Panferov Vasily G, Zhang Wenjun, D'Abruzzo Nicholas, Wang Sihan, Liu Juewen
Department of Chemistry, Waterloo Institute for Nanotechnology, University of Waterloo, Ontario N2L 3G1, Canada.
A.N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Prospect 33, Moscow 119071, Russia.
ACS Nano. 2024 Dec 24;18(51):34870-34883. doi: 10.1021/acsnano.4c12539. Epub 2024 Dec 12.
In contrast to homogeneous enzyme catalysis, nanozymes are nanosized heterogeneous catalysts that perform reactions on a rigid surface. This fundamental difference between enzymes and nanozymes is often overlooked in kinetic studies and practical applications. In this article, using 14 nanozymes of various compositions (core@shell, metal-organic frameworks, metal, and metal oxide nanoparticles), we systematically demonstrate that nontypical features of nanozymes, such as multiple catalytic activities, chemical transformations, and aggregation, need to be considered in nanozyme catalysis. Ignoring these features results in the inaccurate quantification of catalytic activity. Neglecting the multiple activities led to a six-time underestimation of MnO oxidation activity and mischaracterization of this material as a low-active peroxidase-mimicking nanozyme. Additionally, overlooking chemical stability during catalytic reactions led to the reporting of high peroxidase-mimicking activity for Au@Ag nanoparticles, which, in reality, exhibited no intrinsic activity and oxidized the substrate through the leakage of Ag ions. Ignoring the chemical stability of Au@Prussian Blue nanoparticles may lead to more than four times overestimation of peroxidase-mimicking activity after just 24 h of storage. Finally, disregarding the colloidal stability of nanozymes led to a five-time inaccuracy in catalytic activity. These findings underscore the necessity of optimizing procedures to account for these factors in nanozyme kinetic measurements, which will in turn ensure more reliable biosensors and the success of other practical applications.
与均相酶催化不同，纳米酶是在刚性表面上进行反应的纳米级非均相催化剂。酶和纳米酶之间的这一根本差异在动力学研究和实际应用中常常被忽视。在本文中，我们使用14种不同组成的纳米酶（核壳结构、金属有机框架、金属和金属氧化物纳米颗粒），系统地证明了在纳米酶催化中需要考虑纳米酶的非典型特征，如多种催化活性、化学转化和聚集。忽略这些特征会导致催化活性的定量不准确。忽略多种活性导致对MnO氧化活性的低估达六倍，并将该材料错误地表征为低活性过氧化物酶模拟纳米酶。此外，在催化反应过程中忽略化学稳定性导致报道Au@Ag纳米颗粒具有高过氧化物酶模拟活性，而实际上它们没有内在活性，而是通过Ag离子泄漏氧化底物。忽略Au@普鲁士蓝纳米颗粒的化学稳定性可能导致在储存仅24小时后过氧化物酶模拟活性被高估四倍以上。最后，忽略纳米酶的胶体稳定性导致催化活性的测量出现五倍的误差。这些发现强调了优化程序以在纳米酶动力学测量中考虑这些因素的必要性，这反过来将确保更可靠的生物传感器以及其他实际应用的成功。
