Binding of environmental pollutants to the corn protein zein studied by high-performance liquid chromatography.
The interaction of 16 ring-substituted phenols and anilines with the corn protein zein was studied by reversed-phase high-performance liquid chromatography by preparing silica- and alumina-based stationary phases coated with various concentrations of zein. The relationship between the strength of interaction and the physicochemical parameters of solutes was elucidated by principal component analysis followed by the nonlinear mapping technique. The binding of each phenol and aniline derivative to zein has been demonstrated. It was established that the electrostatical parameters of solutes exert the highest influence on the interaction and the involvement of hydrophobic binding forces is of secondary importance. The binding characteristics of phenol and aniline derivatives were different.
Cserháti
Tibor
T
Institute of Chemistry, Chemical Research Centre, Hungarian Academy of Sciences, P.O. Box 17, 1525 Budapest, Hungary.
Forgács
Esther
E
Deyl
Zdenek
Z
Miksik
Ivan
I
Eckhardt
Adam
A
D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D004785:Environmental Pollutants / Q000378:metabolism*; D011485:Protein Binding; D055672:Static Electricity; D003313:Zea mays / Q000378:metabolism*; D015028:Zein / Q000378:metabolism*
D004785:Environmental Pollutants; D015028:Zein