Biomineralization has recently emerged as a highly effective strategy for enzyme immobilization. Zeolitic imidazolate frameworks (ZIFs), a subclass of metal–organic frameworks (MOFs), are particularly attractive carriers due to their structural tunability and chemical stability. While ZIF-8 has been extensively studied, its denser and thermodynamically more stable analog ZIF-zni has received far less attention. In this work, we report the biomineralization of glucose oxidase (GOx) from Aspergillus niger within the ZIF-zni framework and systematically investigate the influence of zinc and imidazole (Im) concentration on immobilization performance. The optimized biocomposite, obtained at 10 mM Zn2+ and a Zn:Im ratio of 1:10, exhibited a specific activity of 2051 IU g−1, which is more than twice the activity obtained for GOx@ZIF-8 in our previous study (874 IU g−1). Furthermore, the GOx@ZIF-zni biocomposite demonstrated remarkable resistance to sodium dodecyl sulfate (SDS) and retained up to 50% of its activity after incubation at 65 °C for one hour. These results demonstrate that ZIF-zni is a highly promising carrier for enzyme immobilization and suggest that framework topology and synthesis conditions play a crucial role in determining the catalytic performance and stability of enzyme@MOF biocomposites.
Stanišić et al. (2026) studied this question.