| dc.description.abstract | Enzymes have characteristics such as promoting biochemical reactions and specificity, making them widely applicable. However, their low tolerance to environmental conditions necessitates immobilization to enhance stability and enable recycling to reduce costs. Metal-organic frameworks (MOFs), with their porous nature and high stability, are well-suited as enzyme carriers. Therefore, in 2015, our laboratory developed a de novo approach for encapsulating catalase (CAT) in zeolitic imidazolate framework-90 (ZIF-90). While this method provided a new perspective on enzyme immobilization, it was time-consuming and only applicable to specific MOFs. Consequently, in 2019, we adopted the liquid-assisted grinding (LAG) to encapsulate enzymes in MOFs such as UiO-66-NH2. However, this method still required optimization, such as the use of organic solvents, a synthesis time of up to five minutes, a two-step encapsulation process instead of a one-pot method, and the inability to encapsulate enzymes in single crystals. Improving these synthesis drawbacks would undoubtedly enhance the competitiveness of the LAG method.
This paper successfully synthesized single-crystal encapsulated enzyme-MOF biocomposites, CAT@ZIF-90, in 10 seconds using the LAG. Compared to our previous research, the enzyme activity increased from 2.68 × 10−2 to 1.98 × 10−1. To further understand the synthesis mechanism of enzyme-MOF biocomposites, different solutions were used for LAG, successfully deducing the criteria for selecting buffer solutions for synthesizing other types of MOFs using the LAG. Based on these results, a study to improve the loading of enzyme-MOF biocomposites was conducted, achieving a maximum loading of approximately 34%, and formulating a new strategy that effectively enhances the loading. | en_US |