School of Chemical and Biomolecular Engineering, University of Sydney, Darlington, NSW 2008, Australia.
School of Physics, Chemistry and Earth Sciences, University of Adelaide, Adelaide, SA 5005, Australia.
J Am Chem Soc. 2023 Sep 20;145(37):20365-20374. doi: 10.1021/jacs.3c05488. Epub 2023 Sep 6.
This study reports the successful development of a sustainable synthesis protocol for a phase-pure metal azolate framework (MAF-6) and its application in enzyme immobilization. An esterase@MAF-6 biocomposite was synthesized, and its catalytic performance was compared with that of esterase@ZIF-8 and esterase@ZIF-90 in transesterification reactions. Esterase@MAF-6, with its large pore aperture, showed superior enzymatic performance compared to esterase@ZIF-8 and esterase@ZIF-90 in catalyzing transesterification reactions using both -propanol and benzyl alcohol as reactants. The hydrophobic nature of the MAF-6 platform was shown to activate the immobilized esterase into its open-lid conformation, which exhibited a 1.5- and 4-times enzymatic activity as compared to free esterase in catalyzing transesterification reaction using -propanol and benzyl alcohol, respectively. The present work offers insights into the potential of MAF-6 as a promising matrix for enzyme immobilization and highlights the need to explore MOF matrices with expanded pore apertures to broaden their practical applications in biocatalysis.
本研究报告了一种用于纯相金属氮化物框架（MAF-6）的可持续合成方案的成功开发及其在酶固定化中的应用。合成了酯酶@MAF-6 生物复合材料，并将其催化性能与酯酶@ZIF-8 和酯酶@ZIF-90 在酯交换反应中的性能进行了比较。由于具有较大的孔径，酯酶@MAF-6 在以 -丙醇和苄醇为反应物的酯交换反应中表现出比酯酶@ZIF-8 和酯酶@ZIF-90 更优异的酶性能。MAF-6 平台的疏水性被证明可以将固定化的酯酶激活为开放盖构象，与游离酯酶相比，在使用 -丙醇和苄醇进行的酯交换反应中，其酶活性分别提高了 1.5 倍和 4 倍。本工作为 MAF-6 作为酶固定化的有前途的基质提供了新的见解，并强调需要探索具有扩展孔径的 MOF 基质，以拓宽其在生物催化中的实际应用。
