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

Abstract

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