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Enzyme Cascade Reactions for the Biosynthesis of Long Chain Aliphatic Amines from Renewable Fatty Acids

Title
Enzyme Cascade Reactions for the Biosynthesis of Long Chain Aliphatic Amines from Renewable Fatty Acids
Authors
Lee, Da-SomSong, Ji-WonVoss, MoritzSchuiten, EvaAkula, Ravi KumarKwon, Yong-UkBornscheuer, UwePark, Jin-Byung
Ewha Authors
박진병권용억송지원
SCOPUS Author ID
박진병scopus; 권용억scopus
Issue Date
2019
Journal Title
ADVANCED SYNTHESIS & CATALYSIS
ISSN
1615-4150JCR Link

1615-4169JCR Link
Citation
ADVANCED SYNTHESIS & CATALYSIS vol. 361, no. 6, pp. 1359 - 1367
Keywords
enzyme cascade reactionslong chain aliphatic aminesamine transaminasewhole cell biotransformationEscherichia coli
Publisher
WILEY-V C H VERLAG GMBH
Indexed
SCIE; SCOPUS WOS
Document Type
Article
Abstract
Enzyme cascade reactions for the synthesis of long chain aliphatic amines such as (Z)-12-aminooctadec-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 methylbenzyl-amine 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.
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DOI
10.1002/adsc.201801501
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엘텍공과대학 > 식품공학전공 > Journal papers
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