After model calibration from chromatograms of bind-and-elute experiments, results were validated with batch isotherms and prediction of further gradient elution chromatograms. The model's capability of describing column chromatography experiments is demonstrated with glucose oxidase, bovine serum albumin (BSA), and lysozyme on Capto™ Phenyl (high sub) as model system. Capto Phenyl (high sub) is an excellent choice for initial and intermediate step purifications requiring a chromatography medium with medium to high. 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. Higher flow rates can, however, be used with Capto Phenyl ImpRes, while the. 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. The selectivity is similar to that of Phenyl Sepharose 6 Fast. Modeling and simulation of hydrophobic interaction chromatography (HIC) in the column mode has been seldom reported. Capto Phenyl and Capto Butyl are intended for the capture and intermediate stages of protein purication.

After removal of storage solution from the filter plate by applying a vacuum of 300 mbar, the adsorber resin was washed five times with 250 L UPW per well.

Mechanistic models are successfully used for protein purification process development as shown for ion-exchange column chromatography (IEX). Aug- Capto Phenyl (high sub) and Capto Butyl media extend GE Healthcare’s hydrophobic interaction chromatography (HIC) portfolio to offer a wide range of hydrophobicity for screening and purification. The preparation of aliquots from Capto Phenyl (high sub) suspension was conducted by using the vacuum manifold device ResiQuot.

Capto phenyl high sub