Retention of activity and secondary structure of hyperthermophilic laccase adsorbed on carbon black

Retention of activity and secondary structure of hyperthermophilic laccase adsorbed on carbon black
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吸附在炭黑上的超耐热漆酶的活性和二级结构的保留

DOI:
10.1088/2515-7655/abe2f6
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发表时间:
2021
期刊:
Journal of Physics: Energy
影响因子:
--
通讯作者:
Takeo Yamaguchi
Takeo Yamaguchi
中科院分区:
--
文献类型:
--
作者:
Takanori Tamaki;Tomoharu Sugiyama;Yuhei Oshiba;Takeo Yamaguchi

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生物燃料电池电流密度的进一步增加在一定程度上受到疏水碳材料吸附后酶失活的限制。采用一种超嗜热酶——超嗜热漆酶,分别用2,2′-氮化氮(3-乙基苯并噻唑啉-6-磺酸盐)的氧化速率和傅里叶变换红外光谱法,与中温漆酶——墨脱菌漆酶(简称中温漆酶)和葡萄糖氧化酶(GOx)进行比较,研究了其在炭黑(CB)上吸附后活性和二级结构的变化。与中温漆酶和GOx酶相比,超嗜热漆酶在CB上的吸附保留了其特定的活性和二级结构。
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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