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.

生物燃料电池电流密度的进一步增加部分受限于酶在疏水性碳材料上吸附时的失活。本研究采用了一种超嗜热酶，即超嗜热漆酶，通过 2,2'- azinobis(3-ethylbenzothiazoline-6-磺酸盐）和傅里叶变换红外光谱，分别与嗜温酶、花斑栓菌漆酶（表示为嗜温漆酶）和葡萄糖氧化酶（GOx）进行比较。与其他两种酶嗜温漆酶和 GOx 相比，超嗜热漆酶在吸附在 CB 上时保留了其特定活性和二级结构。