Enzymatic oxidation of organic compounds using discharge plasma

Enzymatic reactions offer the possibility to synthesize new molecules with high selectivity and turnover. Of particular interest are regio- or even stereo-selective oxidation reactions in order to obtain high value compounds. Peroxygenases are valuable biocatalysts to achive this goal since they use H2O2 (hydrogen peroxide) through the so called “peroxide shunt pathway”, eliminating the need for expensive electron donors, such as flavins or nicotinamide cofactors. However, the industrial application of peroxidases or peroxygenases is limited due to their partial or complete inactivation in the presence of higher concentrations of peroxides. Several strategies have been developed in order to supply low concentrations of H2O2 in situ. However, all of these known methods are ether inefficient or require the addition of extra components to the reaction, making them less efficient and more expensive. A German university developed a solution to this challenge. A plama device is employed to produce H2O2 in an aqueous solution in situ. The “activated” solution is guided to immobilized peroxidases or peroxygenases where the actual enzymatic oxidation of the substrate takes place. The inventors can show that selectivity of the enzymes is retained and stability of the immobilized enzyme is high. Employing UPO (unspecific peroxygenase) from the fungus Agrocybe aegerita as oxygenase and ethylbenzene as substrate, the inventors could show feasability of this approach. The university offers a licence agreement to the chemical or biotechnology industry. If the company is interested in the further development of the process, a research cooperation agreement is also possible.