Binding of substituted phenol and aniline derivatives to the corn protein zein studied by high-performance liquid chromatography

E. Forgács, T. Cserháti, Zdenek Deyl, Ivan Mikšík

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)79-86
Number of pages8
JournalJournal of Chromatography B: Biomedical Sciences and Applications
Volume753
Issue number1
DOIs
Publication statusPublished - Mar 25 2001

Fingerprint

Zein
High performance liquid chromatography
Phenol
Derivatives
Aluminum Oxide
Proteins
Silicon Dioxide
Aminophenols
Electrostatic force
Impregnation
aniline
Water

Keywords

  • Aniline
  • Phenol
  • Zein

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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abstract = "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.",
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T1 - Binding of substituted phenol and aniline derivatives to the corn protein zein studied by high-performance liquid chromatography

AU - Forgács, E.

AU - Cserháti, T.

AU - Deyl, Zdenek

AU - Mikšík, Ivan

PY - 2001/3/25

Y1 - 2001/3/25

N2 - 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.

AB - 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.

KW - Aniline

KW - Phenol

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