Solar light-driven reduction of crystal violet by a composite of g-C3N4, β-Ag2Se, γ-Fe2O3 and graphite

Abstract

In this work, a new g-C₃N₄-based Z-scheme with γ-Fe₂O₃ and β-Ag₂Se both n-type semiconductors, and graphite to favor electron exchange is presented. The composite material was studied by XRD, FTIR, UV-Vis, TEM, XPS, TGA, DSC and TOF-SIMS, and the ability of this photocatalytic system to act as a photo-reductant was assessed using crystal violet (CV⁺) dye. Solar light driven photo-reduction of CV⁺ in the presence of tri-sodium citrate evidenced a synergistic enhancement of the activity of the composite toward reduction, with ～20 times higher conversion rates per unit of surface area than those of g-C₃N₄. Photo-oxidation experiments under Xe lamp irradiation in the presence of H₂O₂ also showed that the AgFeCN composite featured a higher activity (～8×) than g-C₃N₄. This Z-scheme may deserve further study as a photo-reductant to obtain hydrogen or hydrogenated compounds. Moreover, the use of CV⁺ may represent a facile procedure that can aid in the selection of new photocatalysts to be used in hydrogen production.     

Design and evaluation of a mobile smart home interactive system with elderly users in Brazil

Personal and Ubiquitous Computing - This article presents a study concerning the evaluation of a smart home control system for elderly people with a sample of 10 users in a city in the interior of...     

Metabolism of phospholipids in the yeast Schizosaccharomyces pombe

The fission yeast Schizosaccharomyces pombe is an important model organism for the study of fundamental questions in eukaryotic cell and molecular biology. A plethora of cellular processes are membrane associated and/or dependent on the proper functioning of cellular membranes. Phospholipids are not only the basic building blocks of cellular membranes; they also serve as precursors to numerous signaling molecules. In this review, we describe the biosynthetic pathways leading to major S. pombe phospholipids, how these pathways are regulated, and what is known about degradation and turnover of fission yeast phospholipids. This review also addresses the synthesis, regulation and the role of water-soluble phospholipid precursors. The last chapter of the review is devoted to the use of S. pombe for the biotechnological production of value-added lipid molecules.     

Bioinformatic characterization of the extracellular lipases from Kluyveromyces marxianus

Lipases are hydrolytic enzymes that break the ester bonds of triglycerides, generating free fatty acids and glycerol. Extracellular lipase activity has been reported for the nonconventional yeast Kluyveromyces marxianus, grown in olive oil as a substrate, and the presence of at least eight putative lipases has been detected in its genome. However, to date, there is no experimental evidence on the physiological role of the putative lipases nor their structural and catalytic properties. In this study, a bioinformatic analysis of the genes of the putative lipases from K. marxianus L-2029 was performed, particularly identifying and characterizing the extracellular expected enzymes, due to their biotechnological relevance. The amino acid sequence of 10 putative lipases, obtained by in silico translation, ranged between 389 and 773 amino acids. Two of the analysed putative proteins showed a signal peptide, 25 and 33 amino acids long for KmYJR107Wp and KmLIP3p, and a molecular weight of 44.53 and 58.23 kDa, respectively. The amino acid alignment of KmLIP3p and KmYJR107Wp with the crystallized lipases from a patatin and the YlLip2 lipase from Yarrowia lipolytica, respectively, revealed the presence of the hydrolase characteristic motifs. From the 3D models of putative extracellular K. marxianus L-2029 lipases, the conserved pentapeptide of each was determined, being GTSMG for KmLIP3p and GHSLG for KmYJR107Wp; besides, the genes of these two enzymes (LIP3 and YJR107W) are apparently regulated by oleate response elements. The phylogenetic analysis of all K. marxianus lipases revealed evolutionary affinities with lipases from abH15.03, abH23.01, and abH23.02 families.