Abstract
The effects of partial denaturation were investigated on the surface properties of ovalbumin and lysozyme. The surface tension of proteins decreased greatly as denaturation proceeded. The emulsifying and foaming properties of the proteins were remarkably improved by heat denaturation without coagulation. The emulsifying properties of the proteins increased with denaturation, and correlated linearly with surface hydrophobicity. On the other hand, the protein foaming properties incresed with denaturation, correlating curvilinearly with surface hydrophobicity. The foaming power and foam stability of SDS-bound ovalbumin did not improve as much with those of heatdenatured ovalbumin, although surface hydrophobicity increased to the same extent as by heat denaturation. The relationship between the conformation and functionality of proteins is discussed.
