A one-step anion-exchange chromatography method (NaCl gradient elution on a DEAE Sepharose™ Fast Flow gel column) was developed to purify α-lactalbumin (α-LA) from whey protein isolate. α-LA nearly 100% pure (based on the total protein content) was obtained with a yield of about 39%. Besides pure α-LA, which was the main objective of this work, highly pure β-lactoglobulin was also obtained with a yield of about 59%. The high purity of the obtained α-LA samples allowed its use to synthesise protein nanotubes with excellent gelation properties for their use as food thickeners and bioactive carriers. The samples’ purity degree obtained (based on the total protein content) was critical in the formation of proper nanotubes instead of random aggregates, which produced opaque and weak gels, less useful for food applications.

开发了一种一步式阴离子交换色谱法（在DEAE Sepharose™Fast Flow凝胶柱上进行NaCl梯度洗脱）以从乳清蛋白分离物中纯化α-乳白蛋白（α-LA）。获得了近100％纯度（基于总蛋白质含量）的α-LA，收率约为39％。除了纯α-LA（这项工作的主要目标）外，还获得了高纯度的β-乳球蛋白，产率约为59％。所获得的α-LA样品的高纯度使其可用于合成具有出色凝胶化特性的蛋白质纳米管，以用作食品增稠剂和生物活性载体。获得的样品纯度（基于总蛋白质含量）对于形成适当的纳米管而不是随机聚集体至关重要，纳米管会产生不透明和较弱的凝胶，在食品应用中不太有用。