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Analytical and preparative separation of whey proteins by chromatofocusing

Authors: R.J. Pearse and R.M. Shanley


In order to obtain separation of the major whey proteins of bovine milk, β-lactoglobulin, α-lactalbumin and serum albumin and the generic variants of β-lactoglobulin in a single step, the technique of chromatofocusing was applied. Excellent separation of these milk components was obtained by this method. The pH values representing the apparent isoelectric points of the whey proteins were: β-lactoglobulin C, 4.66; bovine serum albumin, 4.61; β-lactoglobulin B, 4.55; α-lactalbumin, 4.45; β-lactoglobulin A, 4.36. Chromatofocusing was effective for both analytical and preparative separation of the whey proteins; at least a 1000-fold range of sample size was applicable to the same column system. The separated whey proteins could be recovered by gel filtration on an appropriate medium. Chromatofocusing was shown to be a useful technique for assessing the protein retentiveness of ultrafiltration systems.

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