Baeyer-Villiger biocatalyst

Scheme 3.90 Extensive substrate profiling of cyclopentadecanone monooxygenase as Baeyer-Villiger biocatalyst reveals novel regiodivergent oxidations [65d].

M.J. Fink, T.C. Fischer, F. Rudroff, H. Dudek, M.W. Fraaije, M.D. Mihovilovic, Extensive substrate profiling of cyclopentadecanone monooxygenase as Baeyer-Villiger biocatalyst reveals... 

Oxidoreductases are, after lipases, the second most-used kinds of biocatalysts in organic synthesis. Two main processes have been reported using this type of enzymes-bioreduction of carbonyl groups [39] and biohydroxylation of non-activated substrates [40]. However, in recent few years other processes such as deracemization of amines or alcohols [41] and enzymatic Baeyer-Villiger reactions of ketones and aldehydes [42] are being used with great utility in asymmetric synthesis. 

When comparing chemical and biocatalytic methods, one could say that, especially for asymmetric oxidations, enzymatic methods enter the scene. This is most evident in the area of asymmetric Baeyer-Villiger oxidation, where biocatalysts take the lead and homogeneous chiral catalysts lag far behind in terms of ee values. Significant progress can be expected in the area of biocatalysis due to the advancement in enzyme production technologies and the possibility of tailor-made enzymes. 

Kamerbeek, N.M., Janssen, D.B., van Berkel, W.J.H. and Fraaije, M.W. (2003) Baeyer-Villiger monooxygenases, an emerging family of flavin-dependent biocatalysts. Advanced Synthesis Catalysis, 345, 667-678. 

Advances in Regeneration Systems of BVMOs Additional contributions to the proliferation of the Baeyer-Villiger biotransformation platform is the combination of the catalytic activity of a redox biocatalyst with concomitant coenzyme recycling in a single fusion protein, reported by Mihovilovic and Fraaije (Scheme 10.3) [102]. 

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