A comparison of the adsorption isotherms of caffeine, theophylline and theobromine and the competitive adsorption of the three compounds on a C18 column were investigated. The experimental parameters of the equilibriu...A comparison of the adsorption isotherms of caffeine, theophylline and theobromine and the competitive adsorption of the three compounds on a C18 column were investigated. The experimental parameters of the equilibrium isotherms were estimated by linear and nonlinear regression analyses. The linear equation as a function of the adsorption concentration of the single compound in its solution and the competitive adsorption of a single compound in a mixed solution were then determined. The adsorption equilibrium data were then correlated to the linear, Langmuir, Freundlich, Langmuir-Freundlich and stoichiometric displacement theory for adsorption（SDT-A） isotherm models. The mixed compounds of the three compounds were competitively adsorbed on the C18 particles. The expression of stoichiometric displacement theory for adsorption was found to be more suitable for adsorption of methylxanthines on a C18 column.展开更多
Based on the fact that the stoichiometric displacement model for retention of solute and the total adsorption free energy of solute on a solid surface can be divided into two components, net adsorption and net desorbe...Based on the fact that the stoichiometric displacement model for retention of solute and the total adsorption free energy of solute on a solid surface can be divided into two components, net adsorption and net desorbed energies, a new principle and an equation for calculating the free energy of protein folding, △△GF, on the solid surface are proposed. With high-performance hydrophobic interaction chromatography (HPHIC), an experimental method for determining the △△GF is established. Lysozyme and a-amylase have been selected as examples to test the new method, and their △△GF on the HPHIC stationary phase surface are found to be much higher than that reported from a solution. In addition, the △△GF of the two proteins are found to increase with the concentration of denaturing agent employed. The average standard deviations,±4.7% for lysozyme and ± 3.0% for a-amylase, indicate that the new method has a satisfactory reproducibility and reliability.展开更多
基金Supported by the Basic Science Research Program Through the National Research Foundation(NRF) of Korea funded by the Ministry of Education, Science and Technology(No.2010-0015731)
文摘A comparison of the adsorption isotherms of caffeine, theophylline and theobromine and the competitive adsorption of the three compounds on a C18 column were investigated. The experimental parameters of the equilibrium isotherms were estimated by linear and nonlinear regression analyses. The linear equation as a function of the adsorption concentration of the single compound in its solution and the competitive adsorption of a single compound in a mixed solution were then determined. The adsorption equilibrium data were then correlated to the linear, Langmuir, Freundlich, Langmuir-Freundlich and stoichiometric displacement theory for adsorption（SDT-A） isotherm models. The mixed compounds of the three compounds were competitively adsorbed on the C18 particles. The expression of stoichiometric displacement theory for adsorption was found to be more suitable for adsorption of methylxanthines on a C18 column.
文摘Based on the fact that the stoichiometric displacement model for retention of solute and the total adsorption free energy of solute on a solid surface can be divided into two components, net adsorption and net desorbed energies, a new principle and an equation for calculating the free energy of protein folding, △△GF, on the solid surface are proposed. With high-performance hydrophobic interaction chromatography (HPHIC), an experimental method for determining the △△GF is established. Lysozyme and a-amylase have been selected as examples to test the new method, and their △△GF on the HPHIC stationary phase surface are found to be much higher than that reported from a solution. In addition, the △△GF of the two proteins are found to increase with the concentration of denaturing agent employed. The average standard deviations,±4.7% for lysozyme and ± 3.0% for a-amylase, indicate that the new method has a satisfactory reproducibility and reliability.
