Effect of different saturated aldehydes on the changes in sardine (Sardinella gibbosa) myoglobin stability.

Effect of saturated aldehydes with different carbon chain lengths, including hexanal, heptanal, octanal, nonanal and decanal, on the changes in sardine (Sardinella gibbosa) myoglobin were investigated in a model system at 4°C for 180 min. The formation of metmyoglobin increased with increasing carbon chain length (p<0.05). The highest metmyoglobin content corresponded with the lowest oxymyoglobin remaining was found in the presence of decanal (p<0.05). The changes in tryptophan fluorescence intensity and soret absorption spectra of myoglobin were observed and varied with aldehydes added. SDS-PAGE revealed that saturated aldehydes did not induce the cross-linking of myoglobin. Generally, decanal was the most reactive saturated aldehyde to alter the fish myoglobin stability.

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