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Deep eutectic solvent tailoring the electrode-enzyme interface for phenylalanine dehydrogenase immobilization and

Jintian Zhang1, Feixuan Li1, Xiaoyan Xiang1

  • 1Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.

Bioelectrochemistry (Amsterdam, Netherlands)
|May 11, 2026
PubMed
Summary

Hierarchical zeolitic imidazole framework-8 and halogenated deep eutectic solvents (DESs) successfully immobilized phenylalanine dehydrogenase. This enhanced enzyme stability and activity for L-homophenylalanine production and bioelectrosynthesis.

Keywords:
Amino dehydrogenaseBioelectrosynthesisCoenzyme regenerationDeep eutectic solvents

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Area of Science:

  • Biocatalysis and enzyme immobilization
  • Green chemistry and sustainable solvents
  • Bioelectrosynthesis and electrochemical regeneration

Background:

  • Deep eutectic solvents (DESs) offer tunable properties for enzyme immobilization.
  • Hierarchical zeolitic imidazole framework-8 (HZIF-8) provides a robust support structure.
  • Phenylalanine dehydrogenase is crucial for amino acid synthesis and cofactor regeneration.

Purpose of the Study:

  • To investigate the efficacy of HZIF-8 and halogenated DESs for immobilizing phenylalanine dehydrogenase.
  • To optimize enzyme activity and stability for L-homophenylalanine production.
  • To develop a bioelectrosynthetic system for phenylpyruvate production using immobilized enzymes and electrochemical regeneration.

Main Methods:

  • Immobilization of phenylalanine dehydrogenase onto HZIF-8 using three halogenated DESs (I, Cl, Br).
  • Enzyme activity assays for L-homophenylalanine production from ethyl 2-oxo-4-phenylbutyrate (EOPB).
  • Stability studies through multiple reaction cycles.
  • Integration of immobilized enzyme onto a poly(methylene blue) electrode for electrochemical NAD+ regeneration.
  • Bioelectrosynthesis of phenylpyruvate using phenylalanine-ethanolamine (Phe-MEA) or L-phenylalanine (L-Phe) as substrates.

Main Results:

  • Optimal activity of 6.11 U/mg achieved at 70°C with a 5.4-fold increase compared to the free enzyme.
  • 78.4% of original enzyme activity retained after six recycles.
  • Successful bioelectrosynthesis of phenylpyruvate, yielding 13.85 mM using Phe-MEA.
  • High total turnover numbers (TTN) for NADH regeneration: 138.5 (Phe-MEA) and 102.2 (L-Phe).

Conclusions:

  • HZIF-8 combined with halogenated DESs is an effective system for phenylalanine dehydrogenase immobilization.
  • The immobilized enzyme exhibits enhanced stability and activity, enabling efficient biocatalysis.
  • The developed bioelectrosynthetic approach offers a sustainable method for phenylpyruvate production with efficient cofactor regeneration.