Isolation and characterization of chickpea (Cicer arietinum L.) seed protein fractions

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DOIResolve DOI: http://doi.org/10.1007/s11947-009-0303-y
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TypeArticle
Journal titleFood Bioprocess Technology
Volume5
Issue2
Pages618625; # of pages: 8
Subjectchickpea protein; cryoprecipitate; isoelectric precipitate; legumin; vicilin; ESI-MS
AbstractProteins 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 withMW70.2, 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.
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedYes
NRC number53179
NPARC number20548173
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Record identifier525faf78-4c43-4571-aca6-afae2c6fe8a2
Record created2012-08-28
Record modified2016-05-09
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