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.

Properties of tilapia carboxy- and oxyhemoglobin at postmortem pH.

Hemoglobin plays an important role in the color and oxidative stability of seafoods. A recent practice in the seafood industry is to stabilize muscle color by the application of gases containing carbon monoxide. The goal of this study was to examine and compare the properties of tilapia hemoglobin complexed to either O(2) (Oxy-Hb) or CO (CO-Hb) at pH 6.5, which reflects the tilapia muscle postmortem pH. CO-Hb was significantly (p < 0.01) more stable against autoxidation compared to Oxy-Hb when kept at 4 and -30 degrees C for 23 days. Almost no loss of CO was detected for both temperatures according to the UV-vis spectra of Hb. This stabilization was also believed to play a role in increased protein structure stabilization (p < 0.001) since less protein aggregation was seen for CO-Hb. The higher protein stabilization for Hb was linked to the heme group, which was maintained in its reduced state longer for CO-Hb vs Oxy-Hb and was likely less exposed to solvent. CO-Hb had significantly (p < 0.01) less peroxidase activity than Oxy-Hb and thus reactivity with H(2)O(2). The pro-oxidative activity of CO-Hb was significantly (p < 0.01) reduced in a linoleic acid micelle system compared to that of Oxy-Hb, while smaller differences in activity were seen in a washed cod and tilapia muscle model system.