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Plasma‐driven in situ production of hydrogen peroxide for biocatalysis

Peroxidases and peroxygenases are promising classes of enzymes for biocatalysis because of their ability to carry out one‐electron oxidation reactions and stereoselective oxyfunctionalizations. However, industrial application is limited, as the major drawback is the sensitivity toward the required peroxide substrates. Herein, we report a novel biocatalysis approach to circumvent this shortcoming: in situ production of H2O2 by dielectric barrier discharge plasma. The discharge plasma can be controlled to produce hydrogen peroxide at desired rates, yielding desired concentrations. Using horseradish peroxidase, it is demonstrated that hydrogen peroxide produced by plasma treatment can drive the enzymatic oxidation of model substrates. Fungal peroxygenase is then employed to convert ethylbenzene to (R)‐1‐phenylethanol with an ee of >96 % using plasma‐generated hydrogen peroxide. As direct treatment of the reaction solution with plasma results in reduced enzyme activity, the use of plasma‐treated liquid and protection strategies are investigated to increase total turnover. Technical plasmas present a noninvasive means to drive peroxide‐based biotransformations.

FieldValue
Publisher
Authors
Release Date
2020-11-18
Rights
potential copyright conflict with publisher
Identifier
18687f98-d046-4c8b-8e12-3f45d4b2d128
Permanent Identifier (URI)
Is supplementing
Plasma Source Name
Plasma Source Application
Plasma Source Specification
Plasma Source Properties
V(RMS) = 13.5 kV, trigger frequency = 300 Hz, diameter=20 mm
Language
English (United States)
Plasma Source Procedure
Aqueous sample of different volumes (40-200) μl on glass support placed on grounded support. Distance between sample and DBD was 2 mm.
License
Plasma Medium Name
Plasma Medium Properties
uncontrolled
Plasma Target Name
Contact Name
Bandow, Julia E.
Plasma Target Properties
Horseradish peroxidase (P8375); unspecific Peroxygenase from Agrocybe aegerita, purified from Pichia pastoris expression strain; both enzymes in 100 mM KPi buffer, pH 7
Contact Email
Public Access Level
Restricted
Funding Agency
Project
Subproject

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