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Hahn, R; Deinhofer, K; Machold, C; Jungbauer, A.
(2003): Hydrophobic interaction chromatography of proteins. II. Binding capacity, recovery and mass transfer properties.
J Chromatogr B Analyt Technol Biomed Life Sci. 2003; 790(1-2):99-114 FullText FullText_BOKU

Hydrophobic interaction chromatography media suited for large scale separations were compared regarding dynamic binding capacity, recovery and mass transfer properties. In all cases, pore diffusion was the rate limiting step. Reduced heights equivalent to a theoretical plate for bovine serum albumin derived from breakthrough curves at reduced velocities between 60 and 1500 ranged from 10 to 700. Pore diffusion coefficients were derived from pulse response experiments for the model proteins alpha-lactalbumin, lysozyme, P-lactoglobulin, bovine serum albumin and immunoglobulin G. Diffusivity of lysozyme did not follow the trend of decreasing diffusivity with increasing molecular mass, as observed for the rest of the proteins. In general, mass transfer coefficients were smaller compared to ion-exchange chromatography. Dynamic binding capacities for the model protein bovine serum albumin varied within a broad range. However, sorbents based on polymethacrylate showed a lower dynamic capacity than media based on Sepharose. Some sorbents could be clustered regarding binding capacity affected by salt. These sorbents exhibited a disproportional increase of binding capacity with increasing ammonium sulfate concentration. Recovery of proteins above 75% could be observed for all sorbents. Several sorbents showed a recovery close to 100%. (C) 2002 Elsevier Science B.V. All rights reserved.
Authors BOKU Wien:
Hahn Rainer
Jungbauer Alois
Find related publications in this database (using NML MeSH Indexing)
Chromatography, Liquid - methods
Osmolar Concentration - methods
Proteins - chemistry

Find related publications in this database (Keywords)
hydrophobic interaction chromatography
pore diffusion
mass transfer
dynamic capacity
binding studies

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