Proteins were isolated from chickpea flour by micellization and isoelectric precipitation techniques. Protein content ranged from 84.8‐87.8%. Denaturation temperature and transition enthalpy, by differential scanning calorimetry, were higher for micelle than for isoelectric proteins. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis showed a molecular weight distribution between 16.6‐66.4 kD for micelle and 14.9‐84.2 kD for isoelectric proteins. Most functional properties compared favorably to a commercial soy isolate. In general, most essential amino acids of chickpea isolates were at acceptable levels compared to a reference pattern. High values of in vitro digestibility and calculated PER were obtained for the isolates.
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Paredes‐López et al. (1991) studied this question.
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