Effect of salts on the binding of some environmental pollutants to corn protein zein studied by HPLC.

The strength and the character of the binding of 14 organic solvents to the corn protein zein in distilled water and in various salt solutions were determined by preparing zein-coated carbon stationary phase and by measuring the retention characteristics of solvents on a high-performance liquid chromatographic column filled with this stationary phase. The relationship between the physicochemical parameters and binding characteristics of solvents was elucidated by principal component analysis. It was established that various interactive forces are involved in the binding of solvent to the protein, suggesting a mixed binding mechanism. Binding characteristics are equally influenced by the molecular hydrophobicity and by the polarity parameters of the solvent. Coordination numbers, ionization, and lattice energies of the monovalent cations significantly influenced the various aspects of the binding of organic solvents to zein.

Binding of some environmental pollutants to corn protein zein studied by high-performance liquid chromatography.

The strength and the character of the binding of 12 organic solvents to the corn protein zein was determined by preparing zein-coated carbon stationary phase and by measuring the retention of solvents on a high-performance liquid chromatographic column filled with this stationary phase. The relationship between the physicochemical parameters and binding characteristics of solvents was elucidated by principal component analysis. Various interactive forces are involved in the binding of solvent to the protein. The strength of the binding is dominantly influenced by the molecular hydrophobicity while the Gaussian or non-Gaussian distribution of the adsorption strength is markedly dependent on the polarity parameters of the solvent. Sterical correspondences exerted considerable influence on each binding parameter.