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The foam separation of bovine serum proteins was investigated and the protein fractionation by foam separation was analyzed by PAG electrophoresis. The protein concentration for the surface excess formation of bovine serum was in the range of 20-800 ㎍/㎖. At pH 5, the foamate volume was maximum, but the enrichment ratio minimum. As the temperature was elevated, the foamate volume decreased and the enrichment ratio increase. As the gas flow rate increased from 25 to 100 ㎖/min, the foamate volume decreased and the enrichment ratio increased. The enrichment ration became maximum when the added ionic strength of serum solution was in the range of 1-3 by the addition of different types of salts, and this was related to the reduction of surface tension of the solution. In general, BSA, α₁, and α₂-globulins, which have relatively small molecular weight and high hydrophobicity, moved easily to the foam, and the separation of protein fractions in the serum varied with the changes in pH, temperature. gas flow rate and ionic strength of the solution.
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