These observations indicate that the protease substrate specificity leads to different hydrolysate products with specific interactive sites on the surface and
specific molecular masses that improve the ability of the peptide to adsorb to the interface of an immiscible liquid emulsion. Extensive hydrolysis can produce large amounts of free amino acids and short-chain peptides that decrease the emulsifying properties of proteins (Figure 2). By contrast, limited proteolysis exposes hydrophobic and hydrophilic residues, enhances the amphiphilic characteristics of proteins, and improves emulsification [20,30,33,34].