Effect of pH and salts on the binding of ring-substituted phenol derivatives to the corn protein zein, studied by thin-layer chromatography

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4 Citations (Scopus)

Abstract

The interaction of seven ring-substituted phenol derivatives with the corn protein zein was studied by reversed-phase thin-layer chromatography (RP-TLC) carried out on zein-impregnated cellulose layers, and the effect of pH and salts on the strength and selectivity of the interaction was determined and elucidated by using spectral mapping techniques (SPM) and stepwise regression analysis (SRA). The binding of each phenol derivative to zein has been demonstrated. Calculations proved that the electron withdrawing capacity of substituents and the molecular hydrophobicity of phenol derivatives exert the highest influence on the phenolzein binding indicating the mixed character of the interaction.

Original languageEnglish
Pages (from-to)2303-2313
Number of pages11
JournalJournal of Liquid Chromatography and Related Technologies
Volume26
Issue number14
DOIs
Publication statusPublished - 2003

Fingerprint

Zein
Thin layer chromatography
Thin Layer Chromatography
Phenol
Zea mays
Salts
Derivatives
Proteins
Reverse-Phase Chromatography
Hydrophobicity
Hydrophobic and Hydrophilic Interactions
Regression analysis
Cellulose
Regression Analysis
Electrons

Keywords

  • Phenol derivatives
  • TLC
  • Zein-coated support

ASJC Scopus subject areas

  • Analytical Chemistry
  • Clinical Biochemistry

Cite this

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abstract = "The interaction of seven ring-substituted phenol derivatives with the corn protein zein was studied by reversed-phase thin-layer chromatography (RP-TLC) carried out on zein-impregnated cellulose layers, and the effect of pH and salts on the strength and selectivity of the interaction was determined and elucidated by using spectral mapping techniques (SPM) and stepwise regression analysis (SRA). The binding of each phenol derivative to zein has been demonstrated. Calculations proved that the electron withdrawing capacity of substituents and the molecular hydrophobicity of phenol derivatives exert the highest influence on the phenolzein binding indicating the mixed character of the interaction.",
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T1 - Effect of pH and salts on the binding of ring-substituted phenol derivatives to the corn protein zein, studied by thin-layer chromatography

AU - Cserháti, T.

AU - Forgács, E.

PY - 2003

Y1 - 2003

N2 - The interaction of seven ring-substituted phenol derivatives with the corn protein zein was studied by reversed-phase thin-layer chromatography (RP-TLC) carried out on zein-impregnated cellulose layers, and the effect of pH and salts on the strength and selectivity of the interaction was determined and elucidated by using spectral mapping techniques (SPM) and stepwise regression analysis (SRA). The binding of each phenol derivative to zein has been demonstrated. Calculations proved that the electron withdrawing capacity of substituents and the molecular hydrophobicity of phenol derivatives exert the highest influence on the phenolzein binding indicating the mixed character of the interaction.

AB - The interaction of seven ring-substituted phenol derivatives with the corn protein zein was studied by reversed-phase thin-layer chromatography (RP-TLC) carried out on zein-impregnated cellulose layers, and the effect of pH and salts on the strength and selectivity of the interaction was determined and elucidated by using spectral mapping techniques (SPM) and stepwise regression analysis (SRA). The binding of each phenol derivative to zein has been demonstrated. Calculations proved that the electron withdrawing capacity of substituents and the molecular hydrophobicity of phenol derivatives exert the highest influence on the phenolzein binding indicating the mixed character of the interaction.

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KW - TLC

KW - Zein-coated support

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JO - Journal of Liquid Chromatography and Related Technologies

JF - Journal of Liquid Chromatography and Related Technologies

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