Ovalbumin is a globular protein. When it is denatured, it can produce
molecular species with different conformational states, each of
which has different adsorption properties at a gas–liquid interface.
Such changes in adsorption can then affect the foaming behaviors
of ovalbumin. Results of semi-batch foam fractionation of both
native and denatured ovalbumin aqueous solutions are reported
in this paper, along with possible relationships between denaturation
and foam fractionation outcomes, such as the enrichment
ratio and mass recovery. Bubble size and foam stability are determined
in the experiments to show the effect of denaturation on
these measured parameters in this system. The relationships between
the bubble size, void fraction, and ovalbumin enrichment
are also reported to reflect the effect of the presence of denatured
species.