Mechanisms of molecular and structural interactions between lentil and quinoa proteins in aqueous solutions induced by pH recycling

There has been a growing interest in plant proteins due to their beneficial health effects, low cost and variety of applications in food industries. The low solubility of lentil proteins (LPs) is one of the significant factors that limit their use in food applications. Quinoa proteins (QPs), which have high water solubility, were combined with LPs at pH 12 to generate LP-QP complexes to generate pH-based soluble protein compounds. The LP-QP complexes demonstrated a large surface charge with an increase solubilisation of the protein complexes by more than 85%, together with resistance to protein aggregation. The combination of LPs to QPs led to a significant increase (P < 0.05) in unique tertiary and secondary protein structures as determined by the protein–protein interaction (PPI) technique involving pH recycling. Interactions between LPs and QPs affected the surface morphology of the protein complexes formed. Electrostatic interactions, hydrophobic forces and hydrogen bonding were indicated to play key roles in the PPIs. The capacity of pH cycling to illustrate the above protein interactions shows that this is a robust approach for assessing the emulsion and foaming properties of food proteins.