Chickpea Protein Isolates: Physicochemical, Functional and Nutritional Characterization

Authors

  • O. PAREDES-LÓPEZ,

    1. Authors Paredes-López and Olivares-Vázquez are with Unidad Irapuato, Centro de Investigación y de Estudios Avanzados- IPN, Apdo. Postal 629, 36500 Irapuato, Gto., México. Author Ordorica-Falomir's present address: Escuela de Ciencias Químico-Biológicas, Universidad Aut. de Sinaloa, Culiacán, Sin., México.
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  • C. ORDORICA-FALOMIR,

    1. Authors Paredes-López and Olivares-Vázquez are with Unidad Irapuato, Centro de Investigación y de Estudios Avanzados- IPN, Apdo. Postal 629, 36500 Irapuato, Gto., México. Author Ordorica-Falomir's present address: Escuela de Ciencias Químico-Biológicas, Universidad Aut. de Sinaloa, Culiacán, Sin., México.
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  • M.R. OLIVARES-VÁZQUEZ

    1. Authors Paredes-López and Olivares-Vázquez are with Unidad Irapuato, Centro de Investigación y de Estudios Avanzados- IPN, Apdo. Postal 629, 36500 Irapuato, Gto., México. Author Ordorica-Falomir's present address: Escuela de Ciencias Químico-Biológicas, Universidad Aut. de Sinaloa, Culiacán, Sin., México.
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  • This research was supported by Consejo National de Ciencia y Tecnología (CONACYT-México) and the European Economic Community.

ABSTRACT

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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