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Gewählte Publikation:

Goncalves, LCP; Kracher, D; Milker, S; Fink, MJ; Rudroff, F; Ludwig, R; Bommarius, AS; Mihovilovic, MD.
(2017): Mutagenesis-Independent Stabilization of Class B Flavin Monooxygenases in Operation
ADV SYNTH CATAL. 2017; 359(12): 2121-2131. FullText FullText_BOKU

This paper describes the stabilization of flavin-dependent monooxygenases under reaction conditions, using an engineered formulation of additives (the natural cofactors NADPH and FAD, and superoxide dismutase and catalase as catalytic antioxidants). This way, a 10(3)- to 10(4)-fold increase of the half-life was reached without resource-intensive directed evolution or structure-dependent protein engineering methods. The stabilized enzymes are highly valued for their synthetic potential in biotechnology and medicinal chemistry (enantioselective sulfur, nitrogen and Baeyer-Villiger oxidations; oxidative human metabolism), but widespread application was so far hindered by their notorious fragility. Our technology immediately enables their use, does not require structural knowledge of the biocatalyst, and creates a strong basis for the targeted development of improved variants by mutagenesis.
Autor/innen der BOKU Wien:
Kracher Daniel
Ludwig Roland
BOKU Gendermonitor:

Find related publications in this database (Keywords)
enzyme stabilization
reactive oxygen species

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