Department of Radiology, Sun Yat-sen Memorial Hospital, Sun Yat-sen University, Guangzhou 510120, China.
MOE Key Laboratory of Bioinorganic and Synthetic ChemistrySchool of Chemistry, Sun Yat-sen University, Guangzhou 510275, China.
ACS Appl Mater Interfaces. 2020 Dec 23;12(51):57343-57351. doi: 10.1021/acsami.0c16689. Epub 2020 Dec 9.
Metal-organic frameworks (MOFs) have become a promising accommodation for enzyme immobilization and protection. However, the integration of multienzymes into MOFs may result in compromise of individual enzymatic activity. In this work, we report an iron mineralization strategy to facilely construct a mesoporous MOF, possessing excellent peroxidase-mimic bioactivity. Furthermore, the feasibility of in situ encapsulating natural enzymes within the developed mesoporous MOF nanozymes endows these natural/nanomimic enzyme hybrids with remarkably enhanced synergistic catalysis ability. Such activity enhancement is mainly due to (1) the fast flux rate of substances through the interconnected mesoporous channels and (2) the simultaneously increased loading amount of enzymes and iron within the MOFs caused by the iron mineralization process.
金属-有机框架（MOFs）已成为酶固定化和保护的有前途的方法。然而，将多种酶整合到 MOFs 中可能会导致单个酶活性受损。在这项工作中，我们报告了一种铁矿化策略，可轻松构建具有出色过氧化物酶模拟生物活性的介孔 MOF。此外，在开发的介孔 MOF 纳米酶中原位封装天然酶的可行性使这些天然/纳米模拟酶杂化物具有显著增强的协同催化能力。这种活性增强主要归因于（1）通过互连成孔的介孔通道的物质快速通量，以及（2）铁矿化过程中 MOFs 内酶和铁的同时增加的负载量。
