Chiral amines represent a pervasive structural motif found in various natural products, pharmaceuticals, agrochemicals and fine chemicals. Their preparation in single-enantiomer form continues to attract significant research attention and although many advances have been made in the area of synthetic organic chemistry to increase the scope of the routes to these moieties, there remains an ever-growing need of general strategies for the assembly of structurally-diverse amines which also conform to the efficiency and environmental requirements of modern manufacturing processes. This report investigates biocatalytic routes as a means for constructing chiral amine scaffolds, which offer a more environmentally benign approach when compared with traditional chemocatalysed processes. Probing the catalysts available in the biocatalytic toolbox of enzymes, several routes were examined in more detail. Imine reductases (IREDs) represent a recent addition to the toolbox, enzymes which by definition are able to reduce pre-formed imines to their corresponding amines with high selectivity. This report analyses the (R)-imine reductase [(R)-IRED] from Streptomyces sp. GF3587, one of the first imine reductases identified for its biocatalytic potential, in greater depth. The enzyme was found to catalyse the reduction of a broad range of cyclic imines while displaying high levels of activity and selectivity, thereby offering a direct route of access to chiral secondary and tertiary amines. Substrate kinetic parameters were established for the enzyme in order to understand its substrate preferences and the enzymeâs catalytic mechanism was probed through the generation of mutant (R)-IREDs. Owing to their operation under physiological conditions as well as the orthogonal nature of their reactions, it is possible to combine multiple enzyme reactions to enable cascades. This report examines a multi-enzyme reaction combining Ï-transaminases (ATAs) with imine reductases, for the synthesis of chiral disubstituted piperidines from simple diketone substrates. The cascade was then taken a step further by the inclusion of the carboxylic acid reductase (CAR) enzyme, for the synthesis of the nitrogen-containing heterocycles morpholine and thiomorpholine from ketoacid compounds. Finally, the well-established deracemisation technique, employing a selective amine oxidase (AO) with either a non-selective chemical reducing agent or a biocatalytic reductant (IRED), was explored in more detail by encompassing new substrate motifs. As biocatalysis becomes more readily accepted as a general technique in the synthetic chemistâs repertoire, the concept of carrying out enzymatic reactions in constant flow was explored as a means for applying this methodology with increased production and decreased processing rates.