Effect of heat treatment duration on the interaction between fish myosin and selected flavor compounds.

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.