Thermal Behavior of Pea and Egg White Protein Mixtures

Abstract

The partial substitution of animal protein by plant protein is a new opportunity to produce sustainable food. Hence, to control the heat treatment of a composite protein ingredient, this work investigated the thermal behavior of mixtures of raw egg white (EW) and a laboratory-prepared pea protein isolate (PPI). Ten-percentage-by-weight protein suspensions prepared with different PPI/EW weight ratios (100/0, 75/25, 50/50, 25/75, 0/100) at pH 7.5 and 9.0 were analyzed by differential scanning calorimetry (DSC) and dynamic rheology in temperature sweep mode (T < 100 °C). The DSC data revealed changes in the thermal denaturation temperatures (Td) of ovotransferrin, lysozyme, and pea legumin, supposing interactions between proteins. Denaturation enthalpy (∆H) showed a high pH dependence related to pea protein unfolding in alkaline conditions and solubility loss of some proteins in admixture. Upon temperature sweeps (25–95 °C), the elastic modulus (G′) of the mixtures increased significantly with the EW content, indicating that the gel formation was governed by the EW protein. Two thermal sol–gel transitions were found in EW-containing systems. In particular, the first sol–gel transition shifted by approximately +2–3 °C at pH 9.0, probably by a steric hindering effect due to the presence of denatured and non-associated pea globulins at this pH.

Keywords

• pea protein isolate
• egg white protein
• differential scanning calorimetry
• gelling point
• solubility
• coagulation