The Design Development of Solar Box Cooker on Wheels as an Alternative for Philippine Rural Households

Cooking accounts for a significant share of the worldwide energy consumption issue. Solar box cookers are a good alternative in mitigating fossil fuels and biomass use, especially for tropical developing nations like the Philippines. Still, their broad acceptance is limited by their high dependence on sufficient sunlight for better performance. Thus, this research aims to develop a thermal-efficient, portable solar box cooker with sand-sensible heat storage materials, coconut coir (Cocos nucifera) agricultural waste insulators, and locally sourced building materials. The designed and constructed cooker was evaluated using three thermal performance tests: the Stagnation Temperature test from the Bureau of Indian Standards (BIS), the Cooking Power test from the American Societal of Agricultural Engineer (ASAE) Standards, and a rice cooking test. Data obtained from the three-day trials of each test were used to determine the first figure of merit (F1), the single measure of performance (Ps(50)), and its ability to cook 300 g of NFA rice with 500 mL of water, respectively. It was found that the cooker achieved an F1 of 0.06 Km2/w, a Ps(50) of 6.651 W, and cooked rice for one-third of the tests. Obtained experimental findings showed that the device is marked as a Grade-B solar cooker. Results indicated that the solar box cooker is capable of pasteurizing water and cooking rice

Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector

Importin-αs are essential adapter proteins that recruit cytoplasmic proteins destined for active nuclear import to the nuclear transport machinery. Cargo proteins interact with the importin-α armadillo repeat domain via nuclear localization sequences (NLSs), short amino acids motifs enriched in Lys and Arg residues. Plant genomes typically encode several importin-α paralogs that can have both specific and partially redundant functions. Although some cargos are preferentially imported by a distinct importin-α it remains unknown how this specificity is generated and to what extent cargos compete for binding to nuclear transport receptors. Here we report that the effector protein HaRxL106 from the oomycete pathogen Hyaloperonospora arabidopsidis co-opts the host cell's nuclear import machinery. We use HaRxL106 as a probe to determine redundant and specific functions of importin-α paralogs from Arabidopsis thaliana. A crystal structure of the importin-α3/MOS6 armadillo repeat domain suggests that five of the six Arabidopsis importin-αs expressed in rosette leaves have an almost identical NLS-binding site. Comparison of the importin-α binding affinities of HaRxL106 and other cargos in vitro and in plant cells suggests that relatively small affinity differences in vitro affect the rate of transport complex formation in vivo. Our results suggest that cargo affinity for importin-α, sequence variation at the importin-α NLS-binding sites and tissue-specific expression levels of importin-αs determine formation of cargo/importin-α transport complexes in plant cells