Copper dehydrogenases derived from multi-copper oxidases and their bioelectrochemical applications

By modifying copper dehydrogenases of multi-copper oxidases to reduce oxidative activity and enhance dehydrogenative activity, the problems of poor stability and oxygen competition for electron transfer of tyrosinase and horseradish peroxidase are solved, achieving efficient and selective detection of L-DOPA, which is suitable for the treatment and management of Parkinson's disease patients.

JP2026522239APending Publication Date: 2026-07-07THE UNIV OF NORTH CAROLINA AT CHAPEL HILL

Patent Information

Authority / Receiving Office
JP · JP
Patent Type
Applications
Current Assignee / Owner
THE UNIV OF NORTH CAROLINA AT CHAPEL HILL
Filing Date
2024-05-30
Publication Date
2026-07-07

AI Technical Summary

Technical Problem

Existing tyrosinases and horseradish peroxidases exhibit poor stability and are easily inhibited by reaction products when monitoring phenolic compounds, and require hydrogen peroxide for catalysis, limiting their practical applications; in the case of native multi-copper oxidases, oxygen competes for electrons during electron transfer, affecting electrode reaction efficiency.

Method used

To develop a copper dehydrogenase that reduces oxidative activity and enhances dehydrogenation activity by modifying a multi-copper oxidase, particularly by modifying the amino acid residues of the T2 and T3 copper ligands to improve selectivity and sustained detection of substrates such as L-DOPA.

Benefits of technology

It enables efficient and selective detection of L-DOPA, which is suitable for the treatment and management of Parkinson's disease patients, improves the accuracy and safety of drug management, and reduces the risk of drug toxicity.

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Abstract

Copper dehydrogenase enzymes engineered from multi-copper oxidases to have reduced oxidase activity are described. Oxygen-insensitive copper dehydrogenases catalyze the dehydrogenation of phenolic substrates on electrodes to generate an electric current. Compositions, devices, kits, and methods for assaying L-DOPA using copper dehydrogenases are disclosed. Anodes, enzyme fuel cells, and batteries are disclosed along with substrate-immobilized copper dehydrogenases.
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