Saufi Syed M, Fee Conan J
Department of Chemical and Process Engineering, University of Canterbury, Private Bag 4800, Christchurch, New Zealand.
Biotechnol Bioeng. 2009 May 1;103(1):138-47. doi: 10.1002/bit.22239.
Mixed matrix membranes (MMMs), which incorporate adsorptive particles during membrane casting, can be prepared simply and have performances that are competitive with other membrane chromatography materials. The application of MMM chromatography for fractionation of beta-Lactoglobulin from bovine whey is described in this article. MMM chromatography was prepared using ethylene vinyl alcohol polymer and lewatit anion exchange resin to form a flat sheet membrane. The membrane was characterized in terms of structure and its static and dynamic binding capacities were measured. The optimum binding for beta-Lactoglobulin was found to be at pH 6.0 using 20 mM sodium phosphate buffer. The MMM had a static binding capacity of 120 mg/g membrane (36 mg/mL membrane) and 90 mg/g membrane (27 mg/mL membrane) for beta-Lactoglobulin and alpha-Lactalbumin, respectively. In batch fractionation of whey, the MMM showed selective binding towards beta-Lactoglobulin compared to other proteins. The dynamic binding capacity of beta-Lactoglobulin in whey solution was about 80 mg/g membrane (24 mg beta-Lac/mL of MMM), which is promising for whey fractionation using this technology. This is the first reported application of MMM chromatography to a dairy feed stream.
混合基质膜（MMMs）是在制膜过程中加入吸附性颗粒制成的，制备方法简单，其性能可与其他膜色谱材料相媲美。本文介绍了MMM色谱法在从牛乳清中分离β-乳球蛋白的应用。采用乙烯-乙烯醇共聚物和Lewatit阴离子交换树脂制备了平板状MMM色谱膜，并对其结构进行了表征，测定了其静态和动态结合容量。结果发现，使用20 mM磷酸钠缓冲液时，β-乳球蛋白的最佳结合pH值为6.0。该MMM对β-乳球蛋白和α-乳白蛋白的静态结合容量分别为120 mg/g膜（36 mg/mL膜）和90 mg/g膜（27 mg/mL膜）。在乳清的分批分离中，与其他蛋白质相比，MMM对β-乳球蛋白表现出选择性结合。乳清溶液中β-乳球蛋白的动态结合容量约为80 mg/g膜（24 mg β-乳球蛋白/mL MMM），这表明该技术用于乳清分离具有良好前景。这是首次报道MMM色谱法应用于乳制品进料流。
