Related Experiment Video
Updated: May 13, 2026
Self-standing Electrochemical Set-up to Enrich Anode-respiring Bacteria On-site
Published on: July 24, 2018
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.
Abstract:
Deep eutectic solvents (DESs) are a group of emerging solvents for biocatalysis with tailored performance. Herein, we report the usage of hierarchical zeolitic imidazole framework-8 (HZIF-8) and halogenated DES for the immobilization of phenylalanine dehydrogenase. Effects of three different halogenated DESs (I, Cl and Br) on the activity of immobilized enzymes for production of homophenylalanine were studied. The optimal activity towards with the model reaction of catalyzing ethyl 2-oxo-4-phenylbutyrate (EOPB) to L-homophenylalanine was 6.11 U/mg at 70 °C, 5.4-fold of that of the free enzyme, with 78.4% of its original activity retained after six recycles. The immobilized enzymes were further loaded on a poly(methylene blue) electrode with electrochemical NAD+ regeneration, leading to bioelectrosynthesis of phenylpyruvate. Using phenylalanine-ethanolamine (Phe-MEA) as the substrate, 13.85 mM phenylpyruvate was obtained after 8 h, with a total turnover number (TTN) value of 138.5 for NADH regeneration, while a TTN of 102.2 using L-Phe as the substrate.
More Related Videos
10:23Characterizing Mediated Extracellular Electron Transfer in Lactic Acid Bacteria with a Three-Electrode, Two-Chamber Bioelectrochemical System
Published on: August 23, 2024
09:00Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1
Published on: April 16, 2018