PURITY AND YIELD OF BETA-LACTOGLOBULIN ISOLATED BY AN N-RETINYL-CELITE BIOAFFINITY COLUMN

A bioaffinity column of all-trans-retinal immobilized on Celite was ca pable of isolating high-purity (94.5%) beta-lactoglobulin from bovine acid whey. Conditions far producing a potentially hypoallergenic reduc ed beta-lactoglobulin whey were investigated. Reapplication of pH 5.1 eluate to the column resulted in a final purity of 87% alpha-lactalbum in. The purity of beta-lactoglobulin was slightly lower upon elution w ith buffers containing <0.4 M sodium phosphate, whereas the yield from desorbing buffers <0.1 Ni decreased to approximately 40% of that obta ined with 0.4 M sodium phosphate. Desorption with low phosphate concen tration was improved when pH was increased, suggesting that desorption involves titration of a protophilic group on beta-lactoglobulin. Thes e findings suggest that the retinal matrix shows promise in its applic ation for creating hypoallergenic products and the isolation of high-p urity beta-lactoglobulin with useful functional properties.