Induction of nucleoside phosphorylase in Enterobacter aerogenes and enzymatic synthesis of adenine arabinoside

Nucleoside phosphorylases (NPases) were found to be induced in Enterobacter aerogenes DGO-04, and cytidine and cytidine 5′-monophosphate (CMP) were the best inducers. Five mmol/L to fifteen mmol/L cytidine or CMP could distinctly increase the activities of purine nucleoside phosphorylase (PNPase), uridine phosphorylase (UPase) and thymidine phosphorylase (TPase) when they were added into medium from 0 to 8 h. In the process of enzymatic synthesis of adenine arabinoside from adenine and uracil arabinoside with wet cells of Enterobacter aerogenes DGO-04 induced by cytidine or CMP, the reaction time could be shortened from 36 to 6 h. After enzymatic reaction the activity of NPase in the cells induced remained higher than that in the cells uninduced.

Hybrid sub-gridding ADE–FDTD method of modeling periodic metallic nanoparticle arrays

In this paper, a modified sub-gridding scheme that hybridizes the conventional finite-difference time-domain（FDTD）method and the unconditionally stable locally one-dimensional（LOD） FDTD is developed for analyzing the periodic metallic nanoparticle arrays. The dispersion of the metal, caused by the evanescent wave propagating along the metal-dielectric interface, is expressed by the Drude model and solved with a generalized auxiliary differential equation（ADE） technique.In the sub-gridding scheme, the ADE–FDTD is applied to the global coarse grids while the ADE–LOD–FDTD is applied to the local fine grids. The time step sizes in the fine-grid region and coarse-grid region can be synchronized, and thus obviating the temporal interpolation of the fields in the time-marching process. Numerical examples about extraordinary optical transmission through the periodic metallic nanoparticle array are provided to show the accuracy and efficiency of the proposed method.

Enzymatic synthesis of nucleosides by nucleoside phosphorylase co-expressed in Escherichia coli

Nucleoside phosphorylase is an important enzyme involved in the biosynthesis of nucleosides.In this study,purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase were co-expressed in Escherichia coli and the intact cells were used as a catalyst for the biosynthesis of nucleosides.For protein induction,lactose was used in place of isopropylβ-D-1-thiogalactopyranoside(IPTG) .When the concentration of lactose was above 0.5 mmol/L,the ability to induce protein expression was similar to that of IPTG.We determined that the reaction conditions of four bacterial strains co-expressing these genes(TUD,TAD,DUD,and DAD) were similar for the biosyntheses of 2,6-diaminopurine nucleoside and 2,6-diaminopurine deoxynucleoside.When the substrate concentration was 30 mmol/L and 0.5%of the recombinant bacterial cell volume was used as the catalyst(pH 7.5) ,a greater than 90%conversion yield was reached after a 2-h incubation at 50°C.In addition,several other nucleosides and nucleoside derivatives were efficiently synthesized using bacterial strains co-expressing these recombinant enzymes.