Snyderlinnet0700

Ageing is a global burden. Increasing age is associated with increased incidence of infections and cancer and decreased vaccine efficacy. This increased morbidity observed with age, is believed to be due in part to a decline in adaptive immunity, termed immunosenescence. However not all aspects of immunity decrease with age as ageing presents with systemic low grade chronic inflammation, characterised by elevated concentrations of mediators such as IL-6, TNFα and C Reactive protein (CRP). Inflammation is a strong predictor of morbidity and mortality, and chronic inflammation is known to be detrimental to a functioning immune system. Although the source of the inflammation is much discussed, the key cells which are believed to facilitate the inflammageing phenomenon are the monocytes and macrophages. In this review we detail how macrophage and monocyte phenotype and function change with age. The impact of ageing on macrophages includes decreased phagocytosis and immune resolution, increased senescent-associated markers, increased inflammatory cytokine production, reduced autophagy, and a decrease in TLR expression. With monocytes there is an increase in circulating CD16+ monocytes, decreased type I IFN production, and decreased efferocytosis. In conclusion, we believe that monocytes and macrophages contribute to immunosenescence and inflammageing and as a result have an important role in defective immunity with age.Economic production of lignocellulose degrading enzymes for biofuel industries is of considerable interest to the biotechnology community. While these enzymes are widely distributed in fungi, their industrial production from other sources, particularly by thermophilic anaerobic bacteria (growth Topt ≥ 60 °C), is an emerging field. Thermophilic anaerobic bacteria produce a large number of lignocellulolytic enzymes having unique structural features and employ different schemes for biomass degradation, which can be classified into four systems namely; 'free enzyme system', 'cell anchored enzymes', 'complex cellulosome system', and 'multifunctional multimodular enzyme system'. Such enzymes exhibit high specific activity and have a natural ability to withstand harsh bioprocessing conditions. However, achieving a higher production of these thermostable enzymes at current bioprocessing targets is challenging. In this review, the research opportunities for these distinct enzyme systems in the biofuel industry and the associated technological challenges are discussed. The current status of research findings is highlighted along with a detailed description of the categorization of the different enzyme production schemes. It is anticipated that high temperature-based bioprocessing will become an integral part of sustainable bioenergy production in the near future.Fumonisins have posed hazardous threat to human and animal health worldwide. Enzymatic degradation is a desirable detoxification approach but is severely hindered by serious shortage of detoxification enzymes. After mining enzymes by bioinformatics analysis, a novel carboxylesterase FumDSB from Sphingomonadales bacterium was expressed in Escherichia coli, and confirmed to catalyze fumonisin B1 to produce hydrolyzed fumonisin B1 by liquid chromatography mass spectrometry for the first time. FumDSB showed high sequence novelty, sharing only ~34% sequence identity with three reported fumonisin detoxification carboxylesterases. Besides, FumDSB displayed its high degrading activity at 30-40 °C within a broad pH range from 6.0 to 9.0, which is perfectly suitable to be used in animal physiological condition. It also exhibited excellent pH stability and moderate thermostability. This study provides a FB1 detoxification carboxylesterase which could be further used as a potential food and feed additive.This study employed mesophilic Bacillus subtilis RTS strain isolated from soil with high xylanolytic activity. this website A 642 bp (xyn) xylanase gene (GenBank accession number MT677937) was extracted from Bacillus subtilis RTS and cloned in Escherichia coli BL21 cells using pET21c expression system. The cloned gene belongs to glycoside hydrolase family 11 with protein size of approximately 23 KDa. The recombinant xylanase showed optimal enzyme activity at 60 °C and at pH 6.5. Thermostability of recombinant xylanase was observed between the temperature range of 30-60 °C. Xylanase also remained stable in different concentration of various organic solvents (ethanol, butanol). This might be due to the formation of protein/organic solvent interface which prevents stripping of essential water molecules from enzyme, thus enzyme conformation and activity remained stable. Finally, the molecular docking analysis through AutoDock Vina showed the involvement of Tyr 108, Arg140 and Pro144 in protein-ligand interaction, which stabilizes this complex. The observed stability of recombinant xylanase at higher temperature and in the presence of organic solvent (ethanol, butanol) suggested possible application of this enzyme in biofuel and other industrial applications.The formation of chitosan dimer and its interaction with urea and creatinine have been investigated at the density functional theory (DFT) level (B3LYP-D3/6-31++G**) to study the transport phenomena in hemodialysis membrane. The interaction energy of chitosan-creatinine and chitosan-urea complexes are in range -4 kcal/mol less then interaction energy less then -20 kcal/mol which were classified in medium hydrogen bond interaction. The chemical reactivity parameter proved that creatinine was more electrophilic and easier to bind chitosan than urea. The energy gap of HOMO-LUMO of chitosan-creatinine complex was lower than chitosan-urea complex that indicating chitosan-creatinine complex was more reactive and easier to transport electron than chitosan-urea complex. Moreover, the natural bond orbital (NBO) analysis showed a high contribution of hydrogen bond between chitosan-creatinine and chitosan-urea. The chitosan-creatinine interaction has a stronger hydrogen bond than chitosan-urea through the interaction O18-H34....N56 with stabilizing energy = -13 kcal/mol. The quantum theory atom in molecule (QTAIM) also supported NBO data. All data presented that creatinine can make hydrogen bond interaction stronger with chitosan than urea, that indicated creatinine easier to transport in the chitosan membrane than urea during hemodialysis process.