Fractionation of β-lactoglubulin (β-lg) and α-lactalbumin (α-la) using conventional separation technologies remains challenging mainly due to similar molecular weight. Herein, casein (CN) was used as ligand protein to specifically aggregate β-lg under high hydrostatic pressure (HHP) in order to separate α-la after acidification to pH 4.6. Specifically, we studied the effect of different concentration of CN on α-la purity and recovery. Model solutions of α-la, β-lg and CN (from 0 to 5 mg/mL) were pressurized (600 MPa–5 min). After acidification and centrifugation of pressure-treated solutions, purity of α-la was increased up to 78% with a recovery of 88% for solution without CN. In contrast with our initial hypothesis, the presence of CN decreased β-lg pressure-induced aggregation and co-precipitation upon acidification and significantly reduced purity (∼71%). Therefore, our results suggest a chaperone-like activity of CN on β-lg pressure-induced aggregation which needs further investigation.

主要由于分子量相似，使用常规分离技术分离β-乳球蛋白（β-lg）和α-乳白蛋白（α-la）仍然具有挑战性。在此，酪蛋白（CN）用作配体蛋白以在高静水压（HHP）下特异性聚集β-Ig，以便在酸化至pH 4.6后分离α-Ia。具体而言，我们研究了不同浓度的CN对α-1a纯度和回收率的影响。对α-la，β-lg和CN（0至5 mg / mL）的模型溶液加压（600 MPa–5分钟）。在酸化和离心处理过的溶液后，α-la的纯度提高到78％，而不含CN的溶液的回收率达到88％。与我们最初的假设相反，CN的存在会降低β-lg压力诱导的酸化后的聚集和共沉淀，并显着降低纯度（约71％）。因此，我们的结果表明CN对β-lg压力诱导的聚集的伴侣状活性，这需要进一步研究。