dc.description.abstract | Immobilized enzymes usually showed lower enzymatic activity than free ones after applying for additional materials or supports, which might influence substrates diffusion, active sites accessibility, subunit dissociation, conformational change, especially volume-confined immobilization. It is necessary to find the potential material which overcomes the above-mentioned shortcomings and provides shell protection for embedded biomolecules to against external denaturing agents. Therefore, metal-organic frameworks (MOFs) with tunable porosity, and variable internal surface property for a targeted application, might be a suitable candidate for advanced enzyme immobilization.
Recently, we reported a paper regrading an additional strength of the de novo approach by demonstrating that embedded enzymes in metal-organic frameworks (MOFs) via de novo approach remain biological functions under a wider range of reaction conditions such as urea. The enhanced stability of the of enzyme molecules arises from the confinement effects provided by MOF structure. However, the enzymatic activity is not as well as the activity of free enzymes, which might be caused by the influence of spatial confinement on the enzymatic functionality.
In order to further investigate the influence of spatial confinement on the enzymatic functionality, herein, we synthesized the new hollow structure of Zeolitic imidazolate frameworks (Hollow ZIF-8 and HZIF-90@ZnTA) by using a modified approach based on a recent report , which embedded enzymes inside of void structures that mimic cytoplasmic conditions with less restricted environment. Accordingly, this part work may contribute to investigate the hollow structure material and the influence of spatial confinement on the enzymatic functionality. | en_US |