Designable immobilization of D-allulose 3-epimerase on bimetallic organic frameworks based on metal ion compatibility for enhanced D-allulose production

• Published in: International journal of biological macromolecules 2024-07, Vol.273 (Pt 1), p.133027, Article 133027
• Main Authors: Tang, Huayang, Chen, Yian, Fan, Dexun, Zhao, Fengguang, Han, Shuangyan
• Format: Article
• Language: English
• Subjects: D-allulose; D-allulose 3-epmimerase; Metal organic frameworks; MOF immobilization enzyme
• ISSN: 0141-8130; 1879-0003; 1879-0003
• DOI: 10.1016/j.ijbiomac.2024.133027

D-allulose, a low-calorie rare sugar catalyzed by D-allulose 3-epimerase (DAE), is highly sought after for its potential health benefits. However, poor reusability and stability of DAE limited its popularization in industrial applications. Although metal-organic frameworks (MOFs) offer a promising enzyme platform for enzyme immobilization, developing customized strategies for MOF immobilization of enzymes remains challenging. In this study, we introduce a designable strategy involving the construction of bimetal-organic frameworks (ZnCo-MOF) based on metal ions compatibility. The DAE@MOFs materials were prepared and characterized, and the immobilization of DAE and the enzymatic characteristics of the MOF-immobilized DAE were subsequently evaluated. Remarkably, DAE@ZnCo-MOF exhibited superior recyclability which could maintain 95 % relative activity after 8 consecutive cycles. The storage stability is significantly improved compared to the free form, with a relative activity of 116 % remaining after 30 days. Molecular docking was also employed to investigate the interaction between DAE and the components of MOFs synthesis. The results demonstrate that the DAE@ZnCo-MOF exhibited enhanced catalytic efficiency and increased stability. This study introduces a viable and adaptable MOF-based immobilization strategy for enzymes, which holds the potential to expand the implementation of enzyme biocatalysts in a multitude of disciplines. •ZnCo-MOF was designed and prepared for D-allulose 3-epimerase (DAE) immobilization.•DAE@ZnCo-MOF shows enhanced stability and activity compared to free enzymes.•After recycling 8 times, DAE@ZnCo-MOF retained 95 % of its initial activity.•Customizable enzyme@MOFs design paves the way for diverse biocatalytic applications.