采用阳离子交换选择性吸附工艺从乳清浓缩物中纯化两种主要蛋白质。

Purification of the two major proteins from whey concentrate using a cation-exchange selective adsorption process.

机构信息

Dept. of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, U.K.

出版信息

Biotechnol Prog. 2010 Jan-Feb;26(1):192-9. doi: 10.1002/btpr.316.

PMID:19927316

Abstract

The packed-bed adsorption and elution of aqueous solutions of whey concentrate powders were investigated at pH 3.7 using a 5-mL SP Sepharose FF column to separate and isolate two major proteins namely, alpha-lactalbumin (ALA) and beta-lactoglobulin (BLG) from these solutions. ALA displaced and eluted BLG from the column in a pure form. Pure ALA could then be eluted with good recovery. A novel consecutive two-stage separation process was developed to separate ALA and BLG from whey concentrate mixtures. Almost all of the BLG in the feed was recovered, with 78% being recovered at 95% purity and a further 20% at 86% purity. In addition, 67% of ALA was recovered, 48% at 54% purity and 19% at 60% purity.

摘要

采用 5mL SP Sepharose FF 柱，在 pH 3.7 下，对乳清浓缩蛋白粉水溶液进行了固定床吸附和解吸研究，以从这些溶液中分离和纯化两种主要蛋白质，即α-乳白蛋白（ALA）和β-乳球蛋白（BLG）。ALA 将 BLG 从柱上置换并洗脱出来，呈纯态。然后可以用良好的回收率洗脱纯 ALA。开发了一种新颖的连续两阶段分离工艺，从乳清浓缩混合物中分离 ALA 和 BLG。进料中几乎所有的 BLG 都被回收，其中 78%以 95%的纯度回收，20%以 86%的纯度回收。此外，回收了 67%的 ALA，其中 48%的纯度为 54%，19%的纯度为 60%。