Calorimetry for studying the adsorption of proteins in hydrophobic interaction chromatography

被引：15
作者：
Rodler, Agnes [1 ,2 ]
Ueberbacher, Rene [1 ]
Beyer, Beate [1 ,2 ]
Jungbauer, Alois [1 ,2 ]
机构：
[1] Univ Nat Resources & Life Sci, Dept Biotechnol, Muthgasse 18, A-1190 Vienna, Austria
[2] Austrian Ctr Ind Biotechnol, Vienna, Austria
来源：
PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY | 2019年 / 49卷 / 01期
关键词：
Hydrophobic interaction chromatography; isotherm behavior; isothermal titration calorimetry; thermodynamic analysis; unfolding; BOVINE SERUM-ALBUMIN; ISOTHERMAL TITRATION CALORIMETRY; POLYPROPYLENE GLYCOL-SEPHAROSE; MIXED ELECTROLYTES; PEGYLATED LYSOZYME; SALT CONCENTRATION; ALPHA-LACTALBUMIN; GLOBULAR-PROTEINS; STATIONARY-PHASE; VANT-HOFF;
D O I：
10.1080/10826068.2018.1487852
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Hydrophobic interaction chromatography is a very popular chromatography method for purification of proteins and plasmids in all scales from analytical to industrial manufacturing. Despite this frequent use, the complex interaction mechanism and the thermodynamic aspects of adsorption in hydrophobic interaction chromatography are still not well understood. Calorimetric methods such as isothermal titration calorimetry and flow calorimetry can help to gain a deeper understanding of the adsorption strength, the influence of salt type and temperature. They can be used to study conformational changes of proteins, which are often associated with the adsorption in hydrophobic interaction chromatography. This review offers a detailed introduction into the thermodynamic fundamentals of adsorption in hydrophobic interaction chromatography with a special focus on the potential applications of isothermal titration calorimetry and flow calorimetry for studying specific problems and relationships of the adsorption behavior of proteins and its various influencing factors. Models for characterizing conformational changes upon adsorption are presented together with methods for assessing this problem for different proteins and stationary phases. All of this knowledge can contribute greatly to forming a sound basis for method development, process optimization and finding modelling strategies in hydrophobic interaction chromatography.
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页码：1 / 20
页数：20
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