Surface tension of native and modified plant seed proteins.

The present review, dedicated to Prof. Zbigniew Adamczyk on the occasion of his 70th anniversary, covers the literature data on surface tension and surface compression (dilational) rheology of the adsorbed layers of 21 plant seed proteins (10 leguminous and 11 non-leguminous plants). They are typically analyzed as protein concentrates or isolates, the latter usually obtained by isoelectric precipitation or diafiltration. Despite generally lower solubility, as compared to their animal counterparts (lactoglobulins, caseins, albumins, etc.), the plant seed proteins are also capable of lowering surface tension and forming viscoelastic adsorbed layers. Many seed proteins serve mostly as amino acids reservoirs for the future seedling (storage proteins), hence their instantaneous amphiphilicity is not always sufficient to induce strong adsorption at the aqueous-air interface. They can be, however, conveniently unfolded, hydrolyzed and/or chemically/enzymatically modified to expose more hydrophilic or hydrophobic patches. As shown in numerous contributions reviewed below, the resulting shift of the hydrophilic-lipophilic balance can boost their surface activity to the level comparable to that of many animal proteins or low molecular weight surfactants. An important advantage of the plant seed proteins over the animal ones is their much lower environmental cost and abundance in many plants (e.g. ~40% in sunflower or soybean seeds).