单一和双组分阳离子交换吸附两种纯乳清主要蛋白质。

Single and two-component cation-exchange adsorption of the two pure major whey proteins.

机构信息

Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.

出版信息

J Chromatogr A. 2009 Dec 11;1216(50):8705-11. doi: 10.1016/j.chroma.2009.02.080. Epub 2009 Mar 5.

DOI:10.1016/j.chroma.2009.02.080

PMID:19298967

Abstract

Adsorption of pure alpha-lactalbumin (ALA) and beta-lactoglobulin (BLG) to the cation exchanger SP Sepharose FF was studied at pH 3.7 with the purpose of developing a process for isolating them from whey. Measurement of Langmuir parameters describing adsorption equilibrium in batch experiments and protein breakthrough time values in 1-ml packed-beds at a linear velocity of 158 cm/h and initial concentrations of 3 mg/ml for BLG and 1.5 mg/ml for ALA suggested the feasibility of using this adsorbent to separate the two proteins when present in a mixture. Subsequent experiments with 5-ml columns at the above concentrations and a linear velocity of 30 cm/h confirmed this and showed evidence of competitive adsorption as ALA displaced and eluted all BLG from the column in a pure form, and the remaining ALA could be eluted thereafter at high purity and with 91% recovery.

摘要

研究了在 pH 值为 3.7 时，纯α-乳白蛋白（ALA）和β-乳球蛋白（BLG）在阳离子交换剂 SP Sepharose FF 上的吸附情况，目的是开发一种从乳清中分离它们的方法。在分批实验中测量描述吸附平衡的 Langmuir 参数，以及在 1-ml 填充床中在 158 cm/h 的线性流速和初始浓度为 3 mg/ml 的 BLG 和 1.5 mg/ml 的 ALA 时的蛋白质穿透时间值，表明当两种蛋白质混合存在时，使用这种吸附剂分离它们是可行的。随后在上述浓度和 30 cm/h 的线性流速下进行的 5-ml 柱实验证实了这一点，并显示出竞争吸附的证据，因为 ALA 将所有 BLG 从柱中置换并洗脱出来，呈纯形式，此后可以用 91%的回收率和高纯度洗脱剩余的 ALA。