Active site engineering of Zn-doped mesoporous ceria toward highly efficient organophosphorus hydrolase-mimicking nanozyme
- Authors
- Lee, Junsang; Le, Xuan Ai; Chun, Hoje; Vu, Trung Hieu; Choi, Daeeun; Han, Byungchan; Kim, Moon Il; Lee, Jinwoo
- Issue Date
- Feb-2024
- Publisher
- ELSEVIER ADVANCED TECHNOLOGY
- Keywords
- Active site engineering; Density functional theory; Mesoporous ceria; Nanozyme; Organophosphorus hydrolase mimic; Paraoxon biosensing
- Citation
- Biosensors and Bioelectronics, v.246
- Journal Title
- Biosensors and Bioelectronics
- Volume
- 246
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/89689
- DOI
- 10.1016/j.bios.2023.115882
- ISSN
- 0956-5663
1873-4235
- Abstract
- Hydrolase-mimicking nanozymes have received increasing attention in recent years, but the effective rational design and development of these materials has not been realized, as they are not at present considered a critical research target. Herein, we report that Zn-doped mesoporous ceria (Zn-m-ceria) engineered to have an abundance of two different active sites with different functions—one that allows both co-adsorption binding of organophosphate (OP) and water and another that serves as a general base—has significant organophosphorus hydrolase (OPH)-like catalytic activity. Specifically, Zn-m-ceria exhibits a catalytic efficiency over 75- and 25-fold higher than those of m-ceria and natural OPH, respectively. First-principles calculations reveal the importance of Zn for the OPH-mimicking activity of the material, promoting substrate adsorption and proton-binding. The OPH-like Zn-m-ceria catalyst is successfully applied to detect a model OP, methyl paraoxon, in spiked tap water samples with excellent sensitivity, stability, and detection precision. We expect that these findings will promote research based on the rational engineering of the active site of nanozymes and efficient strategies for obtaining a diverse range of catalysts that mimic natural enzymes, and hence the utilization in real-world applications of enzyme-mimicking catalysts with properties superior to their natural analogs should follow. © 2023 Elsevier B.V.
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