Isolation of Immunoglobulins by Competitive Displacement of Cheese Whey Proteins During Metal Chelate Interaction Chromatography

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Abstract
Metal chelate interaction chromatography can efficiently recover Ig found in low concentrations in cheese whey. High capacity and purity and recovered Ig resulted from competitive displacment of less tightly bound proteins during whey application. The strength of interaction, i.e., order of displacement, of proteins in Cheddar cheese whey was: .beta.-lactoglobulin, .alpha.-lactalbumin, bovine serum albumin, lactoperoxidase-lactoferrin, and Ig. Tandem column operation enabled maximal utilization of column capacity for Ig. About 100 mg Ig (75 to 95% purity) could be recovered per milliliter of Cu-charged bed volume or 2.5 ml of total bed volume. Proteins in the unbound whey fractions from this chromatographic process retained good emulsifying activity.