Binding of substituted phenol and aniline derivatives to the corn protein zein studied by high-performance liquid chromatography.
The interaction of 12 substituted phenol, three aminophenol and four substituted aniline derivatives with the corn protein zein was studied on zein-coated silica and alumina stationary phases by high-performance liquid chromatography using bidistilled water as mobile phase. Solutes were eluted from the zein-coated supports with different retention times indicating that they bind to the protein with different forces. They were more strongly retained on silica-based than on alumina-based support proving that the original adsorptive character of the support remains even after impregnation. The retention of solutes on both zein-coated stationary phases significantly depended on the steric and electronic parameters of solutes and was independent of the calculated and measured lipophilicity parameters, indicating that hydrophobic forces are not included in the interaction of zein with these class of solutes. It has been concluded that the interaction is governed by steric and electrostatic forces.
Forgács
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Institute of Chemistry, Chemical Research Center, Hungarian Academy of Sciences, Budapest. forgacs@cric.chemres.hu
Cserháti
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T
Deyl
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Z
Miksík
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D000814:Aniline Compounds / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D019800:Phenol / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D003313:Zea mays / Q000737:chemistry*; D015028:Zein / Q000737:chemistry*
D000814:Aniline Compounds; D019800:Phenol; D015028:Zein; C023650:aniline