High Yield Synthesis of 12-Aminolauric Acid by “Enzymatic Transcrystallization” of ω-Laurolactam Using ω-Laurolactam Hydrolase from<i>Acidovorax</i>sp. T31

Fukuta, Yasuhisa; Komeda, Hidetsugu; Yoshida, Yoichi; Asano, Yasuhisa

doi:10.1271/bbb.80551

Cited by 12 publications

(7 citation statements)

References 18 publications

(27 reference statements)

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“…In our previous study, 10 putative ω‐TAs, including selected mll1207 ω‐TA from M. loti , were selected by family profile analysis, and functionally characterized where mll1207 ω‐TA showed good activity toward various amines including methylbenzylamine (MBA), and beta‐phenylalanine . In addition, the sequence alignment and phylogenetic analysis of mll1207 ω‐TA was carried out using reported ω‐TAs, which have been utilized for the synthesis of ω‐AmFA (Figure S8A and S8B, Supporting Information), and the active site of the enzyme was determined by homology modeling (Figure S9, Supporting Information).…”

Section: Resultsmentioning

confidence: 99%

“…To date, the microbial host system is considered the most appropriate means for biotechnological production of polymer building blocks for Nylons or polyesters . Furthermore, it has been reported that omega amino dodecanoic acid (ω‐AmDDA) or 12 amino dodecanoic acid methyl ester (ADAME) are convenient monomers for Nylon 12 biosynthesis . Recently, Schmid's group demonstrated ADAME production from dodecanoic acid methyl ester (DAME) through a hydroxylation–oxidation–amination cascade, where the AlkBGT system was used for ω‐hydroxylation–oxidation and an omega transaminase (ω‐TA) was used for reductive amination.…”

Section: Introductionmentioning

confidence: 99%

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Biosynthesis of the Nylon 12 Monomer, ω‐Aminododecanoic Acid with Novel CYP153A, AlkJ, and ω‐TA Enzymes

Ahsan

Jeon

Nadarajan

et al. 2018

Biotechnology Journal

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Bioplastics are derived from renewable biomass sources, such as vegetable oils, cellulose, and starches. An important and high-performance member of the bioplastic family is Nylon 12. The biosynthesis of ω-amino dodecanoic acid (ω-AmDDA), the monomer of Nylon 12 from vegetable oil derivatives is considered as an alternative to petroleum-based monomer synthesis. In this study, for the production of ω-AmDDA from dodecanoic acid (DDA), the cascade of novel P450 (CYP153A), alcohol dehydrogenase (AlkJ), and ω-transaminase (ω-TA) is developed. The regioselective ω-hydroxylation of 1 mM DDA with near complete conversion (>99%) is achieved using a whole-cell biocatalyst co-expressing CYP153A, ferredoxin reductase and ferredoxin. When the consecutive biotransformation of ω-hydroxy dodecanoic acid (ω-OHDDA) is carried out using a whole-cell biocatalyst co-expressing AlkJ and ω-TA, 1.8 mM ω-OHDDA is converted into ω-AmDDA with 87% conversion in 3 h. Finally, when a one-pot reaction is carried out with 2 mM DDA using both whole-cell systems, 0.6 mM ω-AmDDA is produced after a 5 h reaction. The results demonstrated the scope of the potential cascade reaction of novel CYP153A, AlkJ, and ω-TA for the production of industrially important bioplastic monomers, amino fatty acids, from FFAs.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Biosynthesis of the Nylon 12 Monomer, ω‐Aminododecanoic Acid with Novel CYP153A, AlkJ, and ω‐TA Enzymes

Ahsan

Jeon

Nadarajan

et al. 2018

Biotechnology Journal

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“…Success in such endeavours depends solely on the approach adopted for microorganism isolation. Such an investigation led to development of the first route for production of 12‐aminolauric acid from ω‐laurolactam by enzymatic trans ‐crystallization ( Asano et al ., 2008 ; Fukuta et al ., 2009 ) ( Fig. 4 ) and hydrolase activity was found in various microorganisms such as Cupriavidus sp.…”

Section: Screening For Enzyme Activitymentioning

confidence: 99%

Strategies for discovery and improvement of enzyme function: state of the art and opportunities

Kaul

Asano

2011

Microbial Biotechnology

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SummaryDevelopments in biocatalysis have been largely fuelled by consumer demands for new products, industrial attempts to improving existing process and minimizing waste, coupled with governmental measures to regulate consumer safety along with scientific advancements. One of the major hurdles to application of biocatalysis to chemical synthesis is unavailability of the desired enzyme to catalyse the reaction to allow for a viable process development. Even when the desired enzyme is available it often forces the process engineers to alter process parameters due to inadequacies of the enzyme, such as instability, inhibition, low yield or selectivity, etc. Developments in the field of enzyme or reaction engineering have allowed access to means to achieve the ends, such as directed evolution, de novo protein design, use of non‐conventional media, using new substrates for old enzymes, active‐site imprinting, altering temperature, etc. Utilization of enzyme discovery and improvement tools therefore provides a feasible means to overcome this problem. Judicious employment of these tools has resulted in significant advancements that have leveraged the research from laboratory to market thus impacting economic growth; however, there are further opportunities that have not yet been explored. The present review attempts to highlight some of these achievements and potential opportunities.

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“…T31 or Cupriavidus sp. U124, 12‐aminododecanoic acid formation rates of 2.77 and 1.24 U mg protein −1 were observed, respectively 15…”

Section: Introductionmentioning

confidence: 97%

“…U124, 12-aminododecanoic acid formation rates of 2.77 and 1.24 U mg protein À1 were observed, respectively. [15] In this study, these w-laurolactam hydrolases were investigated regarding their potential to catalyze intramolecular amide bond formation and thus to convert 12-aminododecanoic acid to laurolactam serving as the model reaction (Scheme 1).…”

Section: Introductionmentioning

confidence: 99%

Enzyme‐Catalyzed Laurolactam Synthesis via Intramolecular Amide Bond Formation in Aqueous Solution

et al. 2011

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Lactam formation from w-aminocarboxylic acids is thermodynamically unfavored in aqueous solution and therefore hard to achieve. In the present work w-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 w-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 À1 and molar yields of 11.5% and 13.0% were achieved in biotransformations at pH 10 with recombinant E. coli harboring the w-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 hydrolasecatalyzed laurolactam synthesis can be achieved in aqueous solution by selection of an appropriate substrate and reaction pH.

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High Yield Synthesis of 12-Aminolauric Acid by “Enzymatic Transcrystallization” of ω-Laurolactam Using ω-Laurolactam Hydrolase fromAcidovoraxsp. T31

Cited by 12 publications

References 18 publications

Biosynthesis of the Nylon 12 Monomer, ω‐Aminododecanoic Acid with Novel CYP153A, AlkJ, and ω‐TA Enzymes

Biosynthesis of the Nylon 12 Monomer, ω‐Aminododecanoic Acid with Novel CYP153A, AlkJ, and ω‐TA Enzymes

Strategies for discovery and improvement of enzyme function: state of the art and opportunities

Enzyme‐Catalyzed Laurolactam Synthesis via Intramolecular Amide Bond Formation in Aqueous Solution

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