Interactions between tea polyphenol and two kinds of typical egg white proteins—ovalbumin and lysozyme: Effect on the gastrointestinal digestion of both proteins in vitro

The promotion or inhibition of gastrointestinal digestion of tea polyphenol (TP) towards the two typical proteins from egg white (ovalbumin (OVA) and lysozyme (LYZ)) was examined. The results showed that TP made OVA/LYZ easier for digestion in the pepsin solution at pH1.2 and inhibited OVA/LYZ digestion in pancreatin solution at pH7.5. Non-covalent interactions between OVA/LYZ and TP and the secondary structure of OVA/LYZ were studied by using Fluorescence spectroscopy and Fourier transform infrared spectroscopy (FTIR), respectively. Results suggested that stronger conformational change occurred at pH1.2 compared with that of pH7.5 affected by TP in both proteins. Non-covalent interactions between OVA/LYZ and TP at pH1.2 increased random and β-sheet structures in both proteins at the expense of α-helix, which resulted in the proteins with looser structures. At pH7.5, an opposite second structural change of both proteins caused by the non-covalent interactions between OVA/LYZ and TP. The conformational and second structural change of proteins (substrate) might be a reason for promoting and inhibiting digestion of OVA/LYZ affected by TP. Tea polyphenol facilitated the pepsin digestion of ovalbumin (OVA)/lysozyme (LYZ) at pH1.2 and inhibited the pancreatin digestion of OVA/LYZ at pH7.5. The impact mechanism was also studied. [Display omitted] •TP facilitates pepsin digestion and inhibits pancreatin digestion of OVA/LYZ.•The effect of TP on proteins is in a dose-dependent manner.•TP affects the conformational and second structural change of substrate.•TP influences structural change of substrate thus affects the digestion of proteins.