2020年7月28日
Unique Enzyme Activity of Peroxidase on a Clay Nanosheet
Langmuir
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- 巻
- 36
- 号
- 29
- 開始ページ
- 8384
- 終了ページ
- 8388
- 記述言語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1021/acs.langmuir.0c00607
Copyright © 2020 American Chemical Society. The adsorption behavior and enzyme activity of horseradish peroxidase (HRP) was examined on a synthetic clay nanosheet, whose surface is flat at the atomic level and is negatively charged. The results showed that HRP is adsorbed effectively (adsorption equilibrium constant, K = 1.61 × 107 L mol-1) and that the structure of HRP was altered on the clay surface. The enzyme activity of HRP on the clay surface was evaluated by using H2O2 and tert-BuOOH as a substrate. As a result, HRP on the clay surface was able to work for tert-BuOOH, while HRP in solution did not show any activity. In addition, HRP on SSA showed reactivity even under the high-temperature conditions. These results indicate that the clay nanosheet can be a unique modifier for enzyme activity of HRP.
- リンク情報
- ID情報
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- DOI : 10.1021/acs.langmuir.0c00607
- ISSN : 0743-7463
- eISSN : 1520-5827
- PubMed ID : 32407124
- SCOPUS ID : 85089611093