Unravelling the nutriproteomics of chickpea (Cicer arietinum) seeds
Tiago Santos A B , Catarina Marinho A B , Michael Freitas A B , Hugo M. Santos C D , David Oppolzer E , Ana Barros E , Valdemar Carnide A E and Gilberto Igrejas A B C FA Department of Genetics and Biotechnology, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal.
B Functional Genomics and Proteomics Unit, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal.
C UCIBIO-REQUIMTE, Nova University of Lisbon, Caparica, Portugal.
D ProteoMass Scientific Society, Faculty of Sciences and Technology, University Nova of Lisbon, Caparica, Portugal.
E Centre for the Research and Technology of Agro-Environmental and Biological Sciences, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal.
F Corresponding author. Email: gigrejas@utad.pt
Crop and Pasture Science 68(11) 1041-1051 https://doi.org/10.1071/CP17307
Submitted: 14 February 2017 Accepted: 25 October 2017 Published: 21 November 2017
Abstract
Chickpea (Cicer arietinum L.) is an essential grain for human consumption owing to its high protein content, nutritional quality and energy-efficient production. The aim of this study was to compare the protein extracts of 24 chickpea genotypes by biochemically characterising the storage proteins. The storage protein content was characterised by protein separation with polyacrylamide gel electrophoresis and visualisation of the banding patterns, which revealed considerable genetic variability within and between genotypes in this chickpea collection. High performance liquid chromatography showed that all genotypes had balanced amino acid content and some were rich in seven amino acids. Two chickpea genotypes, Flip97-171C and Elite, representative of the kabuli and desi types, respectively, were chosen for total proteome analysis. Two-dimensional electrophoresis and subsequent mass spectrometry were used to identify 454 protein spots from the Flip97-171C and Elite proteomes. By using Mascot Server software, 37% of the spots were identified as 47 different proteins involved in a large range of metabolic functions. Most proteins from both proteomes were assigned to nutritional storage activity. Chickpea proteome analysis is essential in reaffirming the quality of this grain protein for human nutrition, and will be important in future nutriproteomics and plant-breeding studies.
Additional keywords: MALDI-TOF MS, seed proteins, SDS-PAGE, two-dimensional electrophoresis.
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