Ortín A, Cebrian J A, López-Pérez M J, Johansson G
Department of Biochemistry, University of Lund, Sweden.
Bioseparation. 1991;2(4):197-205.
The partitioning of alpha-lactalbumin and beta-lactoglobulin from bovine whey has been studied in an aqueous poly(ethylene glycol) (PEG)-hydroxypropylstarch two-phase system. The influence of several parameters including concentrations of polymers, sodium phosphate buffer, KSCN, and of PEG palmitate, with and without the presence of Ca2+, on the partitioning of the proteins has been investigated. The separation of the two proteins was demonstrated by counter-current distribution. A purification procedure for both proteins has been developed by using PEG-hydroxypropylstarch two-phase system. This system is compared with the more costly standard system based on PEG and dextran. The possible use of the aqueous two-phase systems for batch extraction for large scale purification of these whey proteins is discussed.
已在聚乙二醇（PEG）-羟丙基淀粉水两相体系中研究了牛血清白蛋白和β-乳球蛋白在牛乳清中的分配情况。研究了包括聚合物浓度、磷酸钠缓冲液、硫氰酸钾以及聚乙二醇棕榈酸酯浓度等几个参数，在有无Ca2+存在的情况下对蛋白质分配的影响。通过逆流分配证明了两种蛋白质的分离。利用PEG-羟丙基淀粉两相体系开发了两种蛋白质的纯化方法。将该体系与基于PEG和葡聚糖的成本更高的标准体系进行了比较。讨论了水两相体系用于大规模纯化这些乳清蛋白的分批萃取的可能性。
