A droplet fractionation method was previously developed to concentrate a dilute nonfoaming protein solution. In that earlier study with invertase, it was demonstrated that droplets created by ultrasonic energy waves could be enriched up to 8 times that of the initial dilute invertase solution. In this study, a mixture of bromelain (a foaming protein) and invertase (a nonfoaming protein) is investigated as a preliminary step to determine if droplet fractionation can also be used to separate a non-foaming protein from foaming proteins. The foaming mixture containing bromelain is first removed by bubbling the binary mixture with air. After the foam is removed, the protein rich air-water interfacial layer is skimmed off (prior to droplet fractionation) so as not to interfere with the subsequent droplet production from the remaining bulk liquid, rich in non-foaming protein. Finally, sonic energy waves are then applied to this residual bulk liquid to recover droplets containing the non-foaming protein, presumed to be invertase. The primary control variable used in this droplet fractionation process is the pH, which ranged for separate experiments between 2 and 9. It was observed that the maximum overall protein partition coefficients of 5 and 4 were achieved at pH 2 and 4, respectively, for the initial foaming experiment followed by the post foaming droplet fractionation experiment.