Long-chain aliphatic amines such as (S,Z)-heptadec-9-en-7-amine and 9-aminoheptadecane were synthesized from ricinoleic acid and oleic acid, respectively,b ywhole-cell cascade reactions using the combination of an alcohol dehydrogenase (ADH) from Micrococcus luteus,a ne ngineered amine transaminase from Vibrio fluvialis (Vf-ATA), and ap hotoactivated decarboxylase from Chlorella variabilis NC64A (Cv-FAP) in aone-pot process.Inaddition, long chain aliphatic esters such as 10-(heptanoyloxy)dec-8-ene and octylnonanoate were prepared from ricinoleic acid and oleic acid, respectively,byusing the combination of the ADH, aBaeyer-Villiger monooxygenase variant from Pseudomonas putida KT2440, and the Cv-FAP.T he target compounds were produced at rates of up to 37 Ug À1 dry cells with conversions up to 90 %. Therefore,this study contributes to the preparation of industrially relevant long-chain aliphatic chiral amines and esters from renewable fatty acid resources.

Enzyme cascade reactions for the synthesis of long chain aliphatic amines such as (Z)-12aminooctadec-9-enoic acid, 10-or 12-aminooctadecanoic acid, and 10-amino-12-hydroxyoctadecanoic acid from renewable fatty acids were investigated. (Z)-12-aminooctadec-9-enoic acid was produced from ricinoleic acid ((Z)-12-hydroxyoctadec-9-enoic acid) via (Z)-12-ketooctadec-9-enoic acid with a conversion of 71% by a two-step in vivo biotransformation involving a long chain secondary alcohol dehydrogenase (SADH) from Micrococcus luteus and a variant of the amine transaminase (ATA) from Vibrio fluvialis. 10-Aminooctadecanoic acid was prepared from oleic acid ((Z)-octadec-9-enoic acid) via 10-hydroxyoctadecanoic acid and 10-ketooctadecanoic acid by an in vivo three-step biocatalysis reaction involving not only the SADH and ATA variants, but also a fatty acid double bond hydratase (OhyA) from Stenotrophomonas maltophilia. 10-Aminooctadecanoic acid was produced at a total rate of 4.4 U/g dry cells with a conversion of 87% by recombinant Escherichia coli expressing the SADH and ATA variants, and OhyA simultaneously. In addition, bulky aliphatic amines could also be produced by the isolated enzymes (i. e., the SADH, the ATA variants, and a nicotinamide adenine dinucleotide (NADH) oxidase from Lactobacillus brevis) with methylbenzylamine or benzylamine as amino donor. This study thus contributes to the biosynthesis of long chain aliphatic amines having two large substituents next to the amine functionality.