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Fractionation of all major and minor whey proteins with radial flow membrane adsorption chromatography at lab and pilot scale

Voswinkel, Linda, Kulozik, Ulrich
International dairy journal 2014 v.39 no.1 pp. 209-214
adsorption, beta-lactoglobulin, binding capacity, blood serum, bovine serum albumin, cations, chromatography, cleaning, fractionation, immunoglobulin G, lactalbumin, lactoferrin, peroxidase, whey, whey protein
A radial flow membrane adsorber system with improved fluid distribution, thereby avoiding high back pressures, was investigated for the complete fractionation of whey proteins. A 50-fold scale-up of the chromatographic separation of all major and minor proteins in acid whey was achieved. The process with anion and cation exchanger membranes consists of two steps. In the first step β-lactoglobulin (β-Lg) and bovine serum albumin are removed. In the second step the minor proteins lactoferrin, lactoperoxidase and immunoglobulin G are isolated and α-lactalbumin remains in the serum phase. The membrane performance over five repeated cycles without cleaning was stable at both scales. The loaded β-Lg equalled the dynamic binding capacity, which was 0.5 mg cm−2 and depletion of β-Lg was 96–99.8%. The yield and purity of the minor whey proteins were consistent at both scales in a range between 80 and 97%, with a concentration factor between 6 and 14.