期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1465, 期 -, 页码 71-78出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.chroma.2016.07.085
关键词
Protein purification; Hydrophobic interaction chromatography; Mechanistic modeling; Isotherm; Water structure
资金
- Ministry of Science, Research and the Arts Baden-Wurttemberg (MWK)
Mechanistic models are successfully used for protein purification process development as shown for ion-exchange column chromatography (IEX). Modeling and simulation of hydrophobic interaction chromatography (HIC) in the column mode has been seldom reported. As a combination of these two techniques is often encountered in biopharmaceutical purification steps, accurate modeling of protein adsorption in HIC is a core issue for applying holistic model-based process development, especially in the light of the Quality by Design (QbD) approach. In this work, a new mechanistic isotherm model for HIC is derived by consideration of an equilibrium between well-ordered water molecules and bulk-like ordered water molecules on the hydrophobic surfaces of protein and ligand. The model's capability of describing column chromatography experiments is demonstrated with glucose oxidase, bovine serum albumin (BSA), and lysozyme on Capto (TM) Phenyl (high sub) as model system. After model calibration from chromatograms of bind-and-elute experiments, results were validated with batch isotherms and prediction of further gradient elution chromatograms. (C) 2016 Elsevier B.V. All rights reserved.
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