Robust Light Driven Enzymatic Oxyfunctionalization via Immobilization of Unspecific Peroxygenase
Piera De Santis, Deborah Wegstein, Bastien O. Burek, Jacqueline Patzsch, Miguel Alcalde, Wolfgang Kroutil, Jonathan Z. Bloh, Selin Kara
Abstract
Abstract Unspecific peroxygenases have attracted interest in synthetic chemistry, especially for the oxidative activation of C−H bonds, as they only require hydrogen peroxide (H 2 O 2 ) instead of a cofactor. Due to their instability in even small amounts of H 2 O 2 , different strategies like enzyme immobilization or in situ H 2 O 2 production have been developed to improve the stability of these enzymes. While most strategies have been studied separately, a combination of photocatalysis with immobilized enzymes was only recently reported. To show the advantages and limiting factors of immobilized enzyme in a photobiocatalytic reaction, a comparison is made between free and immobilized enzymes. Adjustment of critical parameters such as (i) enzyme and substrate concentration, (ii) illumination wavelength and (iii) light intensity results in significantly increased enzyme stabilities of the immobilized variant. Moreover, under optimized conditions a turnover number of 334,500 was reached.