Optimal determination of steric mass action model parameters for beta-lactoglobulin using static batch experiments.

Area of Science:

• Biophysical Chemistry
• Adsorption Science

Background:

• Accurate determination of adsorption isotherms is crucial for understanding protein behavior.
• The steric mass-action (SMA) model offers a framework for adsorption analysis.
• Non-isocratic conditions present challenges in adsorption isotherm determination.

Purpose of the Study:

• To optimally ascertain parameters of the steric mass-action (SMA) formalism for reliable adsorption isotherm determination.
• To investigate the adsorption of beta-lactoglobulin A and B under non-isocratic conditions.
• To validate the SMA model's applicability using static batch experiments.

Main Methods:

• Utilized static batch experiments instead of chromatographic columns.
• Employed a systematic procedure based on optimal model-based experimental design.
• Applied an efficient NLP-solver for parameter determination with a limited number of experiments.

Main Results:

• Successfully determined SMA parameters for reliable adsorption isotherm analysis.
• Corroborated the previously observed anti-Langmuir isotherm shape for beta-lactoglobulin A at low concentrations.
• Identified indications of porosity variation with changing protein concentrations.

Conclusions:

• The optimized SMA model provides a reliable method for determining adsorption isotherms under non-isocratic conditions.
• Static batch experiments combined with model-based design are efficient for parameter ascertainment.
• The study contributes to understanding beta-lactoglobulin adsorption behavior and its dependence on concentration and porosity.