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Fractionation of Extracts and Crystalline and Non‐Crystalline Proteins from White Kidney Beans (Phaseolus vulgaris) by Ion‐Exchange High‐Performance Liquid Chromatography
Author(s) -
ALLI I.,
KERMASHA S.,
MEHRAN M.
Publication year - 1990
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1990.tb05228.x
Subject(s) - high performance liquid chromatography , isoelectric point , chromatography , phaseolus , chemistry , ion chromatography , microstructure , ion exchange , citric acid , fractionation , phosphate , elution , ion , biochemistry , botany , biology , organic chemistry , crystallography , enzyme
Sodium hydroxide solution (0.02%) and citric acid solutions (0.08N, pH 5.5, CA1; 0.60N, pH 3.5, CA2) were used to extract proteins from white kidney beans ( Phaseolus vulgaris ). The extracts were subjected to ion‐exchange high performance liquid chromatography (IE‐HPLC) using a phosphate elution buffer (20 mM, pH 7.0). The charge properties of the protein fractions present in the NaOH extract and the CA1 and CA2 extracts were similar although the relative proportion of total peak area represented by each fraction was different in the different extracts. IE‐HPLC of the isoelectric precipitate (amorphous microstructure) isolated from the CA1 (bipyramidal crystalline microstructure) and the CA2 (spheroidal microstructure) extracts indicated striking differences in the charge properties of the proteins which constituted the isolates. IE‐HPLC also demonstrated that the precipitation processes did not affect the charge properties of the proteins which remained after the proteins were recovered from the different extracts.