Liang, W.Flint, K.Yao, Y.Wu, J.Wang, L.Doonan, C.Huang, J.2023-09-262023-09-262023Journal of the American Chemical Society, 2023; 145(37):20365-203740002-78631520-5126https://hdl.handle.net/2440/139571This 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 n-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 n-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.en© 2023 American Chemical SocietyBiopolymers; encapsulation; metal organic frameworks; peptides and proteins; transesterificationJournal article10.1021/jacs.3c054882023-09-26655194Flint, K. [0000-0002-9043-8369]