Current insights on protein behaviour in hydrophobic interaction chromatography

Lienqueo, María Elena; Mahn, Andrea; Salgado, J. Cristian; Asenjo, Juan A.

doi:10.1016/j.jchromb.2006.11.019

Cited by 100 publications

(57 citation statements)

References 93 publications

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“…Since the discovery that the adsorption of biomolecules onto nonpolar adsorbents could be enhanced by high salt concentrations [24], and impaired by high concentrations of nonpolar solvents [25,26], many attempts have been made to explain the hydrophobic phenomena governing HIC and RPC [27]. Earlier suggestions regarding the driving force for adsorption in HIC were based on the gain in entropy when water molecules, arranged around the hydrophobic solute and ligands, are displaced into the less ordered bulk upon adsorption [28,29].…”

Section: Hydrophobic Effects In Hic and Rpcmentioning

confidence: 99%

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Combined effects of potassium chloride and ethanol as mobile phase modulators on hydrophobic interaction and reversed-phase chromatography of three insulin variants

Johansson

Frederiksen

Degerman

et al. 2015

Journal of Chromatography A

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Section: Hydrophobic Effects In Hic and Rpcmentioning

confidence: 99%

“…This adaptation of the solvophobic theory is probably the most well-known and widely used theory to describe the hydrophobic effects in chromatography [31][32][33][34]. However, it has been shown that the effect of salts on protein retention cannot be explained by their effect on surface tension alone [20,22,27,35].…”

Section: Hydrophobic Effects In Hic and Rpcmentioning

confidence: 99%

Combined effects of potassium chloride and ethanol as mobile phase modulators on hydrophobic interaction and reversed-phase chromatography of three insulin variants

Johansson

Frederiksen

Degerman

et al. 2015

Journal of Chromatography A

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“…This model is governed by a set of mass-balance partial differential equations (PDEs), with a modified Langmuir isotherm and experimentally validated kinetics. In this regard, the advantages of this robust optimal control framework are highlighted through the solution of a challenging ternary mixture separation problem, with human insulin (insulin aspart, desB30 insulin and insulin methyl ester) and the intermediately eluting component as the target, for a hydrophobic interaction chromatography (HIC) [26,27] system. The proposed model-based methodology for robust optimal control implies formulating and solving a large-scale dynamic optimization problem (DOP) constrained by PDEs [28].…”

Section: Pde-constrained Dynamic Optimizationmentioning

confidence: 99%

Methods and Tools for Robust Optimal Control of Batch Chromatographic Separation Processes

et al. 2015

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This contribution concerns the development of generic methods and tools for robust optimal control of high-pressure liquid chromatographic separation processes. The proposed methodology exploits a deterministic robust formulation, that employs a linearization of the uncertainty set, based on Lyapunov differential equations to generate optimal elution trajectories in the presence of uncertainty. Computational tractability is obtained by casting the robust counterpart problem in the framework of bilevel optimal control where the upper level concerns forward simulation of the Lyapunov differential equation, and the nominal open-loop optimal control problem augmented with the robustified target component purity inequality constraint margin is considered in the lower level. The lower-level open-loop optimal control problem, constrained by spatially discretized partial differential equations, is transcribed into a finite dimensional nonlinear program using direct collocation, which is then solved by a primal-dual interior point method. The advantages of the robustification strategy are highlighted through the solution of a challenging ternary complex mixture separation problem for a hydrophobic interaction chromatography system. The study shows that penalizing the changes in the zero-order hold control gives optimal solutions with low sensitivity to uncertainty. A key result is that the robustified general elution trajectories outperformed the conventional linear trajectories both in terms of recovery yield and robustness.

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“…Several retention mechanisms for proteins in HIC have been reported and recently reviewed by Lienqueo et al [98]. The SDT-R for HIC considers eight molecular interactions including three conformational changes in proteins [50].…”

Section: Hydrophobic Interaction Chromatographymentioning

confidence: 99%

“…This yielded 1.4-2.0 mg/100 g of wet tissue and 0.7-1.0 mg/100 mL of bacterial culture. Lienqueo et al [103] recently reviewed the current insights into protein behaviour in HIC including the retention mechanism for molecular interactions in HIC.…”

Section: Hydrophobic Interaction Chromatographymentioning

confidence: 99%