The reason why egg white shows such good foaming properties is the fact that it contains a mixture of different proteins. These proteins all possess different physical properties and thus, all contribute with different functionality in the formation and stabilization of foams. Ovalbumin, which is the most abundant protein in the egg albumen, is heat sensitive and denatures easily if heated. When heat-treated and denaturated, ovalbumin form foams easily in the presence of other proteins in the albumen. If alone, the whipping time for obtaining foams is longer (MacDonell 1955, as cited in Stadelman and Cotterill 1995, p. 420).Globulins (G2 and G3) enhance the initial formation of foams by lowering the surface tension (MacDonell 1955, as cited in Stadelman and Cotterill 1995, p. 420). Sauter and Montoure (1972) investigated the role of lysozyme (G1 globulin) in egg white foaming. The results showed that lysozyme improves foam volume. Additionally the results showed that egg white with a higher amount of lysozyme produced more voluminous foams that those with a minor content of the globulin. Concerning the FC, a study done by Wong and Kitts (2003) showed that dried egg white had a greater foaming capacity than SPI, while other studies shows that there are no difference in foaming capacity between the two. McWatters and Cherry (1997) reported that soy protein was able to form very thick foams (at all pH tested, accept pH 4) that resembled of egg white foams.