<p>Hierarchical mesoporous ZIF-8 (HZIF-8) was synthesized using a thermosensitive hydrogel as a soft template. Zinc ions (Zn<sup>2+</sup>) were uniformly dispersed on the hydrogel surface through metal-ion coordination with salicylic acid and melamine, followed by coordination with 2-methylimidazole at room temperature. After the thermal removal of salicylic acid and melamine, HZIF-8 was obtained which exhibited a bimodal pore structure comprising both micropores and mesopores. α-Glucosidase (α-Glu) was encapsulated into HZIF-8 via an in-situ diffusion method to construct an immobilized α-Glu microreactor. The morphological and structural characteristics of HZIF-8 before and after α-Glu immobilization were thoroughly characterized using Fourier transform infrared spectroscopy (FT-IR), electron microscopy, X-ray diffraction (XRD), and Brunauer-Emmet-Teller (BET) analysis. The immobilization optimization studies revealed that the optimal immobilization time was 3&#xa0;h, and the ideal mass ratio of HZIF-8 to α-Glu was 5:2 (w/w). Under these conditions, the α-Glu loading capacity reached 82.09&#xa0;μg/mg, and the immobilized α-Glu microreactor still retained 70% enzyme activity after seven cycles. The application of the&#xa0;HZIF-8-α-Glu microreactor was verified by coupling with high performance liquid chromatography (HPLC) for the offline screening of α-Glu inhibitors in green tea extract. The experimental results demonstrated the application of the immobilized α-Glu microreactor by screening out catechin and epicatechin gallate from the tea extract.</p> Graphical Abstract <p></p>

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Hierarchical mesoporous ZIF-8–immobilized enzyme microreactor coupled with HPLC for screening of α-glucosidase inhibitors from green tea

  • Ruobing Wu,
  • Xiangrong Wu,
  • Chenjia Jiang,
  • Haodong Zhou,
  • Jinhua Zhu,
  • Zaved H. Khan

摘要

Hierarchical mesoporous ZIF-8 (HZIF-8) was synthesized using a thermosensitive hydrogel as a soft template. Zinc ions (Zn2+) were uniformly dispersed on the hydrogel surface through metal-ion coordination with salicylic acid and melamine, followed by coordination with 2-methylimidazole at room temperature. After the thermal removal of salicylic acid and melamine, HZIF-8 was obtained which exhibited a bimodal pore structure comprising both micropores and mesopores. α-Glucosidase (α-Glu) was encapsulated into HZIF-8 via an in-situ diffusion method to construct an immobilized α-Glu microreactor. The morphological and structural characteristics of HZIF-8 before and after α-Glu immobilization were thoroughly characterized using Fourier transform infrared spectroscopy (FT-IR), electron microscopy, X-ray diffraction (XRD), and Brunauer-Emmet-Teller (BET) analysis. The immobilization optimization studies revealed that the optimal immobilization time was 3 h, and the ideal mass ratio of HZIF-8 to α-Glu was 5:2 (w/w). Under these conditions, the α-Glu loading capacity reached 82.09 μg/mg, and the immobilized α-Glu microreactor still retained 70% enzyme activity after seven cycles. The application of the HZIF-8-α-Glu microreactor was verified by coupling with high performance liquid chromatography (HPLC) for the offline screening of α-Glu inhibitors in green tea extract. The experimental results demonstrated the application of the immobilized α-Glu microreactor by screening out catechin and epicatechin gallate from the tea extract.

Graphical Abstract