Bengtson Lynn (salaryera1)

In this study, antibacterial nanofiber films were prepared by electrospinning gelatin, chitosan, and 3-phenyllactic acid (PLA). The addition of PLA improved the microstructures of the nanofibers, and the nanofiber films (GCP-1 and GCP-2) had uniform and continuous structures with a diameter range of 40--70 nm when the PLA concentrations in the polymers were 1% and 2%. Under acidic conditions, chitosan and PLA interacted and formed hydrogen bonds, which decreased the crystallinity of the nanofiber films. Selleck ART0380 The GCP-2 nanofiber film had the best thermal stability, water stability, and water vapor permeability. Compared with the control GCP-0 film, the four nanofiber films with PLA (GCP-1, GCP-2, GCP-3, and GCP-4) had more effective antibacterial effects, and GCP-2 film reduced approximately 4 log CFU/mL of Salmonella enterica Enteritidis and Staphylococcus aureus in 30 min. Results suggested that the GCP-2 nanofiber film mat can be used as an active food packaging.In this research, a novel polysaccharide (PCP) was extracted from Pleurotus citrinopileatus and purified by Sephadex G-150 gel column, and its antitumor activity was investigated using the model H22 tumor-bearing mice. PCP was found to be composed of arabinose, galactose, glucose, xylose, mannose and glucuronic acid in a proportion of 0.66 14.59 10.77 1 0.69 0.23 with average molecular weight of 7.30 × 105 Da. Further analysis suggested that PCP was a pyranose with α-type and β-type glycosidic residues. The antitumor assays in vivo indicated that PCP could effectively suppress H22 solid tumor growth, protect immune organs and improve inflammation and anemia. Besides, Annexin V-FITC/PI double staining and JC-1 staining demonstrated that PCP could induce apoptosis of H22 hepatoma cells. The PI staining assay revealed that PCP induced H22 hepatoma cells apoptosis by arresting cell cycle in S phase. These results suggest that the polysaccharide from Pleurotus citrinopileatus possesses potential value in the treatment of liver cancer.SARS-CoV-2is the causative agent for the ongoing COVID19 pandemic, and this virus belongs to the Coronaviridae family. The nsp14 protein of SARS-CoV-2 houses a 3' to 5' exoribonuclease activity responsible for removing mismatches that arise during genome duplication. A homology model of nsp10-nsp14 complex was used to carry out in silico screening to identify molecules among natural products, or FDA approved drugs that can potentially inhibit the activity of nsp14. This exercise showed that ritonavir might bind to the exoribonuclease active site of the nsp14 protein. A model of the SARS-CoV-2-nsp10-nsp14 complex bound to substrate RNA showed that the ritonavir binding site overlaps with that of the 3' nucleotide of substrate RNA. A comparison of the calculated energies of binding for RNA and ritonavir suggested that the drug may bind to the active site of nsp14 with significant affinity. It is, therefore, possible that ritonavir may prevent association with substrate RNA and thus inhibit the exoribonuclease activity of nsp14. Overall, our computational studies suggest that ritonavir may serve as an effective inhibitor of the nsp14 protein. nsp14 is known to attenuate the inhibitory effect of drugs that function through premature termination of viral genome replication. Hence, ritonavir may potentiate the therapeutic properties of drugs such as remdesivir, favipiravir and ribavirin.A novel thermostable xylanase gene from Chaetomium sp. CQ31 was cloned and codon-optimized (CsXynBop). The deduced protein sequence of the gene shared the highest similarity of 75% with the glycoside hydrolase (GH) family 10 xylanase from Achaetomium sp. Xz-8. CsXynBop was over-expressed in Pichia pastoris GS115 by high-cell density fermentation, with the highest xylanase yield of 10,017 U/mL. The recombinant xylanase (CsXynBop) was purified to homogeneity and biochemically characterized. CsXynBop was optimally active at pH 6.5 and 85 °C, respectively