疏水性相互作用色谱法分离和回收乳清蛋白。
Fractionation and recovery of whey proteins by hydrophobic interaction chromatography.
机构信息
IBB-Institute for Biotechnology and Bioengineering, Centre of Biological Engineering, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal.
出版信息
J Chromatogr B Analyt Technol Biomed Life Sci. 2011 Mar 1;879(7-8):475-9. doi: 10.1016/j.jchromb.2011.01.003. Epub 2011 Jan 13.
A method for the recovery and fractionation of whey proteins from a whey protein concentrate (80%, w/w) by hydrophobic interaction chromatography is proposed. Standard proteins and WPC 80 dissolved in phosphate buffer with ammonium sulfate 1 M were loaded in a HiPrep Octyl Sepharose FF column coupled to a fast protein liquid chromatography (FPLC) system and eluted by decreasing the ionic strength of the buffer using a salt gradient. The results showed that the most hydrophobic protein from whey is α-lactalbumin and the less hydrophobic is lactoferrin. It was possible to recover 45.2% of β-lactoglobulin using the HiPrep Octyl Sepharose FF column from the whey protein concentrate mixture with 99.6% purity on total protein basis.
提出了一种从乳清蛋白浓缩物（80%，w/w）中通过疏水相互作用色谱法回收和分级乳清蛋白的方法。标准蛋白质和溶解在含 1 M 硫酸铵的磷酸盐缓冲液中的 WPC80 加载到与快速蛋白质液相色谱（FPLC）系统相连的 HiPrep 辛基琼脂糖 FF 柱上，并通过使用盐梯度降低缓冲液的离子强度进行洗脱。结果表明，乳清中最疏水的蛋白质是α-乳白蛋白，其次是乳铁蛋白。使用 HiPrep 辛基琼脂糖 FF 柱从乳清蛋白浓缩物混合物中回收β-乳球蛋白的产率为 45.2%，总蛋白纯度为 99.6%。
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