Functional properties of the α-chain of a major legumin subunit of Pisum sativum legumin

The constituting polypeptides of a heavy pea legumin subunit were separated. The interfacial and emulsifying properties of the α-chains were studied and compared with those of the respective subunit and the native legumin molecules. The α-polypeptides show modified interface behaviour as compared to the legumin. Faster diffusion and higher adsorption barriers during the phase of rearrangement, higher interface coverage in the equilibrium state and improved emulsifying properties were measured.