Role of pulse globulins and albumins in air-water interface and foam stabilization

Pulse protein isolates are promising substitutes for animal protein in foam preparation, but they typically are complex mixtures of multiple proteins, and the contribution of the individual proteins to the behavior of the mixture in air-water interface stabilization is largely unknown. The major protein fractions in isolates are the globulins and albumins, and this study systematically investigated the molecular properties, and interfacial and foaming properties of these two fractions for three different pulses: lentils, faba beans and chickpeas. The key parameters of these pulse proteins in air-water interface and foam stabilization were investigated by correlation analysis. Based on this, low denaturation enthalpy tends to result in both high foamability and foam stability, most likely due to a greater conformational flexibility that allows for a faster adsorption to the air-water interface, and higher degree of structural rearrangement at the interface, which increases interfacial network stiffness. For globulin-rich pulse protein fractions, vicilins and convicilins tend to introduce high surface hydrophobicity, which increases the affinity of the proteins for the interface, and increases protein-protein in-plane interactions through hydrophobic interactions, resulting in the enhancement of interfacial network connectivity and the level of network branching. These factors increase the interfacial resistance to large deformations and increase foam stability. Vicilins and convicilins also tend to have a high value of the surface charge and further promote foam stability by increasing electrostatic repulsion between air bubbles. Legumins tend to reduce foamability since they adsorb to the air-water interface slowly and tend to disrupt the interfacial network structure. These findings provide deeper insights in the role of pulse globulins and albumins in air-water interface and foam stabilization. The proposed key parameters will benefit the predictability of the interfacial and foaming behavior of pulse proteins.