Food and Bioprocess Technology

, Volume 5, Issue 2, pp 618–625 | Cite as

Isolation and Characterization of Chickpea (Cicer arietinum L.) Seed Protein Fractions

  • Yu-Wei Chang
  • Inteaz Alli
  • Aline T. Molina
  • Yasuo Konishi
  • Joyce I. Boye
Original Paper


Proteins of ground chickpea seeds were extracted with sodium hydroxide (NaOH) solution and precipitated with addition of acid (isoelectric precipitate (C-IP)) and by cryoprecipitation (cryoprecipitate (C-CP)). The protein isolates were characterized by Native PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), reversed-phase high performance liquid chromatography (RP-HPLC) and electrospray-ionization mass spectrometry (ESI/MS). Both the isoelectric precipitate and cryoprecipitate contained the globulin protein 11S legumins and 7S vicilins as the major protein fractions and 2S albumin proteins as a minor protein fraction. The major subunits of RP-HPLC protein fractions from both cryoprecipitate and isoelectric precipitate were found to contain subunits of both legumins and vicilins. SDS-PAGE identified legumin α-subunits with MW 40.6 and 39.5 kDa and legumin β- subunits with MW 23.5 and 22.5 kDa, and vicilin subunits with MW 70.2, 50.7, 35.0, 33.6, 18.9 and 15.5 kDa. ESI-MS molecular weights 35,366, 35,268 and 14,648 Da are likely vicilin subunits while the 24,894 Da is a legumin β-subunit.


Chickpea protein Cryoprecipitate Isoelectric precipitate Legumin Vicilin ESI-MS 



The authors acknowledge the assistance from Ms. Beata Usakiewicz with ESI-MS analysis.


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Copyright information

© Springer Science + Business Media, LLC 2009

Authors and Affiliations

  • Yu-Wei Chang
    • 1
  • Inteaz Alli
    • 1
  • Aline T. Molina
    • 1
  • Yasuo Konishi
    • 2
  • Joyce I. Boye
    • 3
  1. 1.Department of Food Science and Agricultural ChemistryMcGill UniversitySte-Anne de BellevueCanada
  2. 2.National Research Council of CanadaBiotechnology Research InstituteMontrealCanada
  3. 3.Agriculture and Agri-Food CanadaSaint-HyacintheCanada

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