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Nano Research 2024, 17(1): 290-296 https://doi.org/10.1007/s12274-023-5811-y
Research Article | Issue | Published: 15 July 2023

Metal-organic framework hybrid materials of ZIF-8/RGO for immobilization of D-amino acid dehydrogenase

Show Author's Information Hangbin Lei1,  Qian Zhang1,  Xiaoyan Xiang1,  Liang Jiang1,  Shiyan Wang1,  Lingxuan Duan1,  Shizhen Wang1,2( )
Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China
Xiamen Key Laboratory of Synthetic Biotechnology, Xiamen University, Xiamen 361005, China
Keywords:
metal-organic frameworks, reduced graphene oxide, immobilization, D-Amino acid dehydrogenase, zeolitic imidazolate framework-8 (ZIF-8)
Topics:
Catalytic
Cite this article:
Lei H, Zhang Q, Xiang X, et al. Metal-organic framework hybrid materials of ZIF-8/RGO for immobilization of D-amino acid dehydrogenase. Nano Research, 2024, 17(1): 290-296. https://doi.org/10.1007/s12274-023-5811-y
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Abstract Full text Electronic supplementary material About this article

Immobilization of D-amino acid dehydrogenase (DAADH) by the assembly of peptide linker was studied for the biosynthesis of D-phenylalanine. Hybrid material of zeolitic imidazolate framework-8 (ZIF-8) combined with reduced graphene oxide (RGO) was applied for the immobilization of DAADH from Ureibacillus thermosphaericus. The recovery rate of DAADH/ZIF-8/RGO was 165.6%. DAADH/ZIF-8/RGO remained 53.4% of its initial activity at 50 °C for 10 h while the free enzyme was inactivated. DAADH/ZIF-8/RGO maintained 70.5% activity in hyperalkaline solution with pH 12. Kinetic parameters indicated that DAADH/ZIF-8/RGO had greater affinity of phenylpyruvate as Vmax/Km of DAADH/ZIF-8/RGO was 1.27-fold than free enzyme. After seven recycles, the activity of DAADH/ZIF-8/RGO remained 64.3%. Furthermore, one-step separation and in situ immobilization of DAADH by ZIF-8/RGO/Ni was carried out with 1.5-fold activity enhancement. Combining peptide linker and metal-organic framework (MOF) immobilization, thermostability and activity of the immobilized DAADH were significantly improved.


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About this article

Metal-organic framework hybrid materials of ZIF-8/RGO for immobilization of D-amino acid dehydrogenase

Show Author's information Hangbin Lei1, Qian Zhang1, Xiaoyan Xiang1, Liang Jiang1, Shiyan Wang1, Lingxuan Duan1, Shizhen Wang1,2( )
Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China
Xiamen Key Laboratory of Synthetic Biotechnology, Xiamen University, Xiamen 361005, China

Abstract

Immobilization of D-amino acid dehydrogenase (DAADH) by the assembly of peptide linker was studied for the biosynthesis of D-phenylalanine. Hybrid material of zeolitic imidazolate framework-8 (ZIF-8) combined with reduced graphene oxide (RGO) was applied for the immobilization of DAADH from Ureibacillus thermosphaericus. The recovery rate of DAADH/ZIF-8/RGO was 165.6%. DAADH/ZIF-8/RGO remained 53.4% of its initial activity at 50 °C for 10 h while the free enzyme was inactivated. DAADH/ZIF-8/RGO maintained 70.5% activity in hyperalkaline solution with pH 12. Kinetic parameters indicated that DAADH/ZIF-8/RGO had greater affinity of phenylpyruvate as Vmax/Km of DAADH/ZIF-8/RGO was 1.27-fold than free enzyme. After seven recycles, the activity of DAADH/ZIF-8/RGO remained 64.3%. Furthermore, one-step separation and in situ immobilization of DAADH by ZIF-8/RGO/Ni was carried out with 1.5-fold activity enhancement. Combining peptide linker and metal-organic framework (MOF) immobilization, thermostability and activity of the immobilized DAADH were significantly improved.

Keywords: metal-organic frameworks, reduced graphene oxide, immobilization, D-Amino acid dehydrogenase, zeolitic imidazolate framework-8 (ZIF-8)

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Publication history
Copyright
Acknowledgements

Publication history

Received: 07 December 2022
Revised: 25 April 2023
Accepted: 07 May 2023
Published: 15 July 2023
Issue date: January 2024

Copyright

© Tsinghua University Press 2023

Acknowledgements

Acknowledgements

This work was supported by the National Natural Science Foundation of China (Nos. 21776233 and 22078273) and National Key Research and Development Program (No. 2022YFA0912000).

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