4.7 Article

Three-dimensional ordered magnetic macroporous metal-organic frameworks for enzyme immobilization

Journal

JOURNAL OF COLLOID AND INTERFACE SCIENCE
Volume 590, Issue -, Pages 436-445

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jcis.2021.01.078

Keywords

Metal-organic frameworks (MOFs); Ordered macropores structure; Polystyrene template; Immobilized enzymes; Immobilization efficiency

Funding

  1. Science and Technology Program of Tianjin, China [20ZYJDJC00080]
  2. National Natural Science Foundation of China [21676069]
  3. Innovation Project of Excellent Doctoral Dissertation of Tianjin University of Science and Technology [2019010]
  4. Postgraduate Research Innovation project of Tianjin [2020YJSB122]

Ask authors/readers for more resources

A novel magnetic amino-functionalized ZIF-8 with highly ordered macroporous structure was successfully synthesized using PS nanosphere monoliths as a template, and catalase molecules were immobilized with high efficiency and loading capacity. The immobilized CAT showed 500% higher activity than CAT/ZIF-8 and maintained 90% activity after 8 cycles of reuse, indicating excellent recyclability and enhanced activity.
Metal-organic frameworks (MOFs) have been emerged as a promising support for immobilizing enzymes owing to the tunable porosity, high surface area, and structural diversity. However, most of these possess nanometer size and small pores, which are difficult to recover them from the reaction medium and present low immobilization efficiency and protein loading capacity, and high substrate diffusion limitations. Herein, a novel magnetic amino-functionalized zeolitic imidazolate framework-8 (ZIF-8) with 3D highly ordered macroporous structure was synthesized using the assembled polystyrene (PS) nanosphere monoliths as a template. Subsequently, catalase (CAT) molecules were immobilized on the surface of macroporous magnetic ZIF-8 and inside the macropores by precipitation, covalent binding and crosslinking. The resultant immobilized CAT showed high immobilization efficiency (58%) and protein loading capacity (29%), leading to 500% higher activity than the immobilized CAT on ZIF-8 (CAT/ZIF-8). Meanwhile, the immobilized CAT could be easily recovered with a magnet without obvious activity loss. The traditional CAT/ZIF-8 lost its activity after 6 cycles, whereas, the immobilized CAT retained 90% activity of its initial activity after reusing for 8 cycles, indicating excellent reusability. In conclusion, this study provides a facile and efficient approach to immobilize enzymes on/in MOFs with enhanced activity and excellent recyclability. (c) 2021 Elsevier Inc. All rights reserved.

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