Abstract
Interaction between tuna myoglobin and myosins from tuna and sardine was investigated in a model system at 4 °C for up to 24 h. Both sardine and tuna myosins bound progressively with tuna myoglobin as the storage time increased ( P < 0.05). The soret absorption peak was noticeable in the myoglobin–myosin mixture. The oxidation of oxymyoglobin in the presence of myosin was generally greater than that found in the absence of myosin ( P < 0.05). Oxymyoglobin underwent oxidation to a greater extent in the presence of tuna myosin than sardine myosin ( P < 0.05). The interaction between fish myoglobin and myosin also caused changes in reactive sulfhydryl content and altered the tryptophan fluorescent intensity. The loss in Ca 2+-ATPase activity of myosin varied with fish species and was governed by the myoglobin added. Thus, the interaction between fish myoglobin and myosin most likely occurred as a function of time and was species-specific.
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