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Immobilization of 5-Hydroxymethylfurfural Oxidase within MOFs for Catalysis |
Feng-qin GONG1,2,Qi-shun LIU2,Hai-dong TAN2,hua JIN3,Cheng-yu TAN1,**(),Heng YIN2,**() |
1 College of Marine Science and Environment, Dalian Ocean University, Dalian 116023, China 2 Dalian Institute of Chemical Physics, Chinese Academy of Sciences, CAS, Dalian 116023, China 3 College of Material and Engineering, Ningbo University, Ningbo 315211, China |
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Abstract Immobilized enzymes are biocatalysts that typically have higher functional efficiency and reproducibility than free enzymes. However, the use of enzyme immobilization is still limited, and the research is mainly conducted within model enzymes. In recent years, the study of metal organic frameworks (MOFs) as enzyme immobilization carriers has attracted great attention, and the nature of MOF-enzyme complexes remains to be elucidated. In the present study, a novel immobilized biocatalyst was prepared by embedding a 5-hydroxymethylfurfural oxidase (HMFO) in zeolite imidazole ester skeleton ZIF-8(a typical MOF) through biomimetic mineralization. The morphology of the composite catalyst under scanning electron microscope was different from the classical rhombohedral dodecahedron of MOF immobilized enzyme. Protein concentration assay conducted by Commassie brilliant blue G-250 method indicated that the immobilization efficiency was reached 89.0%. Moreover, the conversion efficiency of HMFO@ZIF-8 to 5-hydroxymethylfurfural reached 84.3%, and the yield and selectivity were significantly improved as compared to free HMFO.New knowledge for the research of MOFs immobilized enzymes and facilitates the development of immobilized biomacromolecules and synthetic biocatalysts were provided.
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Received: 30 October 2018
Published: 12 July 2019
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Corresponding Authors:
Cheng-yu TAN,Heng YIN
E-mail: tanchyu@dlou.edu.cn;yinheng@dicp.ac.cn
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