Journal
CHEMCATCHEM
Volume 7, Issue 19, Pages 3121-3124Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.201500589
Keywords
alcohol oxidase; amination; biocatalysis; cascade; transaminase
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Funding
- Austrian Science Fund (FWF) within the DK Molecular Enzymology [W9]
- Erwin-Schrodinger fellowship [J3466]
- Austrian BMWFW
- BMVIT
- SFG
- Standortagentur Tirol
- Government of Lower Austria
- ZIT through the Austrian FFG-COMET-Funding Program
- Austrian Science Fund (FWF) [J3466] Funding Source: Austrian Science Fund (FWF)
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Amination of non-activated aliphatic fatty alcohols to the corresponding primary amines was achieved through a five-enzyme cascade reaction by coupling a long-chain alcohol oxidase from Aspergillus fumigatus (LCAO_Af) with a -transaminase from Chromobacterium violaceum (omega-TA_Cv). The alcohol was oxidized at the expense of molecular oxygen to yield the corresponding aldehyde, which was subsequently aminated by the PLP-dependent omega-TA to yield the final primary amine product. The overall cascade was optimized with respect to pH, O-2 pressure, substrate concentration, decomposition of H2O2 (derived from alcohol oxidation), NADH regeneration, and biocatalyst ratio. The substrate scope of this concept was investigated under optimized conditions by using terminally functionalized C-4-C-11 fatty primary alcohols bearing halogen, alkyne, amino, hydroxy, thiol, and nitrile groups.
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