Partial substitution of animal protein by plant protein is a new opportunity to produce sustainable food for human beings. However, separated studies of plant protein and egg white cannot help to have a direct understanding of the complex structure in a mixed food product. In this work, we used low-denatured pea globulins (PG) in admixture with raw egg white (EW) to study the thermal and rheological behavior of the mixed systems submitted to heat treatment (<100 °C). The protein systems were studied at pH 7.5 and 9 for different PG/EW weight ratios by using Differential Scanning Calorimetry and dynamic rheology. At pH 7.5, the PG-EW mixtures did not show significant changes in thermo-denaturation parameters, i.e. denaturation temperature (Td) and enthalpy (ΔH), of the respective proteins. At pH 9, only the Td of conalbumin decreased significantly from 63 ℃ to 59 ℃ with addition of pea protein. Furthermore, dynamic rheology data during temperature sweep (25-100-25 °C) showed that the first gel point (~59 ℃) assigned to conalbumin in egg white proteins were not detected for the mixtures indicating that early gel formation could be hindered by the presence of pea globulins. The higher gel points corresponding to other proteins (i.e. ovalbumin and pea globulins) were very similar and didn’t appear modifications in the mixture. Frequency sweep indicated a strong viscoelastic gel structure (G’>>G’’) for all the protein samples whatever the pH. Higher storage modulus (G’) values for egg white indicated stronger elastic behavior as for the mixtures. From strain sweep experiments, the addition of PG in the mixture led to a longer linear viscoelastic region compared to EW gels indicating higher stiffness in the PG-EW gel structure. These data are crucial information to define gel properties in mixed plant-animal protein systems.