Department of Biochemistry, University of Otago, Dunedin, New Zealand.
Department of Food Science, University of Otago, Dunedin, New Zealand.
Food Chem. 2016 Jul 15;203:165-174. doi: 10.1016/j.foodchem.2016.02.065. Epub 2016 Feb 10.
This study reports a procedure for the simultaneous purification of glyco(caseino)macropeptide, immunoglobulin, lactoperoxidase, lactoferrin, α-lactalbumin and β-lactoglobulin from sheep cheese sweet whey, an under-utilized by-product of cheese manufacture generated by an emerging sheep dairy industry in New Zealand. These proteins have recognized value in the nutrition, biomedical and health-promoting supplements industries. A sequential fractionation procedure using economical anion and cation exchange chromatography on HiTrap resins was evaluated. The whey protein fractionation is performed under mild conditions, requires only the adjustment of pH between ion exchange chromatography steps, does not require buffer exchange and uses minimal amounts of chemicals. The purity of the whey protein fractions generated were analyzed by reversed phase-high performance liquid chromatography and the identity of the proteins was confirmed by mass spectrometry. This scalable procedure demonstrates that several proteins of recognized value can be fractionated in reasonable yield and purity from sheep cheese whey in one streamlined process.
本研究报告了一种从绵羊奶酪甜乳清中同时纯化糖巨肽（酪蛋白）、免疫球蛋白、乳过氧化物酶、乳铁蛋白、α-乳白蛋白和β-乳球蛋白的方法，这是奶酪生产过程中新兴绵羊奶制品产业产生的一种未充分利用的副产品。这些蛋白质在营养、生物医学和促进健康的补充剂行业具有公认的价值。评估了使用 HiTrap 树脂进行经济的阴离子和阳离子交换层析的顺序分级程序。乳清蛋白分级在温和的条件下进行，仅需要在离子交换层析步骤之间调整 pH 值，不需要缓冲液交换，并且使用的化学品量最少。通过反相高效液相色谱法分析了乳清蛋白级分的纯度，并通过质谱法确认了蛋白质的身份。这种可扩展的程序表明，可以在一个简化的过程中从绵羊奶酪乳清中以合理的产率和纯度分离出几种具有公认价值的蛋白质。
