural stability based on secondary and tertiary structure, acid-induced unfolding, and thermal aggregation measurements. It is suggested that the structural instability and lipid oxidation capacity of trout Hb were at least partly due to low hemin affinity. Trout and tilapia Hb were equivalent in their ability to cause lipid oxidation in washed cod muscle heated to 80 degrees C. Apparently, these high temperatures denature both trout and tilapia Hb to such an extent that any differences in conformational stability observed at lower temperatures were negated.