TY - JOUR
T1 - Co-immobilization of glucose oxidase and catalase for enhancing the performance of a membraneless glucose biofuel cell operated under physiological conditions
AU - Christwardana, Marcelinus
AU - Chung, Yongjin
AU - Kwon, Yongchai
N1 - Publisher Copyright:
© 2017 The Royal Society of Chemistry.
PY - 2017/2/7
Y1 - 2017/2/7
N2 - Glucose oxidase (GOx)-catalase co-immobilized catalyst (CNT/PEI/(GOx-Cat)) was synthesized, and its catalytic activity and electrical performance were investigated and compared, whereas the amount of immobilized catalase was optochemically inspected by chemiluminescence (CL) assay. With the characterizations, it was confirmed that the catalase was well immobilized on the CNT/PEI surface, whereas both the GOx and catalase play their roles well in the catalyst. According to the measurements of the current density peak of the flavin adenine dinucleotide (FAD) redox reaction, electron transfer rate, Michaelis-Menten constants and sensitivity, CNT/PEI/(GOx-Cat) shows the best values, and this is attributed to the excellent catalytic activity of GOx and the H2O2 decomposition capability of the catalase. To evaluate the electrical performance, a membraneless glucose biofuel cell (GBFC) adopting the catalyst was operated under physiological conditions and produced a maximum power density (MPD) of 180.8 ± 22.3 μW cm-2, which is the highest value compared to MPDs obtained by adoption of other catalysts. With such results, it was clarified that the CNT/PEI/(GOx-Cat) manufactured by co-immobilization of GOx and catalase leads to enhancements in the catalytic activity and GBFC performance due to the synergetic effects of (i) effective removal of harmful H2O2 moiety by catalase and (ii) superior activation of desirable reactions by GOx.
AB - Glucose oxidase (GOx)-catalase co-immobilized catalyst (CNT/PEI/(GOx-Cat)) was synthesized, and its catalytic activity and electrical performance were investigated and compared, whereas the amount of immobilized catalase was optochemically inspected by chemiluminescence (CL) assay. With the characterizations, it was confirmed that the catalase was well immobilized on the CNT/PEI surface, whereas both the GOx and catalase play their roles well in the catalyst. According to the measurements of the current density peak of the flavin adenine dinucleotide (FAD) redox reaction, electron transfer rate, Michaelis-Menten constants and sensitivity, CNT/PEI/(GOx-Cat) shows the best values, and this is attributed to the excellent catalytic activity of GOx and the H2O2 decomposition capability of the catalase. To evaluate the electrical performance, a membraneless glucose biofuel cell (GBFC) adopting the catalyst was operated under physiological conditions and produced a maximum power density (MPD) of 180.8 ± 22.3 μW cm-2, which is the highest value compared to MPDs obtained by adoption of other catalysts. With such results, it was clarified that the CNT/PEI/(GOx-Cat) manufactured by co-immobilization of GOx and catalase leads to enhancements in the catalytic activity and GBFC performance due to the synergetic effects of (i) effective removal of harmful H2O2 moiety by catalase and (ii) superior activation of desirable reactions by GOx.
UR - http://www.scopus.com/inward/record.url?scp=85011392330&partnerID=8YFLogxK
U2 - 10.1039/c6nr09103b
DO - 10.1039/c6nr09103b
M3 - Article
C2 - 28106225
AN - SCOPUS:85011392330
SN - 2040-3364
VL - 9
SP - 1993
EP - 2002
JO - Nanoscale
JF - Nanoscale
IS - 5
ER -