Constructing Bimetallic ZIF-Derived Zn,Co-Containing N-Doped Porous Carbon Nanocube as the Lithiophilic Host to Stabilize Li Metal Anodes in Li-O2 Batteries.

Li metal, because of its ultrahigh theoretical capacity, has attracted extensive attention. However, uncontrollable dendritic Li formation and infinite electrode dimensional variation hinder application of Li anodes. Herein, Zn,Co bimetallic zeolitic imidazolate frameworks (ZIFs) were synthesized and further pyrolyzed to obtain Zn,Co-containing N-doped porous carbon nanocube (Zn/Co-N@PCN), which was further applied as lithiophilic host to construct the lithiated Zn/Co-N@PCN (Li-Zn/Co-N@PCN). Zn vapor produced many pores on the carbon framework during calcination process that could store enough Li and thus inhibit the huge electrode volume change. Additionally, there were abundant lithiophilic groups in Zn/Co-N@PCN, such as N- or Co/Zn-based species, which were beneficial to uniform Li deposition. Moreover, the stable and conductive carbon-based matrix could ensure superior and reproducible Li plating/stripping behavior in Zn/Co-N@PCN over cycling. As a result, the Li-Zn/Co-N@PCN anode showed a steady and high columbic efficiency of around 99.0 % for 600 cycles at 0.5 mA cm-2 . The Li-Zn/Co-N@PCN-based Li-O2 battery could continuously work beyond 200 cycles, superior to a cell with a Li-Cu anode. These results in this work provide a novel way for construction of the advanced Li-based anodes and the corresponding high-performance Li-O2 batteries.

Polydopamine-coated bimetallic ZIF derivatives as an air cathode for acidic Zn-air batteries with super-high potential.

NC@Co-HPNC is synthesized, which exhibits a superior ORR/OER performance in acid/base solution. Hence, acid-base dual-electrolyte-based Zn-air batteries using NC@Co-HPNC reveal a long cycling life and a super-high voltage (2.1 V).

Intracellular expression and purification of the Canstatin-N protein in Pichia pastoris.

Canstatin-N DNA fragment amplified from human genome was inserted into the MCS of pGAP9K*, an intracellular expression vector of Pichia pastoris, to generate pGAP9K*-can-N which was then transformed into P. pastoris GS115 by electroporation. A transformant was chosen as an engineering strain from the plate containing G418 (700 µg/ml). D-sorbitol was selected as the only carbon source. The fermentation was carried out in a 50 L bioreactor at a 20 L working volume. After 48 h fermentation with continuous feeding of 25% (w/v) D-sorbitol and 0.8% PTM4, the cell grew to A(600)=178 and intracellularly expressed Canstatin-N reached 780 mg/L. Snail enzyme was combined with water to crack P. pastoris and to release intracellular proteins. The purified recombinant Canstatin-N inhibited CAM angiogenesis and induced significant apoptosis of the human umbilical vein endothelial cell (EVC340).

Isolation of laccase gene from Bacillus subtilis and analysis of its physicochemical properties.

The present study reports the cloning and sequencing of lac2 from Bacillus subtilis. The gene is composed of 1542 bp and encodes a 514-amino acid protein. The gene has 86% homology with a published laccase with GeneID 936023. The lac2 gene was deposited in GenBank as a new nucleotide sequence. This new sequence was cloned into the multiple cloning site of pPIC9K to generate pPIC9K-lac2, which was then transformed into Pichia pastoris GS115 via electroporation. The recombinant GS115 (pPIC9K-lac2) was grown initially in BMGY medium and transferred to BMMY to induce gene expression for 48 h. The recombinant Lac2 protein shows laccase activity with α-naphthol and guaiacol as substrates. The optimal pH is between 3.2 and 4.7, and the optimal temperature is 25°C for enzyme reaction.