For complex cascade biocatalysis, multienzyme compartmentalization helps to optimize substrate transport channels and promote the orderly and tunable progress of step reactions. Herein, a simple and general synthesis strategy is proposed for the construction of a multienzyme biocatalyst by compartmentalizing glucose oxidase and horseradish peroxidase (GOx and HRP) within core-shell zeolite imidazole frameworks (ZIF)-8@ZIF-8 nanostructures. Owing to the combined effects of biomimetic mineralization and the fine regulation of the ZIF-8 growth process, the uniform shell encloses the seed (core) surface by epitaxial growth, and the bienzyme system is accurately localized in a controlled manner. The versatility of this strategy is also reflected in ZIF-67. Meanwhile, with the ability to covalently bind divalent metal ions, lithocholic acid (LCA) is used as a competitive ligand to improve the pore structure of the ZIF from a single micropore to a hierarchical micro/mesopore network, which greatly increases mass transfer efficiency. Furthermore, the multienzyme cascade reaction is exemplified by the oxidation of o-phenylenediamine (OPD). The findings show that the bienzyme assembly strategy significantly affects the biocatalytic efficiency mainly by influencing the utilization efficiency of the intermediate (Hydrogen peroxide, H2 O2 ) between the step reactions. This study sheds new light on facile synthetic routes to constructing in vitro multienzyme biocatalysts.
Keywords: cascade biocatalysis; compartmented multienzymes; core-shell zeolitic imidazole frameworks; lithocholic acid; positional assembly strategies.
© 2022 Wiley-VCH GmbH.