Unravelling the nutriproteomics of chickpea (Cicer arietinum) seeds

被引:0
|
作者
Santos, Tiago [1 ,2 ]
Marinho, Catarina [1 ,2 ]
Freitas, Michael [1 ,2 ]
Santos, Hugo M. [3 ,4 ]
Oppolzer, David [5 ]
Barros, Ana [5 ]
Carnide, Valdemar [1 ,5 ]
Igrejas, Gilberto [1 ,2 ,3 ]
机构
[1] Univ Tras Os Montes & Alto Douro, Dept Genet & Biotechnol, Vila Real, Portugal
[2] Univ Tras Os Montes & Alto Douro, Funct Genom & Prote Unit, Vila Real, Portugal
[3] Nova Univ Lisbon, UCIBIO REQUIMTE, Caparica, Portugal
[4] Univ Nova Lisboa, Fac Sci & Technol, ProteoMass Sci Soc, Caparica, Portugal
[5] Univ Tras Os Montes & Alto Douro, Ctr Res & Technol Agroenvironm & Biol Sci, Vila Real, Portugal
来源
CROP & PASTURE SCIENCE | 2017年 / 68卷 / 10-11期
关键词
MALDI-TOF MS; seed proteins; SDS-PAGE; two-dimensional electrophoresis; DRAFT GENOME SEQUENCE; 2-DIMENSIONAL ELECTROPHORESIS; NUTRITIONAL QUALITY; L; PROTEOMICS; PROTEINS; IMPROVEMENT; WATER; MATURATION; TOLERANCE;
D O I
10.1071/CP17307
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
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.
引用
收藏
页码:1041 / 1051
页数:11
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