No abstract

No abstract

No abstract

We investigated resistance switching in top-electrode/NiO∕Pt structures where the top electrode was Au, Pt, Ti, or Al. For Pt∕NiO∕Pt and Au∕NiO∕Pt structures with ohmic contacts, the effective electric field inside the film was high enough to induce trapping or detrapping at defect states and thus resistance switching. For a Ti∕NiO∕Pt structure with well-defined Schottky contact at Ti∕NiO interface accompanied by an appreciable voltage drop, the effective electric field inside the NiO film was not enough to induce resistance switching. For an Al∕NiO∕Pt structure with a low Schottky barrier at the Al∕NiO interface, resistance switching could be induced at a higher voltage since the voltage drop at the Al∕NiO interface was not negligible but small.

No abstract

We have compared resistance switching of NiO films deposited on Pt and SrRuO3 (SRO): unipolar switching in Pt/NiO/Pt and bipolar switching in Pt/NiO/SRO. Linear fitted current-voltage curves and capacitance-voltage results show that on- and off-states conductions in unipolar switching are dominated by inductive Ohmic behavior and Poole–Frenkel effect, respectively. However, the conductions of on- and off-states in bipolar switching follow capacitive Ohmic behavior and Schottky effect, respectively. Therefore, we infer that the mechanisms of the unipolar and bipolar switching behaviors in NiO films are related with changes in bulk-limited filamentary conduction and interfacial Schottky barrier, respectively.

A recombinant putative lipoxygenase from Burkholderia thailandensis with a specific activity of 26.4 U mg(-1) was purified using HisTrap affinity chromatography. The native enzyme was a 75-kDa dimer with a molecular mass of 150 kDa. The enzyme activity and catalytic efficiency (k cat/K m) were the highest for linoleic acid (k cat of 93.7 s(-1) and K m of 41.5 μM), followed by arachidonic acid, α-linolenic acid, and γ-linolenic acid. The enzyme was identified as an omega-6 linoleate lipoxygenase (or a linoleate 13S-lipoxygenase) based on genetic and HPLC analyses as well as substrate specificity. The reaction conditions for the enzymatic production of 13-hydroxy-9,11(Z,E)-octadecadienoic acid (13-HODE) were optimal at pH 7.5, 25 °C, 20 g l(-1) linoleic acid, 2.5 g l(-1) enzyme, 0.1 mM Cu(2+), and 6% (v/v) methanol. Under these conditions, linoleate 13-lipoxygenase from B. thailandensis produced 20.8 g l(-1) 13-HODE (70.2 mM) from 20 g l(-1) linoleic acid (71.3 mM) for 120 min, with a molar conversion yield of 98.5% and productivity of 10.4 g l(-1) h(-1). The molar conversion yield and productivity of 13-HODE obtained using B. thailandensis lipoxygenase were 151 and 158% higher, respectively, than those obtained using commercial soybean lipoxygenase under the optimum conditions for each enzyme at the same concentrations of substrate and enzyme.

The aim of this study is the first time demonstration of cis-12 regio-selective linoleate double-bond hydratase. Hydroxylation of fatty acids, abundant feedstock in nature, is an emerging alternative route for many petroleum replaceable products thorough hydroxy fatty acids, carboxylic acids, and lactones. However, chemical route for selective hydroxylation is still quite challenging owing to low selectivity and many environmental concerns. Hydroxylation of fatty acids by hydroxy fatty acid forming enzymes is an important route for selective biocatalytic oxyfunctionalization of fatty acids. Therefore, novel fatty acid hydroxylation enzymes should be discovered. The two hydratase genes of Lactobacillus acidophilus were identified by genomic analysis, and the expressed two recombinant hydratases were identified as cis-9 and cis-12 double-bond selective linoleate hydratases by in vitro functional validation, including the identification of products and the determination of regio-selectivity, substrate specificity, and kinetic parameters. The two different linoleate hydratases were the involved enzymes in the 10,13-dihydroxyoctadecanoic acid biosynthesis. Linoleate 13-hydratase (LHT-13) selectively converted 10 mM linoleic acid to 13S-hydroxy-9(Z)-octadecenoic acid with high titer (8.1 mM) and yield (81%). Our study will expand knowledge for microbial fatty acid-hydroxylation enzymes and facilitate the designed production of the regio-selective hydroxy fatty acids for useful chemicals from polyunsaturated fatty acid feedstocks.