Protein and tea polyphenols are common interaction systems.The purpose of this study is to investigate the interaction between casein and theaflavins by fluorescence spectroscopy,and to determine their binding mechanism by model fitting at different temperatures.The results showed that theaflavins could quench the self-fluorescence of casein,and the fluorescence was static.When the concentration of theaflavins was 0.028 mg/mL,the fluorescence intensity of casein decreased by 66.7％,55.6％and 52.2％at 29 ℃,37 ℃and 45 ℃,respectively,and the maximum emission wavelength showed a slight redshift.At different temperatures,casein can spontaneously bind to theaflavins,the number of binding sites is about 1,and the binding mode is mainly dominated by hydrogen bond and van derWaals force.The results provide a foundation for the application of casein-theaflavins complex in functional food.
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