Interaction mechanisms of sea cucumber proteins with flavor compounds: Adsorption behavior, dynamic equilibrium and structural changes.

Adsorption capacity of sea cucumber collagen crude extract (CCE) for characteristic flavor compounds in a gas-mediated environment was compared. The results revealed the CCE-Flavor system stabilizes after 240 min of adsorption time, manifested as a non-linear binding relationship. When the four compounds compete and coexist, the system reached a dynamic equilibrium. Meanwhile, hydrophobic interactions serve as the primary driving force between CCE and flavors. Fourier transform infrared (FTIR) and fluorescence (FL) spectroscopy analyses demonstrated that saturated concentrations of flavor compounds can induce changes in the secondary and tertiary structures of CCE. The decrease in α-helix content, the depolymerization of proteins, and the increase in hydrophobic groups within CCE create additional binding sites for flavors. This study establishes a foundation for understanding the interaction mechanism between sea cucumber protein and flavor substances by analyzing the conformational changes of CCE and the adsorption behavior of these flavor substances.