Purification of β-lactoglobulin with a high-capacity anion exchanger: high-throughput process development and scale-up considerations.

BACKGROUND

β-Lactoglobulin is the most abundant protein in bovine whey. It is a valuable nutriceutical with multiple physiological functions. There are many ongoing efforts to improve approaches by which this whey protein can be conveniently and economically purified in significant quantities. High-capacity resins for protein fractionation are currently available in the biotech industry. One such resin is evaluated in the present investigation.

RESULTS

This work describes a high-capacity ion exchange chromatography method for one-column fractionation of β-lactoglobulin from whey. It was obtained with a >90% purity. The dynamic binding capacity was measured in packed columns. Comparable value predicted on the basis of Langmuir isotherm analysis from batch adsorption data in a high-throughput 96-well format is shown. Scale-up considerations are discussed with respect to feed concentration and binding capacity.

CONCLUSIONS

The feasibility of preparing purified β-lactoglobulin with a single high-capacity anion exchanger step was demonstrated. A capacity of >200 mg mL(-1) was obtained. A significant improvement in productivity can be realized by a simultaneous increase of binding capacity and feed concentration.