Straussbreum6965

Membrane proteins play important roles in health and disease. Despite their importance, the study of membrane proteins has been significantly limited by the difficulties inherent to their successful expression, purification, and stabilization once they have been extracted from the cell membrane. In addition, expression of human membrane proteins commonly requires the use of expensive and/or time-consuming eukaryotic systems, hence their successful expression in bacteria will be obviously beneficial for experimental research. Furthermore, since lipids can have critical effects on the activity of membrane proteins and given the composition similarities between the inner mitochondrial membrane and the bacterial plasma membrane, production of mitochondrial membrane proteins in E. coli represents a logical choice. Here, we present a novel protocol to produce a human mitochondrial ATP-Binding Cassette (ABC) transporter in E. coli. The function of the three known human mitochondrial ABC transporters is not fully understood, but X-ray crystallography models of ABCB10 produced in insect cells are available. We have successfully expressed and purified ABCB10 from E. coli. The yield is close to that of another bacterial ABC transporter routinely produced in our laboratory under similar conditions. In addition, we can efficiently reconstitute detergent purified ABCB10 into lipid nanodiscs. Measurements of ATPase activity of ABCB10 produced in E. coli show an ATP hydrolysis rate similar to other human ABC transporters. This novel protocol facilitates the production of this human mitochondrial transporter for biochemical, structural, and functional analysis, and can likely be adjusted for production of other mitochondrial transporters.An environmentally friendly nanocomposite adsorbent composed of two renewable biomaterials, bacterial cellulose (BC) nanofibrils and hydroxyapatite (HA) nanocrystals, was synthetized by an in situ wet chemical precipitation technique, using clam shell biowaste as feedstock. HA nanocrystals embedded in an ultrafine BC network were confirmed and characterized trough different instrumental techniques (SEM, FTIR, XRD, EDS, surface charge and BET analysis), describing its nanostructure, chemical composition and thermal stability. The adsorptive removal of lead ions by the nanocomposite was investigated through batch experiments conducted under different pH, contact times and Pb(II) initial concentrations, proving that the process was highly favorable according to the Langmuir isotherm model (monolayer adsorption) with chemisorption as the main mechanism and kinetic data obeying a nonlinear pseudo-second order kinetic model. The developed nanocomposite showed a strong removal capacity of Pb(II) both in batch experiments (192 mg/g) and packed-bed column systems (188 mg/g), placing this new nanocomposite among top-performing BC-based biomaterials for lead removal.Biodegradable films are a promising strategy to reduce the environmental impact caused by conventional plastics commonly used in agriculture. This study focused on the production and characterization of Konjac glucomannan (KGM) and alginate (ALG) based films enriched with sugarcane vinasse (VIN), a nutrient-rich wastewater generated in large volumes by the sugar-ethanol producing industries. ALG, KGM and ALG/KGM blended (5050) films were produced by casting and treated with calcium ions (Ca2+) (ALG films) and a combination of Ca2+, alkali, and ethanol (KGM and ALG/KGM films). Vinasse addition tended to reduce transparency and water resistance of the films and had less effect on their mechanical properties. Crosslinking of ALG films resulted in enhanced mechanical properties and reduced moisture content, water solubility, swelling, water vapor permeability, and flexibility. KGM films were less impacted by crosslinking/deacetylation but showed improved water resistance while maintain a high degree of swelling (290% and 185% for KGM and KGM/VIN films respectively). Blended films exhibited characteristic properties of the two biopolymers and adequate compatibility indicated by Fourier transform infrared spectroscopy (FTIR) and morphologies. Vinasse-added ALG/KGM films represent a novel nutrient-enriched, bio-based material for agricultural applications and could help to face the environmental challenges imposed by vinasse disposal.Pachynomidae is a poorly known heteropteran group currently considered as a distinct family closely related to Reduviidae. Taxonomic position of Pachynomidae has been debated for a long time. Knowledge about mitochondrial genome (mitogenome) of this family also remain limited. In the present study, we describe the complete mitogenome of Camarochiloides weiweii, the first mitogenome sequenced for this family. This mitogenome consists of 13 protein-coding genes, two rRNA genes and 21 tRNA genes. Two tRNA gene rearrangements in this genome, including the translocation of trnA and trnR as well as the transposition of trnH, were observed and could be explained by the tandem duplication-random loss (TDRL) model. Bayesian and maximum likelihood analyses based on sequences of three different mitogenomic datasets recovered the monophyly of Reduvioidea, and the sister relationship between Reduvioidea and the remaining Cimicomorpha lineages. This study enlightens the future application of mitogenomic data in the phylogenetic study of Cimicomorpha based on the large-scale sampling.The enzyme ficin, abundantly found in the leaves of the common Fig (Ficus carica. selleck kinase inhibitor L), is a cysteine protease of the plant endopeptidase family. In terms of activity, this enzyme mimics the activity of the papain enzyme. However, the enzyme is more acidic than papain and binds with higher efficiency to its substrate. Ficin is widely used in the food and pharmaceutical industry along with the medical diagnosis. To date, there are no available data on cloning and recombinant production of various isoforms of ficin. In the present study, after the cloning process and optimized expression of ficin in E. coli BL21, by means of the central composite design (CCD) and approach-based response surface methodology (RSM), the recombinant protein was purified using the Ni-sepharose column and gel filtration. The activity of ficin was determined by its ability to hydrolyze the bovine casein enzyme as a substrate. These results showed the presence of different isoforms of ficin in this cultivar that they are distinct in terms of DNA coding sequences.