Article ID Journal Published Year Pages File Type
4562141 Food Research International 2011 11 Pages PDF
Abstract

Albumin, globulin and glutelin fractions were prepared from chickpea and oat seeds using sequential extractions. Molecular characteristics of individual protein fractions were investigated using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) in combination with proteomic techniques. SDS-PAGE results revealed that chickpea albumin and globulin fractions (C-Ab and C-Gb) showed protein bands with molecular weights (MWs) related to subunits of legumin (11S globulin) and pea vicilin (7S globulin); oat protein fractions (O-Ab, O-Gb and O-Gt) showed most protein bands with MWs related to subunits of oat 12S globulin (avenalin). With proteomic analysis, eighteen tryptic peptides from chickpea globulin fraction showed sequence homology that corresponded to chickpea legumin α- and β-subunit (NCBI accession number: gi|6273402; theoretical mass 56,216 Da) while sixteen tryptic peptides from chickpea albumin fraction (C-Ab) were identified as chickpea provicilin precursor (NCBI accession number: gi|82173888; theoretical mass 51,390 Da); fifteen tryptic peptides from oat protein fractions were identified with origin from oat 12S seed storage globulin 1 (NCBI accession number: gi|134918; theoretical mass 58,508 Da). The identified tryptic peptide, ALIVPQNFAIAAK, was commonly found in chickpea glutelin fraction (C-Gt), rice glutelin fraction (R-Gt), and oat albumin, globulin and glutelin fractions (O-Ab, O-Gb and O-Gt).

► Albumin, globulin and glutelin fractions from chickpea and oat seeds were characterized using proteomic techniques. ► 18 tryptic peptides from chickpea globulin fraction corresponded to sequenced chickpea legumin. ► 16 tryptic peptides from chickpea albumin fraction identified as sequenced chickpea provicilin precursor. ► 15 tryptic peptides from oat protein fractions identified as sequenced oat 12S seed storage globulin 1. ► The tryptic peptide, ALIVPQNFAIAAK, was commonly found in chickpea, rice and oat protein fractions.

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Life Sciences Agricultural and Biological Sciences Food Science
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