| dc.description.abstract | Metal organic frameworks(MOFs) composed by metal ions and organic linkers are porous materials which were emerging and developed rapidly in recent years. Many applications are contributed by high porosity and specific aperture of its structure. One of the MOF applications is used as the platform for enzyme immobilizations.
Recently, a de novo approach was used for encapsulating enzymes into MOFs materials, our group successfully preformed that biocomposites have been generated under aqueous and mild condition by encapsulating catalase, enzymes for hydrogen peroxide hydrolysis, into zeolitic imidazolate framework-90 (CAT@ZIF-90). By this approach, enzyme could not only be protected in protease solution by aperture size limitation but also reduce unfolding by MOF structure confinement which difficultly achieved by adsorption immobilization.
In addition to ZIFs with 3.5Å aperture which limited penetrability of large substrates, most of MOF materials are synthesized by solvothermal ways under harsh conditions such as organic solvent and high temperature etc. in which the biological activity of enzyme is hardly maintained. To this end, we thought out of the box and proposed another concept that takes the method of mechanochemical approach with advantages of rapidly time and almost non-solvent to immobilize enzymes inside of MOFs. We demonstrated a mechanochemical method for the facile preparation of biocomposites by embedding -glucosidase, enzymes for disaccharide hydrolysis, in a Zr-MOF analog, UiO-66-NH2 and also determined the apparent biological activity. UiO-66-NH2 has a large aperture and high acid resistance, thus demonstrating potential for size-shielding against protease as well as maintaining biological function. Thus, this study provides an alternative route for encapsulating enzymes into MOFs, especially for biocomposites that are difficult to obtain under mild aqueous conditions. | en_US |