Silver Nanowire-Conducting Polymer-ITO Hybrids for Flexible and Transparent Conductive Electrodes with Excellent Durability.

Solution-processed silver nanowire (AgNW) films have attracted attention as transparent and conductive electrodes for flexible optoelectronic devices and touch screens, to replace sputtered indium-tin-oxide (ITO) films. However, the mechanical flexibility, environmental durability, and the optical (such as transparency and a haze) and electrical properties of the AgNW films should be improved for their practical application. In this work, high-performance and roll-to-roll processed AgNW-based hybrid electrodes comprising poly(3,4-ethylenedioxythiophene):poly(styrenesulfonate) ( PEDOT: PSS) and/or ITO are introduced. The optical and electrical properties of the AgNW films combined with PEDOT: PSS, ITO, or both of them were systematically examined. Among the films, the AgNW-PEDOT:PSS-ITO hybrid film exhibits a high transmittance (88%) and a low sheet resistance (44 Ω sq(-1)) with a small haze (1.9%). Moreover, the hybrid films show excellent durability to a variety of environmental stresses. By virtues of the high performance and durability, it is believed that the AgNW-PEDOT:PSS-ITO hybrid electrodes are highly suitable for practical use.

Novel intracellular GH10 xylanase from Cohnella laeviribosi HY-21: biocatalytic properties and alterations of substrate specificities by site-directed mutagenesis of Trp residues.

The novel intracellular GH10 xylanase (iXylC) gene (1023-bp) of Cohnella laeviribosi HY-21 encoded a protein consisting of 340 amino acids with a deduced molecular mass of 39,330Da and a calculated pI of 5.81. The primary structure of iXylC was 70% identical to that of Geobacillus sp. GH10 enzyme (GenBank accession number: EDV78425). Xylanolytic activity of the His-tagged iXylC overproduced in Escherichiacoli BL21 was stimulated by 2.2-fold in the presence of 0.5% non-ionic detergents. iXylC produced a mixture of xylooligosaccharides (xylobiose to xylooctaose) from xylotriose and xylotetraose used as the hydrolytic substrate. In addition, it exhibited considerable cleavage activities for p-nitrophenylxylopyranoside (PNP-xylopyranoside) and PNP-cellobioside, indicating that iXylC is a unique GH10 enzyme. The hydrolytic activity (57.8IUmL(-1)) of iXylC toward PNP-xylopyranoside increased to 8.3-fold by W217A and W315A mutations, while mutations of W133A, W295A, and W303A abolished the hydrolytic activity of the enzyme.

Novel GH10 xylanase, with a fibronectin type 3 domain, from Cellulosimicrobium sp. strain HY-13, a bacterium in the gut of Eisenia fetida.

The gene encoding a novel modular xylanase from Cellulosimicrobium sp. strain HY-13 was identified and expressed in Escherichia coli, and its truncated gene product was characterized. The enzyme consisted of three distinct functional domains, an N-terminal catalytic GH10 domain, a fibronectin type 3 domain, and C-terminal carbohydrate-binding module 2.