This study investigated the effects of different freeze-thaw (F-T) cycles and subsequent heat treatment on the odor-binding properties of myofibrillar protein (MP) in grass carp to four key fishy substances. The odor-binding ability of MP significantly decreased as freeze-thaw (F-T) cycles increased (p < 0.05). After heating, the odor-binding ability of MP further decreased. Freeze-thaw treatment induced the oxidative denaturation, decreased total sulfhydryl content and unfolded the α-helix in MP, which modified and re-buried the exposed odor-binding sites, reducing odor-binding ability. After heating, the oxidative damage and aggregation of MP induced by freeze-thaw cycles, along with thermal effects, synergistically accelerated the oxidative denaturation and formation of disordered structures of heated MP. Enhanced hydrophobic interactions led to a dominant aggregation effect, which reduced the binding sites and further decreased the odor-binding ability of heated MP, resulting in more release of odors.
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