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Designable immobilization of D-allulose 3-epimerase on bimetallic organic frameworks based on metal ion compatibility for enhanced D-allulose production.
Tang, Huayang; Chen, Yian; Fan, Dexun; Zhao, Fengguang; Han, Shuangyan.
Affiliation
  • Tang H; Guangdong Key Laboratory of Fermentation and Enzyme Engineering, School of Biology and Biological Engineering, South China University of Technology, Guangzhou 510640, PR China.
  • Chen Y; State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, PR China.
  • Fan D; Guangdong Key Laboratory of Fermentation and Enzyme Engineering, School of Biology and Biological Engineering, South China University of Technology, Guangzhou 510640, PR China.
  • Zhao F; School of Light Industry and Engineering, South China University of Technology, Guangzhou, 510640, PR China.
  • Han S; Guangdong Key Laboratory of Fermentation and Enzyme Engineering, School of Biology and Biological Engineering, South China University of Technology, Guangzhou 510640, PR China. Electronic address: syhan@scut.edu.cn.
Int J Biol Macromol ; 273(Pt 1): 133027, 2024 Jul.
Article in En | MEDLINE | ID: mdl-38857717
ABSTRACT
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Enzymes, Immobilized / Molecular Docking Simulation / Metal-Organic Frameworks Language: En Journal: Int J Biol Macromol Year: 2024 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Enzymes, Immobilized / Molecular Docking Simulation / Metal-Organic Frameworks Language: En Journal: Int J Biol Macromol Year: 2024 Document type: Article