Enzyme Cascade Reactions for the Biosynthesis of Long Chain Aliphatic Amines from Renewable Fatty Acids
Enzyme Cascade Reactions for the Biosynthesis of Long Chain Aliphatic Amines from Renewable Fatty Acids
复制标题
DOI：
10.1002/adsc.201801501
复制
发表时间：
2019-03-15
影响因子：
5.4
通讯作者：
Park, Jin-Byung
中科院分区：
文献类型：
--
作者：
Lee, Da-Som;Song, Ji-Won;Park, Jin-Byung
研究了由可再生脂肪酸合成长链脂肪胺如（Z）-12-氨基十八碳-9-烯酸、10-或12-氨基十八烷酸和10-氨基-12-羟基十八烷酸的酶级联反应。以蓖麻油酸（Z）-12-羟基十八碳-9-烯酸）为原料，经（Z）-12-酮十八碳-9-烯酸转化为（Z）-12-氨基十八碳-9-烯酸，转化率为71%。10-以油酸（Z）-十八碳-9-烯酸为原料，经10-羟基十八烷酸和10-酮基十八烷酸，通过体内三步生物催化反应制备氨基十八烷酸，不仅涉及SADH和ATA变体，而且还有来自嗜麦芽寡养单胞菌的脂肪酸双键水合酶（OhyA）。10-氨基十八烷酸以4.4U/g干细胞，通过同时表达SADH和ATA变体以及OhyA的重组大肠杆菌转化率为87%。此外，大体积脂肪胺也可以由分离的酶产生（即，例如，SADH、ATA变体和来自短乳杆菌（Lactobacillus brevis）的烟酰胺腺嘌呤二核苷酸（NADH）氧化酶）与甲基苄胺或苄胺作为氨基供体。因此，这项研究有助于生物合成的长链脂肪胺具有两个大的取代基旁边的胺功能。
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.