The incidence of short episodes of high temperature in the most productive rice growing region is a severe threat for sustainable rice production. Screening for heat tolerance and breeding to increase the heat tolerance of rice is major objective in the situation of recent climate change. Replacing sensitive genotypes with heat tolerant cultivars, modification in sowing time, and use of growth regulators are some of the adaptive strategies for the mitigation of yield reduction by climate change. Different strategies could be adopted to enhance the thermos-tolerance of rice by (1) the modification of agronomic practices i.e., adjusting sowing time or selecting early morning flowering cultivars; (2) induction of acclimation by using growth regulators and fertilizers; (3) selecting the genetically heat resistant cultivars by breeding; and, (4) developing genetic modification. Understanding the differences among the genotypes could be exploited for the identification of traits that are responsible for thermo-tolerance for breeding purpose. The selection of cultivars that flowers in early morning before the increase of temperature, and having larger anthers with long basal pore, higher basal dehiscence, and pollen viability could induce higher thermo-tolerance. Furthermore, the high expression of heat shock proteins could impart thermo-tolerance by protecting structural proteins and enzymes. Thus, these traits could be considered for breeding programs to develop resistant cultivars under a changing climate.

Kunitz-type trypsin inhibitor was first characterized from Enterolobium contortisiliquum (EcTI) (Batista et al., 1996). Plant-based KTIs have shown inhibition of trypsin or chymotrypsin along other serine proteinases such as subtilisin and elastase (Revina et al., 2004; Sumikawa et al., 2006). Some individual KTIs typically have shown more specific activities in comparison to those that inhibit cysteine or aspartic proteinases (Heibges et al., 2003). Kunitz-type trypsin inhibitors are also found in

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Vicilin has nutraceutical potential and different noteworthy medicative health-promoting biotic diversions, and it is remarkable against pathogenic microorganisms and insects. In this study, Vigna aconitifolia vicilin (VacV) has been identified and characterized from the seed of Vigna aconitifolia (Jacq.) Marechal (Moth beans). LC-MS/MS analysis of VacV provided seven random fragmented sequences comprising 238 residues, showing significant homology with already reported Vigna radiata vicilin (VraV). VacV was purified using ammonium sulfate precipitation (60%) followed by size exclusion chromatography on Hi-Load 16/60 Superdex 200 pg column and anion-exchange chromatography (Hi trap Q FF column). Purified VacV showed a major ~50 kDa band and multiple lower bands on 12% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) under both reduced and non-reduced conditions. After all, a three-dimensional molecular structure of VacV was predicted, which showed β-sheeted molecular conformation similar to crystallographic structure of VraV. All Vicilins from V. aconitifolia and other plants were divided into six sub-groups by phylogenetic analysis, and VacV shared a high degree of similarity with vicilins of Vigna radiata, Pisum sativum, Lupinus albus, Cicer arietinum and Glycine max. Additionally, VacV (20 μg) has significant growth inhibition against different pathogenic bacteria along strong antifungal activity (50 μg). Likewise, VacV (3.0 mg) produced significant growth reduction in Rice Weevil Sitophilus oryzae larvae after 9 days compared with control. Furthermore, by using MMT assay, the cytotoxicity effect of VacV on the growth of HepG2 liver cancerous cells was tested. VacV showed cytotoxicity against the HepG-2 line and the acquired value was 180 µg after 48 h. Finally, we performed molecular docking against caspase-3 protein (PDB ID: 3DEI) for VacV bioactive receptor interface residues. Hence, our results reveal that VacV, has nutraceutical potential and moth beans can be used as a rich resource of functional foods.

In comparison to other reported ML-I complexes, we observed distinct differences in the vicinity of the nucleic acid base binding site upon interaction with FC. Therefore, data obtained will provide new insights in understanding the specificity, inhibition, and cytotoxicity of the ML-I A-chain, and related RIPs.