Electrochemical contrast switching between black and white appearance of gelatin-covered zinc

Zinc and its alloys are widely used in the surface protection of metallic structural materials. Thus, zinc is an interesting and relevant candidate material for preparing stimuli-responsive surfaces. In this work, the switching of the optical appearance of zinc between black and white by an applied electrode potential is demonstrated. The zinc surface was covered by gelatin films and subjected to cyclic voltammetry (CV) in a chloride-containing electrolyte which induced pitting corrosion on the zinc surface. Between the different parts of the CV cycles, a reversible change in optical appearance was observed. During the oxidative half-cycles, the surfaces appear white, and during the reductive half-cycles, the surfaces appear brown to black, i.e. dark. Surface characterisation by x-ray photoelectron spectroscopy (XPS) and infrared (IR) spectroscopy shows that the gelatin coating is slightly oxidised during intial stages of the process, but remains intact and present at the surface. Raman spectra prove the presence of ZnO at the interface. Surface analysis shows only minor differences in composition between the black and white surfaces. Based on the available characterisation data, the white appearance associated with anodic currents is attributed to the formation of a non-passivating ZnO. The black appearance associated with cathodic currents is attributed to reduction of surface-confined zinc species, including ZnO and Zn2+. The role of the gelatin is presumably to prevent diffusion of the dissolution products into solution by complex formation and by acting as a diffusion barrier; gelatin will also affect the morphology of the reduction products. A similar switching was observed when gelatin was added to chloride electrolyte; surface analysis showed gelatin adsorption in this case. The black/white switching may, e.g. be useful for surfaces self-indicating corrosion potentials of galvanised steel

Analysis of conglutin seed storage proteins across lupin species using transcriptomic, protein and comparative genomic approaches

Background - The major proteins in lupin seeds are conglutins that have primary roles in supplying carbon, sulphur and nitrogen and energy for the germinating seedling. They fall into four families; α, β, γ and δ. Interest in these conglutins is growing as family members have been shown to have beneficial nutritional and pharmaceutical properties. Results - An in-depth transcriptome and draft genome from the narrow-leafed lupin (NLL; Lupinus angustifolius) variety, Tanjil, were examined and 16 conglutin genes were identified. Using RNAseq data sets, the structure and expression of these 16 conglutin genes were analysed across eight lupin varieties from five lupin species. Phylogenic analysis suggest that the α and γ conglutins diverged prior to lupin speciation while β and δ members diverged both prior and after speciation. A comparison of the expression of the 16 conglutin genes was performed, and in general the conglutin genes showed similar levels of RNA expression among varieties within species, but quite distinct expression patterns between lupin species. Antibodies were generated against the specific conglutin families and immunoblot analyses were used to compare the levels of conglutin proteins in various tissues and during different stages of seed development in NLL, Tanjil, confirming the expression in the seed. This analysis showed that the conglutins were expressed highly at the mature seed stage, in all lupin species, and a range of polypeptide sizes were observed for each conglutin family. Conclusions - This study has provided substantial information on the complexity of the four conglutin families in a range of lupin species in terms of their gene structure, phylogenetic relationships as well as their relative RNA and protein abundance during seed development. The results demonstrate that the majority of the heterogeneity of conglutin polypeptides is likely to arise from post-translational modification from a limited number of precursor polypeptides rather than a large number of different genes. Overall, the results demonstrate a high degree of plasticity for conglutin expression during seed development in different lupin species