Proteins and phenolics compounds interaction may lead to properties changes in both components. The effect of whey proteins (WPI) and epigallocatechin gallate (EGCG) association on digestibility and digests characteristics were investigated. Complexes were obtained by mixture of aqueous WPI and EGCG solutions at 1:0.5 molar relation. The complexation was carried out at 25 °C at pH 3.5 (WPI:EGCG-3.5) or 7.0 (WPI:EGCG-7.0). Static in vitro digestion, based on the method standardized by Infogest, started with 2% (w/v) protein solution, using pepsin (4,900 U/mg enzyme) and pancreatin (enzyme:substrate 1:20 w/w). WPI and EGCG solutions were also digested. EGCG solution contained the same phenolic compound concentration of the complex, with pH adjustment to 3.5 and 7.0. Digestibility was assessed by soluble nitrogen in 13.3% TCA. Molecular mass (MM) profile was evaluated by SDS-PAGE/Tricine and hydrophilic profile by RP-HPLC. WPI:EGCG complexes obtained at pH 3.5 and 7.0 presented digestibility similar to WPI (83%) (p<0.05). Although WPI and WPI:EGCG electrophoretic profiles showed intact β-Lg, the band was more intense in the complexes profiles. This suggests that interaction with EGCG decreased the proteolysis of β-Lg. Chromatograms of undigested complexes showed that the peak intensity corresponding to EGCG standard was higher in the chromatographic profile of WPI:EGCG-3.5 than in WPI:EGCG-7.0 and EGCG. This suggests that complexation at pH 3.5 improved the EGCG stability to degradation during the in vitro digestion. Furthermore, chromatograms of digested complexes presented peptides profile with higher hydrophilicity than the digested WPI. Although WPI:EGCG-3.5 and WPI:EGCG-7.0 chromatographic profiles were similar, peak intensities were different. The digestion of the complexes released more hydrophobic peptides than WPI. In summary, the presence of EGCG and pH of complexation affected the protein cleavage by gastrointestinal enzymes, resulting in different peptides pattern.