693-57-2Relevant academic research and scientific papers
The screening, characterization, and use of ω-laurolactam hydrolase: A new enzymatic synthesis of 12-aminolauric acid
Asano, Yasuhisa,Fukuta, Yasuhisa,Yoshida, Yoichi,Komeda, Hidenobu
, p. 2141 - 2150 (2008)
Several ω-laurolactam degrading microorganisms were isolated from soil samples. These strains were capable of growing in a medium containing ω-laurolactam as sole source of carbon and nitrogen. Among them, five strains (T7, T31, U124, U224, and U238) were identified as Cupriavidus sp. T7, Acidovorax sp. T31, Cupriavidus sp. U124, Rhodococcus sp. U224, and Sphingomonas sp. U238, respectively. The ω-laurolactam hydrolyzing enzyme from Rhodococcus sp. U224 was purified to homogeneity, and its enzymatic properties were characterized. The enzyme acts on ω-octalactam and ω-laurolactam, but other lactam compounds, amides and amino acid amides, cannot be substrates. The enzyme gene was cloned, and the deduced amino acid sequence showed high homology with 6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12) from Arthrobacter sp. KI72 and Pseudomonas sp. NK87. Enzymatic synthesis of 12-aminolauric acid was performed using partially purified ω-laurolactam hydrolase from Rhodococcus sp. U224.
Multi-enzymatic cascade reactions with Escherichia coli-based modules for synthesizing various bioplastic monomers from fatty acid methyl esters?
Jung, Hyunsang,Kim, Byung-Gee,Kim, Ye Chan,Park, Beom Gi,Patil, Mahesh D.,Sarak, Sharad,Yoo, Hee-Wang,Yun, Hyungdon
supporting information, p. 2222 - 2231 (2022/04/03)
Multi-enzymatic cascade reaction systems were designed to generate biopolymer monomers using Escherichia coli-based cell modules, capable of carrying out one-pot reactions. Three cell-based modules, including a ω-hydroxylation module (Cell-Hm) to convert fatty acid methyl esters (FAMEs) to ω-hydroxy fatty acids (ω-HFAs), an amination module (Cell-Am) to convert terminal alcohol groups of the substrate to amine groups, and a reduction module (Cell-Rm) to convert the carboxyl groups of fatty acids to alcohol groups, were constructed. The product-oriented assembly of these cell modules involving multi-enzymatic cascade reactions generated ω-ADAs (up to 46 mM), α,ω-diols (up to 29 mM), ω-amino alcohols (up to 29 mM) and α,ω-diamines (up to 21 mM) from 100 mM corresponding FAME substrates with varying carbon chain length (C8, C10, and C12). Finally 12-ADA and 1,12-diol were purified with isolated yields of 66.5% and 52.5%, respectively. The multi-enzymatic cascade reactions reported herein present an elegant ‘greener’ alternative for the biosynthesis of various biopolymer monomers from renewable saturated fatty acids.
Amino acid preparation method comprising a step of hydroformylation of an unsaturated fatty nitrile
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Page/Page column 17, (2018/11/30)
A process for synthesizing an ω-amino acid compound of formula [in-line-formulae]HOOC—(CH2)r+2—CH2NH2,[/in-line-formulae] wherein 4≤r≤13 from a monounsaturated fatty nitrile compound of formula [in-line-formulae]CH2═CH—(CH2)r—CN[/in-line-formulae] the process comprising: 1) a step of hydroformylation of the mono unsaturated fatty nitrile compound by reacting said nitrile with carbon monoxide and di hydrogen 5e-a5 to obtain a nitrile aldehyde compound of formula HOC—(CH2)r+2-CN, then 2) a step of oxidation, in the presence of dioxygen, of the nitrile aldehyde compound to obtain a corresponding nitrile acid compound of formula HOOC—(CH2)r+2-CN, and 3) a step of reduction of the nitrile acid compound to give an w-amino acid of formula [in-line-formulae]HOOC—(CH2)r+2—CH2NH2.[/in-line-formulae]
Parallel anti-sense two-step cascade for alcohol amination leading to ω-amino fatty acids and α,ω-diamines
Sung, Sihyong,Jeon, Hyunwoo,Sarak, Sharad,Ahsan, Md Murshidul,Patil, Mahesh D.,Kroutil, Wolfgang,Kim, Byung-Gee,Yun, Hyungdon
supporting information, p. 4591 - 4595 (2018/10/23)
Running two two-step cascades in parallel anti-sense to transform an alcohol to an amine allowed the conversion of ω-hydroxy fatty acids (ω-HFAs) and α,ω-diols to the corresponding ω-amino fatty acids (ω-AmFAs) and α,ω-diamines, respectively. The network required only two enzymes namely an aldehyde reductase (AHR) and a transaminase (TA). Benzylamine served on the one hand as amine donor and on the other hand after deamination to benzaldehyde also as oxidant. All ω-HFAs tested were efficiently transformed to their corresponding ω-AmFAs using purified enzymes as well as a whole-cell system, separately expressing both the enzymes, with conversions ranging from 80-95%. Additionally, a single-cell co-expressing all enzymes successfully produced the ω-AmFAs as well as the α,ω-diamines with >90% yield. This system was extended by employing a lactonase, enabling the transformation of ?-caprolactone to its corresponding ω-AmFA with >80% conversion.
Method for preparing 12-aminododecanoic acid
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Paragraph 0015; 0016, (2018/04/01)
The invention relates to a method for preparing 12-aminododecanoic acid and belongs to the technical field of synthesis of long carbon chain nylon monomers. The method comprises the following steps: carrying out a substitution reaction on 10-undecenoic acid and hydrogen bromide to produce 11-bromo-undecanoic acid; carrying out a hydrocyanation reaction with a cyanide reagent K[Fe(CN)6].3H2O to produce 11-cyan-undecanoic acid; and carrying out a reduction reaction, thereby obtaining the final product 12-aminododecanoic acid. The method disclosed by the invention has the advantages of being short in synthetic route, low in cost, flexible in operation, high in reaction yield, capable of obtaining the high-purity product and the like, and is very suitable for small-dose large-scale production of pharmaceutical companies or labs.
NOVEL PROCESS FOR MAKING OMEGA-AMINOALKYLENIC ALKYL ESTER
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Paragraph 0191; 0192; 0193; 0194, (2016/08/17)
A method for making a compound of formula (V): is provided. The method comprises converting a compound of formula (III): to the compound of formula (V), wherein A is a C6-C10 alkene group having at least one carbon-carbon double bond, B is a C6-C10 alkyl chain; and R1 is an alkyl group, and R3 is an oxygenated functional group.
Microbial synthesis of medium-chain α,ω-dicarboxylic acids and ω-aminocarboxylic acids from renewable long-chain fatty acids
Song, Ji-Won,Lee, Jung-Hoo,Bornscheuer, Uwe T.,Park, Jin-Byung
, p. 1782 - 1788 (2014/06/09)
Biotransformation of long-chain fatty acids into medium-chain α,ω-dicarboxylic acids or ω-aminocarboxylic acids could be achieved with biocatalysts. This study presents the production of α,ω-dicarboxylic acids (e.g., C9, C11, C 12, C13) and ω-aminocarboxylic acids (e.g., C 11, C12, C13) directly from fatty acids (e.g., oleic acid, ricinoleic acid, lesquerolic acid) using recombinant Escherichia coli-based biocatalysts. ω-Hydroxycarboxylic acids, which were produced from oxidative cleavage of fatty acids via enzymatic reactions involving a fatty acid double bond hydratase, an alcohol dehydrogenase, a Baeyer-Villiger monooxygenase and an esterase, were then oxidized to α,ω- dicarboxylic acids by alcohol dehydrogenase (ADH, AlkJ) from Pseudomonas putida GPo1 or converted into ω-aminocarboxylic acids by a serial combination of ADH from P. putida GPo1 and an ω-transaminase of Silicibacter pomeroyi. The double bonds present in the fatty acids such as ricinoleic acid and lesquerolic acid were reduced by E. coli-native enzymes during the biotransformations. This study demonstrates that the industrially relevant building blocks (C9 to C13 saturated α,ω- dicarboxylic acids and ω-aminocarboxylic acids) can be produced from renewable fatty acids using biocatalysis.
Direct terminal alkylamino-functionalization via multistep biocatalysis in one recombinant whole-cell catalyst
Schrewe, Manfred,Ladkau, Nadine,Buehler, Bruno,Schmid, Andreas
supporting information, p. 1693 - 1697 (2013/07/19)
Direct and regiospecific amino-functionalization of non-activated carbon could be achieved using one recombinant microbial catalyst. The presented proof of concept shows that heterologous pathway engineering allowed the construction of a whole-cell biocatalyst catalyzing the terminal amino-functionalization of fatty acid methyl esters (e.g., dodecanoic acid methyl ester) and alkanes (e.g., octane). By coupling oxygenase and transaminase catalysis in vivo, both substrates are converted with absolute regiospecificity to the terminal amine via two sequential oxidation reactions followed by an amination step. Such demanding chemical three-step reactions achieved with a single catalyst demonstrate the tremendous potential of whole-cell biocatalysts for the production of industrially relevant building blocks. Copyright
Enzyme-catalyzed laurolactam synthesis via intramolecular amide bond formation in aqueous solution
Ladkau, Nadine,Hermann, Inna,Buehler, Bruno,Schmid, Andreas
experimental part, p. 2501 - 2510 (2011/11/07)
Lactam formation from ω-aminocarboxylic acids is thermodynamically unfavored in aqueous solution and therefore hard to achieve. In the present work ω-laurolactam hydrolases from Acidovorax sp. T31 and Cupriavidus sp. U124 were investigated regarding their potential to catalyze lactam formation. Both enzymes are known to hydrolyze laurolactam to 12-aminododecanoic acid. The ω-laurolactam hydrolase genes were expressed in Escherichia coli BL21 (DE3) and the catalytic activity of the respective proteins was investigated. As expected from thermodynamics, only laurolactam hydrolysis but not 12-aminododecanoic acid cyclization was observed in whole-cell biotransformations and cell extract assays. The utilization of 12-aminododecanoic acid methyl ester, as an activated form of 12-aminododecanoic acid, resulted in intramolecular amide bond formation with the product laurolactam. Maximum laurolactam formation rates of 13.5 and 14.3 U g CDW-1 and molar yields of 11.5% and 13.0% were achieved in biotransformations at pH 10 with recombinant E. coli harboring the ω-laurolactam hydrolase from Cupriavidus sp. U124 and Acidovorax sp. T31, respectively. Furthermore, it was shown that under the harsh reaction conditions applied, the utilization of whole-cell biocatalysts enables 17.2-fold higher laurolactam formation activity in comparison to free enzymes in solution. This study shows that hydrolase-catalyzed laurolactam synthesis can be achieved in aqueous solution by selection of an appropriate substrate and reaction pH. Copyright
High yield synthesis of 12-aminolauric acid by "enzymatic transcrystallization" of ω-laurolactam using ω-laurolactam hydrolase from acidovorax sp. T31
Fukuta, Yasuhisa,Komeda, Hidenobu,Yoshida, Yoichi,Asano, Yasuhisa
experimental part, p. 980 - 986 (2010/02/28)
The genes encoding ω-laurolactam hydrolases from Cupriavidus sp. T7, Acidovorax sp. T31, Cupriavidus sp. U124, and Sphingomonas sp. U238 were cloned and sequenced. Nucleotide and amino acid sequence analysis of the four genes indicated that the primary structures of these ω-laurolactam hydrolases are significantly similar to the 6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12). These genes were expressed in Escherichia coli, and the ω-laurolactam hydrolysing activity of the recombinant enzymes was compared with that of 6-aminohexanoate-cyclic-dimer hydrolase from Arthrobacter sp. KI72. The enzyme from Acidovorax sp. T31 was most successfully expressed in E. coli. Cell-free extract of the recombinant strain was used for the synthesis of 12-aminolauric acid from ω-laurolactam by "enzymatic transcrystallization," because crystalline ω-laurolactam added into the enzyme solution was converted to crystalline 12-aminolauric acid (97:3% yield). Under the optimum conditions, 208 g/l of 12-aminolauric acid was produced in 17 h. The resulting pure product was identical to authentic 12-aminolauric acid.
