PUB - Publikationen an der Universität Bielefeld

Chiral and enantiopure amines can be produced by enantioselective transaminases via kinetic resolution of amine racemates. This transamination reaction requires stoichiometric amounts of co-substrate. A dual-enzyme recycling system overcomes this limitation: L-amino acid oxidases (LAAO) recycle the accumulating co-product of ( S )-selective transaminases in the kinetic resolution of racemic amines to produce pure ( R )-amines. However, availability of suitable LAAOs is limited. Here we use the heterologously produced, highly active fungal hcLAAO4 with broad substrate spectrum. H 2 O 2 as by-product of hcLAAO4 is detoxified by a catalase. The final system allows using sub-stoichiometric amounts of 1mol% of the transaminase co-substrate as well as the initial application of L-amino acids instead of alpha-keto acids. With an optimized protocol, synthetic potential of this kinetic resolution cascade was proven at the preparative scale (>90mg) by the synthesis of highly enantiomerically pure ( R )-methylbenzylamine (>99%ee) at complete conversion (50%). © 2022 Wiley-VCH GmbH.