%0 Journal Article %A Bin Bao %A Qianqian Chu %A Wenhui Wu %T Mechanism of Interaction between Phenolic Compounds and Proteins Based on Non-Covalent and Covalent Interactions %D 2018 %R 10.21127/yaoyimr20180014 %J Medicine Research %P 180014- %V 2 %N 3 %X Phenolic compounds are widely used in natural plant foods and have strong antioxidant properties, so they are widely used in food and medicine. The reaction between the phenolic compound and the protein can affect the functional properties of the protein, such as emulsifying properties, gel properties, solubility, thermal stability, and foaming properties. The mechanism of interaction between phenolic compounds and proteins are described from the aspects of non-covalent interaction and covalent interaction, and the characterization methods of the interaction mechanism between phenolic compounds and proteins are described. The indexes for characterizing the covalent bonding of phenolic compounds and proteins include the free amino group content, total sulfhydryl content, tryptophan content. Ninhydrin method, 2,4,6-trinitrobenzenesulfonic acid (TNBS) method, o-phthal- aldehyde (OPA) method and high-performance liquid phase chromatography were applied to o measure the free amino group content. Ellman’s method was applied to investigate total sulfhydryl content. Fluorescence measurements can be used for changes in tryptophan modification. The indexes for characterizing the con-covalent bonding of phenolic compounds and proteins include hydrogen bonding, hydrophobic interactions, disulfide bonds and hydrophobicity of protein surface. Hydrogen bonding, hydrophobic interactions and disulfide bonds can be investigated by Gómez-Guillén’s method. ANS fluorescent probe method was applied to measure the changes of hydrophobicity of protein surface. %U http://www.medicineresearch.org/EN/10.21127/yaoyimr20180014