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- W2612185815 abstract "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 103- to 104-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." @default.
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- W2612185815 date "2017-05-19" @default.
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- W2612185815 title "Mutagenesis-Independent Stabilization of Class B Flavin Monooxygenases in Operation" @default.
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- W2612185815 doi "https://doi.org/10.1002/adsc.201700585" @default.
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