The results reported in this study are concerned with the effects of pre-he
ating treatments of ovalbumin and lysozyme solutions on the formation, stab
ility and texture morphology of their corresponding foams. It was shown tha
t pre-heating solutions of these proteins to temperatures higher than that
of their thermal denaturation led to an enhanced rate of surface pressure d
evelopment and enhanced foaming properties relative to the unheated protein
s. The effect of pre-heating was more clearly apparent for lysozyme, which
has a higher rigidity than ovalbumin in the native conformational state. Fu
rthermore, the evolution of liquid volume retained in the lysozyme- and ova
lbumin-based foams and foam images during the destabilisation step indicate
d the slowest drainage and the finest, most homogeneous and most stable foa
m texture for foams formed from pre-heated protein solutions. (C) 2000 Soci
ety of Chemical Industry.