| 摘要 |
A method is provided for isolating the proteins, beta -lactoglobulin and alpha -lactalbumin, from whey with a single cation exchanger, and using different pH values for eluting the proteins as separate fractions without using salt elution. A whey protein solution is adjusted to a pH of less than about 4.5. The solution is contacted with a cation exchanger to obtain a bound fraction containing alpha -lactalbumin and beta -lactoglobulin. The bound fraction is adjusted to a pH of about 4.0 to 6.0 and a beta -lactoglobulin fraction is eluted at this pH in the absence of sodium chloride. The pH of an remaining bound fraction is adjusted to about 6.5 or greater and an alpha -lactalbumin fraction is eluted. The method is advantageously conducted at elevated temperatures ranging from 35 DEG C. to 50 DEG C. The ion exchanger may be cross-linked polymeric beads made of cellulose, agarose or dextran, or a microporous polymeric membrane made of regenerated cellulose, polysulfone or cellulose acetate, and may contain charged immobilized molecules such as carboxymethyl or sulfopropyl moieties.
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