Interaction mechanism of collagen peptides with four phenolic compounds in the ethanol-water solution

Abstract

This study demonstrated the interaction mechanism of collagen peptides (CPs) with 4-ethylphenol (4-EP), phenol, guaiacol, and 4-ethylguaiacol (4-EG) in the ethanol-water solution. The ultraviolet visible spectroscopy, zeta potential tests and hydrogen nuclear magnetic spectroscopy manifested that CPs interacted with the phenolic compounds. Meanwhile, Isothermal titration calorimetry determination indicated that the CPs was hydrogen bonded with 4-EP in 52 %(v/v) ethanol-water solution, while the hydrophobic forces played a major role in the interaction of CPs with guaiacol and 4-EG, respectively. Moreover, hydrogen and hydrophobic bonds were involved in the interaction between CPs and phenol. Finally, Head Space-solid Phase Microextraction Gas Chromatography Mass Spectrometry analysis indicated that the content of phenolic compounds in model solution efficiently decreased with the presence of CPs. In the real liquor, it was found that the content of volatile compounds (including phenolic compounds) was obviously decreased after CPs added.