Cycling pressure-switching process enriches micropores in activated carbon by accelerating reactive gas internal diffusion in porous channels

2021 ◽  
Vol 28 ◽  
pp. e00248
Author(s):  
Jingjing Xiong ◽  
Guancong Jiang ◽  
Yu Qian ◽  
Liwen Mu ◽  
Xin Feng ◽  
...  
2020 ◽  
Author(s):  
Feng Xiao ◽  
Bin Yao ◽  
Pavankumar Challa Sasi ◽  
Svetlana Golovko ◽  
Dana Soli ◽  
...  

2001 ◽  
Vol 11 (PR3) ◽  
pp. Pr3-279-Pr3-286
Author(s):  
X. Dabou ◽  
P. Samaras ◽  
G. P. Sakellaropoulos

2020 ◽  
Vol 64 (1-4) ◽  
pp. 1261-1268
Author(s):  
Shu Otani ◽  
Dang-Trang Nguyen ◽  
Kozo Taguchi

In this study, a portable and disposable paper-based microbial fuel cell (MFC) was fabricated. The MFC was powered by Rhodopseudomonas palustris bacteria (R. palustris). An activated carbon sheet-based anode pre-loaded organic matter (starch) and R. palustris was used. By using starch in the anode, R. palustris-loaded on the anode could be preserved for a long time in dry conditions. The MFC could generate electricity on-demand activated by adding water to the anode. The activated carbon sheet anode was treated by UV-ozone treatment to remove impurities and to improve its hydrophilicity before being loaded with R. palustris. The developed MFC could generate the maximum power density of 0.9 μW/cm2 and could be preserved for long-term usage with little performance degradation (10% after four weeks).


2015 ◽  
Vol 14 (1) ◽  
pp. 66-72 ◽  
Author(s):  
Seo-Hyun Pak ◽  
◽  
Myung-Seop Shin ◽  
Hyun-Jung Kim ◽  
Yong-Woo Jeon

2004 ◽  
Vol 9 (2) ◽  
pp. 139-144 ◽  
Author(s):  
J. Kulys

A model of biosensor containing three immobilized enzymes utilizing consecutive substrate conversion in the chain was developed. The modeling was performed at an internal diffusion limitation and a steadystate condition. The calculations showed that significant response of biosensors was produced if diffusion modules were larger than 1 for all enzyme reactions. Due to diffusion limitation the apparent stability of biosensor response increased many times in comparison to stability of the most labile enzyme of the chain.


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