Evaluation of adaptability and stability for iron, zinc and protein content in cowpea genotypes using GGE biplot approach.

Cowpea is a widely cultivated crop in the world. Biofortification strategies aim to reduce mineral and protein deficiencies, especially among the poorest people. The aim of this study was to estimate adaptability and stability of cowpea genotypes for iron, zinc and protein contents, through GGE biplot analysis. Twenty cowpea genotypes were evaluated in the municipalities of Piauí Monsenhor Hipólito, Pio IX and São Miguel do Tapuio, under rainfed conditions. The experimental design was a randomized block design with four replications. The traits evaluated were grain yield, iron, zinc and protein contents in dry grains. Iron (Fe) and zinc (Zn) were determined by flame atomic absorption spectrophotometer, and protein contents by Kjeldahl methods. Adaptability and stability were evaluated by GGE biplot analyses. The means of the experiments were 1,209.1 kg ha-1, 51.1 mg kg-1, 46.8 mg kg-1 and 24.3% for grain yield, Fe, Zn and protein contents, respectively. The joint analysis of variance showed significant difference (p < 0.05) for the effect of interaction genotypes by environments for Fe, Zn and protein contents. The lines G6 and G8 were the most promising for grain yield, mineral and protein content through adaptability and stability by GGE biplot approach.

The resistance of the cowpea cv. BRS Xiquexique to infestation by cowpea weevil is related to the presence of toxic chitin-binding proteins.

The cowpea weevil (Callosobruchus maculatus) is the main pest that attacks cowpea (Vigna unguiculata) seeds during storage, causing nutritional and economic losses in the cowpea crop. Thus, studies aiming to identify resistant cowpea cultivars have been developed. Chitin-binding proteins (CBP), such vicilins and chitinases, have been detected in seeds and related with the toxicity to insects. In this work, we investigated the presence of chitin-binding proteins in the partially resistant cowpea cv. BRS Xiquexique and evaluated their toxicity towards cowpea weevil. The CBP fraction was isolated by chitin affinity chromatography. CBP fraction showed, through 15% SDS PAGE, protein bands with varying molecular masses, mainly below 55 kDa. Proteins present in CBP fraction were identified by Western blotting and mass spectrometry analysis, as vicilins and chitinases. CBP fraction, at 5%, was able to interfere with the development of cowpea weevil, decreasing larval mass and length. A CBV (chitin-binding vicilin) fraction isolated from CBP fraction was toxic, at 2.0%, to C. maculatus, decreasing larval mass and length in 64.3% and 33.23%, respectively. These results suggest that chitin binding proteins, such vicilins and chitinases, may be related to the resistance of cowpea cv. BRS Xiquexique to the infestation by C. maculatus.