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With the aim to discover and create suitable biocatalysts for the synthesis of chiral amines in a faster and more efficient way, this thesis includes protein engineering studies (Article I), explores transaminase substrate specificities (Articles II and IV), and an ultrahigh-throughput growth system-based for the directed evolution of amine-forming enzymes (Article III).
The protein engineering studies described in Article I deal with the creation of a (R)-amine transaminase activity in the α-amino acid transaminase scaffold to expand our knowledge of the evolutionary relationship between amine transaminase and α-amino acid transaminase. Article II describes the broadening of the limited substrate scope of transaminases to enable the conversion of bulky substrates. In Article III, a growth selection system is described for an ultra-high throughput screening strategy to accelerate the identification of desired mutants, which can be widely applied to the directed evolution of amine-forming enzymes.