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.

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