Process Applications R&D, Process Chromatography Division, Bio-Rad Laboratories, Hercules, CA, 94547, USA.
J Sci Food Agric. 2013 Oct;93(13):3231-6. doi: 10.1002/jsfa.6162. Epub 2013 May 8.
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.
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.
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.
β-乳球蛋白是牛乳中含量最丰富的蛋白质。它是一种具有多种生理功能的有价值的营养物质。目前正在进行许多研究，以改进方便且经济地大量纯化这种乳清蛋白的方法。目前，生物科技行业提供了许多用于蛋白质分级分离的高容量树脂。本研究评估了其中一种树脂。
本工作描述了一种从乳清中单柱分离β-乳球蛋白的高容量离子交换色谱法，可获得纯度 >90%的β-乳球蛋白。在填充柱中测量了动态结合容量。根据高通量 96 孔板中批量吸附数据的 Langmuir 等温线分析预测了相当的数值。讨论了进料浓度和结合容量对放大的影响。
证明了用单一高容量阴离子交换剂一步法制备纯化的β-乳球蛋白是可行的。获得了 >200mg/mL 的容量。通过同时提高结合容量和进料浓度，可以实现生产力的显著提高。
