Abstract:Objective This study aims to reveal the interactions between collagen and volatile compounds during the cooking process.Method The relative molecular weight, particle size, solubility, secondary structure, and surface hydrophobicity of collagen and the droplet size of the collagen emulsion were studied. Furthermore, the binding ability of collagen to volatile compounds of the aqueous and emulsion systems of collagen was measured.Result As the heating time was extended, the triple-helix structure of collagen was destroyed and the polypeptide chains were degraded, which were accompanied with the decrease in surface hydrophobicity, increase in solubility, and heat-induced aggregation. The binding ability of collagen to volatile compounds gradually decreased with the extension of heating time. In the aqueous system, the release of volatile compounds was promoted after heating for 4 h. In the emulsion system, collagen exhibited a higher binding ability to volatile compounds and did not exhibit the effect of promoting release of volatile compounds even after heating for 4 h.Conclusion The triple-helix structure of collagen is beneficial to the binding to volatile compounds and the heating time has a negative correlation with the binding ability of collagen to volatile compounds. Collagen exhibits the strongest binding ability to volatile compounds in the case of short-term heating and the coexistence with lipids.
