TY  - JOUR
U1  - Wissenschaftlicher Artikel
A1  - Coenen, Anna
A1  - Ferrer, Manuel
A1  - Jaeger, Karl-Erich
A1  - Schörken, Ulrich
T1  - Synthesis of 12-aminododecenoic Acid by Coupling Transaminase to Oxylipin Pathway Enzymes
JF  - Applied Microbiology and Biotechnology
N2  - Biobased polymers derived from plant oils are sustainable alternatives to petro based polymers. In recent years, multienzyme cascades have been developed for the synthesis of biobased ω-aminocarboxylic acids, which serve as building blocks for polyamides. In this work, we have developed a novel enzyme cascade for the synthesis of 12-aminododeceneoic acid, a precursor for nylon-12, starting from linoleic acid. Seven bacterial ω-transaminases (ω-TAs) were cloned, expressed in Escherichia coli and successfully purified by affinity chromatography. Activity towards the oxylipin pathway intermediates hexanal and 12-oxododecenoic acid in their 9(Z) and 10(E) isoforms was demonstrated for all seven transaminases in a coupled photometric enzyme assay. The highest specific activities were obtained with ω-TA from Aquitalea denitrificans (TRAD), with 0.62 U mg−1 for 12-oxo-9(Z)-dodecenoic acid, 0.52 U mg−1 for 12-oxo-10(E)-dodecenoic acid and 1.17 U mg−1 for hexanal. A one-pot enzyme cascade was established with TRAD and papaya hydroperoxide lyase (HPLCP-N), reaching conversions of 59% according to LC-ELSD quantification. Starting from linoleic acid, up to 12% conversion to 12-aminododecenoic acid was achieved with a 3-enzyme cascade comprising soybean lipoxygenase (LOX-1), HPLCP-N and TRAD. Higher product concentrations were achieved by the consecutive addition of enzymes compared to simultaneous addition at the beginning.
KW  - Polyamide
KW  - Transaminase
KW  - 12-aminododecenoic acid
KW  - Nylon-12
KW  - Enzyme cascade
KW  - Biological Sciences
Y1  - 2023
UN  - https://nbn-resolving.org/urn:nbn:de:hbz:832-epub4-27663
SN  - 0175-7598
SS  - 0175-7598
SN  - 1432-0614
SS  - 1432-0614
U6  - https://doi.org/10.1007/s00253-023-12422-6
DO  - https://doi.org/10.1007/s00253-023-12422-6
VL  - 107
IS  - 7
SP  - 2209
EP  - 2221
S1  - 13
PB  - Springer Berlin Heidelberg
ER  -