BACKGROUND: Interactions between flavor compounds and proteins during food processing are critical to flavor perception of the final product. Here, we investigated the effect of the duration of heat treatment on the interaction between bighead carp myosin and selected flavor compounds including hexanal, heptanal, octanal, nonanal, (E)-2-heptenal, and 1-octen-3-ol. RESULTS: The binding of flavor compounds to native myosin was strong and decreased in the order nonanal > octanal > (E)-2-heptenal > heptanal > hexanal >1-octen-3-ol. The aldehydes, especially trans-2-undecenal, were more conducive to hydrophobic binding to myosin than alcohols. Within the initial 5 min of heating, the surface hydrophobicity and total sulfhydryl exposure increased, while α-helix turned into β-sheets, β-turns, and random coils. However, upon further heating, the hydrophobicity and sulfhydryl contents declined, β-sheets, β-turns and random coils shifted to α-helix. Throughout the heating process, the particle size increased, and the absolute zeta potential decreased continuously, indicating that thermal aggregation of myosin occurred simultaneously. Changes in binding capacities of flavor compounds to myosin were consistent with changes in hydrophobicity and sulfhydryl contents. CONCLUSION: The initial enhancement of the flavor-binding capacity of myosin was attributed to the unfolding of secondary structures by exposing more hydrophobic bonding sites and hydrogen bonding sites. The rebuilding and aggregating of myosin was enhanced upon prolonged heating, thus favoring hydrophobic protein-protein interactions and weakening the resultant flavor binding capacity of myosin.
BACKGROUND: Interactions between flavor compounds and proteins during food processing are critical to flavor perception of the final product. Here, we investigated the effect of the duration of heat treatment on the interaction between bighead carp myosin and selected flavor compounds including hexanal, heptanal, octanal, nonanal, (E)-2-heptenal, and 1-octen-3-ol. RESULTS: The binding of flavor compounds to native myosin was strong and decreased in the order nonanal > octanal > (E)-2-heptenal > heptanal > hexanal >1-octen-3-ol. The aldehydes, especially trans-2-undecenal, were more conducive to hydrophobic binding to myosin than alcohols. Within the initial 5 min of heating, the surface hydrophobicity and total sulfhydryl exposure increased, while α-helix turned into β-sheets, β-turns, and random coils. However, upon further heating, the hydrophobicity and sulfhydryl contents declined, β-sheets, β-turns and random coils shifted to α-helix. Throughout the heating process, the particle size increased, and the absolute zeta potential decreased continuously, indicating that thermal aggregation of myosin occurred simultaneously. Changes in binding capacities of flavor compounds to myosin were consistent with changes in hydrophobicity and sulfhydryl contents. CONCLUSION: The initial enhancement of the flavor-binding capacity of myosin was attributed to the unfolding of secondary structures by exposing more hydrophobic bonding sites and hydrogen bonding sites. The rebuilding and aggregating of myosin was enhanced upon prolonged heating, thus favoring hydrophobic protein-protein interactions and weakening the resultant flavor binding capacity of myosin.