期刊
BIOTECHNOLOGY PROGRESS
卷 32, 期 2, 页码 346-354出版社
WILEY-BLACKWELL
DOI: 10.1002/btpr.2166
关键词
hydrophobic interaction chromatography; mixed salts; dynamic binding capacity; surface tension; aggregation temperature
资金
- German Federal Ministry of Education and Research (BMBF) [0315342B]
Hydrophobic interaction chromatography (HIC) is one of the most frequently used purification methods in downstream processing of biopharmaceuticals. During HIC, salts are the governing additives contributing to binding strength, binding capacity, and protein solubility in the liquid phase. A relatively recent approach to increase the dynamic binding capacity (DBC) of HIC adsorbers is the use of salt mixtures. By mixing chaotropic with kosmotropic salts, the DBC can strongly be influenced. For salt mixtures with a higher proportion of chaotropic than kosmotropic salt, higher DBCs were achieved compared with single salt approaches. By measuring the surface tensions of the protein salt solutions, the cavity theoryproposed by Melander and Horvaththat higher surface tensions lead to higher DBCs, was found to be invalid for salt mixtures. Aggregation temperatures of lysozyme in the salt mixtures, as a degree of hydrophobic forces, were correlated to the DBCs. Measuring the aggregation temperatures has proven to be a fast analytical methodology to estimate the hydrophobic interactions and thus can be used as a measure for an increase or decrease in the DBCs. (c) 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:346-354, 2016
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据