Abstract The interest in individual whey protein fractions, especially the main proteins α-lactalbumin and β-lactoglobulin, has been growing due to their unique nutritional value and their exceptional technofunctional properties. Various fractionation and purification methods have been published. However, none of them achieved highest purity, maximal recovery, and transferability to industrial scale. This study used thermal treatment for selective aggregation of β-lactoglobulin, which was subsequently separated in a pilot-scale decanter centrifuge from the α-lactalbumin-enriched centrate. The aim was to investigate if the centrifugal separation can be improved by pH-induced flocculation of the aggregates compared with non-flocculated suspensions at pH 7.0. With various analytical methods, it was demonstrated that the strongest flocculation occurred at pH 4.4 and facilitated separation of aggregate fragments sized below 20 μm. Finally, separation efficiencies of more than 99% were achieved by aggregate flocculation in the pilot-scale decanter even at low centrifugal forces.

中文翻译：

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在卧螺离心机中以优化的产量分离聚集的 β-乳球蛋白

摘要 由于其独特的营养价值和卓越的技术功能特性，人们对个别乳清蛋白组分，尤其是主要蛋白质 α-乳清蛋白和 β-乳球蛋白的兴趣一直在增长。已经发表了各种分馏和纯化方法。然而，它们都没有达到最高纯度、最大回收率和可转移到工业规模。本研究使用热处理来选择性聚集 β-乳球蛋白，随后在中试规模的卧螺离心机中将其从富含 α-乳清蛋白的离心液中分离出来。目的是研究与 pH 7.0 的非絮凝悬浮液相比，是否可以通过 pH 诱导的聚集体絮凝来改善离心分离。通过各种分析方法，结果表明，最强的絮凝发生在 pH 4.4 时，有助于分离尺寸低于 20 μm 的聚集体碎片。最后，即使在低离心力下，通过中试规模滗析器中的聚集体絮凝也实现了超过 99% 的分离效率。