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

Abstract

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.