Large-scale preparation of β-lactoglobulin A and B by ultrafiltration and ion-exchange chromatography
Large-scale preparation of β-lactoglobulin A and B by ultrafiltration and ion-exchange chromatography
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DOI：
10.1016/s0958-6946(98)00028-4
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发表时间：
1998-02-01
影响因子：
3.1
通讯作者：
Qvist, KB
中科院分区：
文献类型：
--
作者：
Kristiansen, KR;Otte, J;Qvist, KB
在非常温和的条件下，采用超滤和阴离子交换色谱法纯化β -乳球蛋白A和B；在过程的任何一步，温度和pH值分别不超过50摄氏度和7.0。新鲜。使用β -乳球蛋白A或B纯合子奶牛的原料奶。干物质蛋白含量分别为96.3、97.1和97.2%的β -乳球蛋白B和β -乳球蛋白A分别为485和125 g和460 g。通过在pH值为4和接近中性的pH下进行超滤和滤，获得了不同钙含量的产品。这些产品含有很少的脂肪。电喷雾质谱分析结果表明，产品中含有少量单乳糖化β -乳球蛋白。动态光散射结果表明，三种制剂中蛋白质的粒径分别为98、99.8%和99.8%，水动力半径均为3.5 nm，与β -乳球蛋白单体相对应。1998爱思唯尔科学有限公司版权所有。
Purification of beta-lactoglobulin A and B was carried out by ultrafiltration and anion-exchange chromatography under very gentle conditions; temperature and pH did not exceed 50 degrees C and 7.0, respectively, at any step of the process. Fresh. raw milk from cows homozygotic in beta-lactoglobuiin A or B was used. Two batches of beta-lactoglobulin B, 485 and 125 g, and one batch of beta-lactoglobulin A, 460 g, was produced with 96.3, 97.1 and 97.2% protein in dry matter, respectively. By performing ultrafiltration and diafiltration at pH 4 versus near neutral pH products with varying calcium contents were acheived. The products contained very little fat. Electrospray mass spectrometry showed that the products contained a small amount of mono lactosylated beta-lactoglobulin. Dynamic light scattering showed the particle size of 98, 99.8 and 99.8% of the protein in the three preparations to be with a hydrodynamic radius of 3.5 nm, which corresponds to the beta-lactoglobulin monomer. (C) 1998 Elsevier Science Ltd. All rights reserved.