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The concentration ranges forming surface excess of bovine serum albumin(BSA) and ovalbumin solutions were determined, and the factors affecting the foam separation of BSA were investigated. The surface tension of BSA solution decreased from 72 to 61 dynelcm, when the concentration changed from 5 × 10^(-3) to 3 × 10^(-2)%, and the critical micelle concentration was appeared to be at 0.03% of BSA. At the isoelectric point (pH 4.9) of BSA, the foamate volume was maximum, but enrichment ratio was minimum, resulting in the maximum recovery rate. When the pH deviated from the isoelectric point, the foamate volume decreased and the enrichment ratio increased. The enrichment ratio increased, while the foamate volume decreased drastically as the temperature was elevated above 20℃, resulting in the decrease in recovery rate. As the gas flow rate increased, the enrichment ratio decreased and the foamate volume increased. When (NH₄)₂SO₄ was added, the enrichment ratio decreased, but the maximum foamate was obtained at ionic strength 7. The concentration to form the surface excess of ovlbumin, which has lower surface hydrophobicity than BSA, was 200 times higher than that of BSA. This fact indicates the possibility of selective foam separation by hydrophobicity difference of proteins.
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