Impact of pH on molecular structure and surface properties of lentil legumin-like protein and its application as foam stabilizer

Abstract

The capacity of a protein to form and stabilize foams and emulsions depends on its structural characteristics and its physicochemical properties. The structural properties of lentil legumin-like protein including molecular weight, hydrodynamic size, surface charge and hydrophobicity, and conformation were studied in relation to its air–water interfacial behaviors. Kinetics study suggested that the foaming stability was closely related to the surface conformation of the protein that strongly affected adsorption and re-organization of the protein layer at the air–water interface. Foams prepared at neutral pH showed dense and strong networks at the interface, where combination of the α-helix secondary structure, medium hydrodynamic molecular size, and balance between solubility/hydrophobicity all contributed to the formation of such strong protein network at the interface. At pH 5.0, the protein formed a dense and thick network composed of randomly aggregated protein particles at the air–water interface. Whereas at pH 3.0, the unordered structure increased intra-protein flexibility producing a less compact and relaxed interface that reduces elasticity modulus with time and reduced foam resistance against collapse. This research revealed that lentil legumin-like protein could form long-life foams at mild acidic and neutral pH. The potential for use of lentil protein as a novel foaming plant-based stabilizer is demonstrated in food and non-food applications where stable, long-life foams are required.