Morphological,anatomical, physiological,and cytological studies in diploid and tetraploid plants of Plantago psyllium

Plant Cell, Tissue and Organ Culture (PCTOC) - Plantago psylliumis is under development as the source of mucilage, but has not been entirely domesticated. Since mucilage content is low and variable...     

Preparation and Characterization of Zein/Sodium Caseinate/Xanthan Gum Complex for Encapsulation of Piperine and its In Vitro Release Study

To encapsulate piperine (Pip), as a poor water-soluble bioactive compound, zein-sodium caseinate-xanthan gum (Z-SG-XG) nanocomplex was prepared as a colloidal delivery system. The effect of different parameters involved in complexation process, including concentration of proteins, polysaccharide, and Pip on the encapsulation efficiency of Pip, particle size and stability of the nanocomplexes was investigated. Powders obtained by freeze-drying of the colloidal solution had relatively uniform particles compared to those obtained from conventional drying system and showed well redispersibility in water. At the optimal condition, a stable and homogeneous nanocomplex with a mean particle size of 145.9 ± 2.7 nm, PDI of 0.27 ± 0.01, and ζ-potential of −39.7 ± 1.3 mV was obtained. The antioxidant activity of Pip was significantly improved by encapsulation into the Z-SC-XG nanocomplex. Also, the in vitro release of Pip from the synthesized nanocomplexes in phosphate-buffer saline (PBS) solution and simulated gastrointestinal fluids (SGIF) was investigated and the release kinetic was studied as well. The Pip/Z-SG-XG nanocomplex showed a slower release in SGIF compared to the free Pip and nanoparticles without XG and SC, while its antioxidant activity was remarkable. Results suggested a possible utilization of Z-SC-XG nanocomplex for improving the water solubility, bioavailability and storage stability of Pip.

     

Effects of different lengths of high-intensity interval training microcycles on the systemic and hippocampal inflammatory state and antioxidant balance of immature rats

Molecular Biology Reports - There is a lack of evidence on the effects of high-intensity interval training (HIIT) microcycle duration on the antioxidant capacity and hippocampal inflammatory...     

Atomic insight into designed carbamate-based derivatives as acetylcholine esterase (AChE) inhibitors: a computational study by multiple molecular docking and molecular dynamics simulation

Over 100 variants have been designed and studied, using multiple docking methods such as Autodock Vina, ArgusLab, Molegro Virtual Docker, and Hex-Cuda, to study the effect of alteration in the structure of carbamate-based acetylcholyne esterase (AChE) inhibitors. Sixteen selected systems were then subjected to 14 ns molecular dynamics (MD) simulations. Results from all the docking methods are in agreement. Variants that involved biphenyl substituents possess the most negative binding energies in the ?37.64 to ?39.31 kJ mol^?1 range due to their π–π interactions with AChE aromatic residues. The root mean square deviation values showed that all of these components achieved equilibration after 6 ns. Gyration radius (R_g) and solvent accessibility surface area were calculated to further investigate the AChE conformational changes in the presence of these components. MD simulation results suggested that these components might interact with AChE, possibly with no major changes in AChE secondary and tertiary structures.     

Metagenomic analysis reveals a dynamic microbiome with diversified adaptive functions to utilize high lignocellulosic forages in the cattle rumen

Rumen microbiota play a key role in the digestion and utilization of plant materials by the ruminant species, which have important implications for greenhouse gas emission. Yet, little is known about the key taxa and potential gene functions involved in the digestion process. Here, we performed a genome-centric analysis of rumen microbiota attached to six different lignocellulosic biomasses in rumen-fistulated cattle. Our metagenome sequencing provided novel genomic insights into functional potential of 523 uncultured bacteria and 15 mostly uncultured archaea in the rumen. The assembled genomes belonged mainly to Bacteroidota, Firmicutes, Verrucomicrobiota, and Fibrobacterota and were enriched for genes related to the degradation of lignocellulosic polymers and the fermentation of degraded products into short chain volatile fatty acids. We also found a shift from copiotrophic to oligotrophic taxa during the course of rumen fermentation, potentially important for the digestion of recalcitrant lignocellulosic substrates in the physiochemically complex and varying environment of the rumen. Differential colonization of forages (the incubated lignocellulosic materials) by rumen microbiota suggests that taxonomic and metabolic diversification is an evolutionary adaptation to diverse lignocellulosic substrates constituting a major component of the cattle’s diet. Our data also provide novel insights into the key role of unique microbial diversity and associated gene functions in the degradation of recalcitrant lignocellulosic materials in the rumen.Subject terms: Bacterial genetics, Metagenomics     

G219S mutagenesis as a means of stabilizing conformational flexibility in the bacterial sodium channel NaChBac

The NaChBac sodium channel from Bacillus halodurans is a homologue of eukaryotic voltage-gated sodium channels. It can be solubilized in a range of detergents and consists of four identical subunits assembled as a tetramer. Sodium channels are relatively flexible molecules, adopting different conformations in their closed, open and inactivated states. This study aimed to design and construct a mutant version of the NaChBac protein that would insert into membranes and retain its folded conformation, but which would have enhanced stability when subjected to thermal stress. Modelling studies suggested a G219S mutant would have decreased conformational flexibility due to the removal of the glycine hinge around the proposed gating region, thereby imparting increased resistance to unfolding. The mutant expressed in Escherichia coli and purified in the detergent dodecyl maltoside was compared to wildtype NaChBac prepared in a similar manner. The mutant was incorporated into the membrane fraction and had a nearly identical secondary structure to the wildtype protein. When the thermal unfolding of the G219S mutant was examined by circular dichroism spectroscopy, it was shown to not only have a Tm ～10°C higher than the wildtype, but also in its unfolded state it retained more ordered helical structure than did the wildtype protein. Hence the G219S mutant was shown to be, as designed, more thermally stable.