Unique Enzyme Activity of Peroxidase on a Clay Nanosheet
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) a...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 36(2020), 29 vom: 28. Juli, Seite 8384-8388 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2020
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Hydrogen Peroxide BBX060AN9V Horseradish Peroxidase EC 1.11.1.- Peroxidases Peroxidase EC 1.11.1.7 Clay T1FAD4SS2M |
| Zusammenfassung: | 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 |
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| Beschreibung: | Date Completed 21.06.2021 Date Revised 21.06.2021 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.0c00607 |