Enhanced Diffusion Kinetics of Li Ions in Double-Shell Hollow Carbon Fibers.

The rational design and preparation of hierarchical hollow structures have promising potential in electrochemical energy storage systems. In this paper, double-shell hollow carbon fibers (DSHCFs) with tunable thickness and shell spacing are prepared using hollow electrospun polystyrene fibers as the hard template and in situ coated polypyrrole as the carbon source. The as-prepared DSHCFs with an optimized structure exhibit a submicrometer shell spacing and a nanoscaled shell thickness, which guarantees sufficient contact area with the electrolyte and provides abundant electrochemical active sites for Li+ storage. Owing to the unique structural advantages, a DSHCF-based anode shows favorable transport kinetics for both Li+ ions and electrons during the lithiation/delithiation process, and a high reversible capacity of 348 mAh g-1 at 5.0 A g-1 is well maintained even after 500 cycles with no obvious capacity attenuation. Particular emphasis is given to kinetic Li+ storage mechanisms in DSHCFs that are discussed in detail, providing a new avenue for developing high-performance carbon materials for the practical application of energy storage devices.

Brittle culm15 encodes a membrane-associated chitinase-like protein required for cellulose biosynthesis in rice.

Plant chitinases, a class of glycosyl hydrolases, participate in various aspects of normal plant growth and development, including cell wall metabolism and disease resistance. The rice (Oryza sativa) genome encodes 37 putative chitinases and chitinase-like proteins. However, none of them has been characterized at the genetic level. In this study, we report the isolation of a brittle culm mutant, bc15, and the map-based cloning of the BC15/OsCTL1 (for chitinase-like1) gene affected in the mutant. The gene encodes the rice chitinase-like protein BC15/OsCTL1. Mutation of BC15/OsCTL1 causes reduced cellulose content and mechanical strength without obvious alterations in plant growth. Bioinformatic analyses indicated that BC15/OsCTL1 is a class II chitinase-like protein that is devoid of both an amino-terminal cysteine-rich domain and the chitinase activity motif H-E-T-T but possesses an amino-terminal transmembrane domain. Biochemical assays demonstrated that BC15/OsCTL1 is a Golgi-localized type II membrane protein that lacks classical chitinase activity. Quantitative real-time polymerase chain reaction and ß-glucuronidase activity analyses indicated that BC15/OsCTL1 is ubiquitously expressed. Investigation of the global expression profile of wild-type and bc15 plants, using Illumina RNA sequencing, further suggested a possible mechanism by which BC15/OsCTL1 mediates cellulose biosynthesis and cell wall remodeling. Our findings provide genetic evidence of a role for plant chitinases in cellulose biosynthesis in rice, which appears to differ from their roles as revealed by analysis of Arabidopsis (Arabidopsis thaliana).