Details

Autor(en) / Beteiligte

• Ng, Paul K
• Snyder, Mark A

Titel

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

Ist Teil von

• Journal of the science of food and agriculture, 2013-10, Vol.93 (13), p.3231-3236

Ort / Verlag

Chichester, UK: John Wiley & Sons, Ltd

Erscheinungsjahr

2013

Quelle

Wiley-Blackwell Journals

Beschreibungen/Notizen

• 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. © 2013 Society of Chemical Industry