期刊
JOURNAL OF PHYSICS-ENERGY
卷 3, 期 3, 页码 -出版社
IOP PUBLISHING LTD
DOI: 10.1088/2515-7655/abe2f6
关键词
hyperthermophilic enzyme; mesophilic enzyme; adsorption; deactivation; carbon black; secondary structures
资金
- JSPS KAKENHI [JP18K04822]
- Five-star Alliance
In this study, the hyperthermophilic laccase showed no loss in specific activities and secondary structures upon adsorption on carbon black (CB) compared to mesophilic laccase and glucose oxidase (GOx), indicating its potential for further increases in the current density of biofuel cells.
Further increases in the current density of biofuel cells are partly limited by the deactivation of enzymes upon adsorption on hydrophobic carbon materials. A hyperthermophilic enzyme, hyperthermophilic laccase, was employed in the present study and the change in the activities and secondary structures upon adsorption on carbon black (CB) were evaluated by the oxidation rate of 2,2 '-azinobis(3-ethylbenzothiazoline-6-sulfonate) and by Fourier transform infrared spectroscopy, respectively, in comparison with the mesophilic enzymes, laccase from Trametes versicolor (denoted as mesophilic laccase), and glucose oxidase (GOx). Hyperthermophilic laccase retained its specific activities and secondary structures upon adsorption on CB compared with the other two enzymes mesophilic laccase and GOx.
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