62701-49-9Relevant academic research and scientific papers
Biocatalytic Racemization Employing TeSADH: Substrate Scope and Organic Solvent Compatibility for Dynamic Kinetic Resolution
Pop?oński, Jaros?aw,Reiter, Tamara,Kroutil, Wolfgang
, p. 763 - 768 (2018/02/27)
Racemization in combination with a kinetic resolution is the base for a dynamic kinetic resolution (DKR). Biocatalytic racemization was successfully performed for a broad scope of sec-alcohols by employing a single alcohol dehydrogenase (ADH) variant from Thermoanaerobacter pseudoethanolicus (formerly T. ethanolicus; TeSADH W110A I86A C295A). The catalyst employed as a lyophilized whole cell preparation or cell free extract, which tolerated various non-water miscible organic solvents under micro-aqueous or two-phase conditions, whereby cyclohexane and n-hexane suited best. Various concepts for combining the enzymatic racemization with an enzymatic kinetic resolution to achieve overall a bis-enzymatic DKR were evaluated. A proof of concept showed a successful DKR with racemization in aqueous phase combined with acylation in the organic phase.
ALKANE OXIDATION BY MODIFIED HYDROXYLASES
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Paragraph 0323; 0324, (2016/02/16)
This invention relates to modified hydroxylases. The invention further relates to cells expressing such modified hydroxylases and methods of producing hydroxylated alkanes by contacting a suitable substrate with such cells.
Bioproduction of chiral epoxyalkanes using styrene monooxygenase from rhodococcus sp. ST-10 (RhSMO)
Toda, Hiroshi,Imae, Ryouta,Itoh, Nobuya
supporting information, p. 3443 - 3450 (2015/02/05)
We describe the enantioselective epoxidation of straight-chain aliphatic alkenes using a biocatalytic system containing styrene monooxygenase from Rhodococcus sp. ST-10 and alcohol dehydrogenase from Leifsonia sp. S749. The biocatalyzed enantiomeric epoxidation of 1-hexene to (S)-1,2-epoxyhexane (44.6 mM) using 2-propanol as the hydrogen donor was achieved under optimized conditions. The biocatalyst had broad substrate specificity for various aliphatic alkenes, including terminal, internal, unfunctionalized, and di- and tri-substituted alkenes. Here, we demonstrate that this biocatalytic system is suitable for the efficient production of enantioenriched (S)-epoxyalkanes.
In vitro double oxidation of n-heptane with direct cofactor regeneration
Mueller, Christina A.,Akkapurathu, Beneeta,Winkler, Till,Staudt, Svenja,Hummel, Werner,Groeger, Harald,Schwaneberg, Ulrich
supporting information, p. 1787 - 1798 (2013/07/19)
A novel concept for the direct oxidation of cycloalkanes to the corresponding cyclic ketones in a one-pot synthesis in water with molecular oxygen as sole oxidizing agent was reported recently. Based on this concept we have developed a new strategy for the double oxidation of n-heptane to enable a biocatalytic resolution for the direct synthesis of heptanone and (R)-heptanols in a one-pot reaction. The bicatalytic cascade employs an NADH driven P450 BM3 monooxygenase variant (WTNADH, 19A12NADH or CM1 NADH) and an (S)-enantioselective alcohol dehydrogenase (RE-ADH). In the initial step n-heptane is hydroxylated under consumption of NADH to produce (R/S)-heptanol. In the second oxidation step the (S)-heptanol enantiomers are transformed to the corresponding ketones, reducing and thereby regenerating the cofactor. Characterization of initial hydroxylation step revealed high turnover frequencies (TOF) of up to 600 min-1, as well as high coupling efficiencies using NADH as cofactor (up to 44%). In the cascade reaction a nearly 2-fold improved product formation was achieved, compared to the single hydroxylation reaction. The total product concentration reached 1.1 mM, corresponding to a total turnover number (TTN) of 2500. Implementation of an additional cofactor regeneration system (D-glucose/glucose dehydrogenase) enabled a further enhancement in product formation with a total product concentration of 1.8 mM and a TTN of 3500. Copyright
