Biosynthesis of Nylon 12 Monomer, ω-Aminododecanoic Acid Using Artificial Self-Sufficient P450, AlkJ and ω-TA

Ahsan, Md. Murshidul; Patil, Mahesh D.; Jeon, Hyeongtag; Sung, Sihyong; Chung, Taeowan; Yun, Hyungdon

doi:10.3390/catal8090400

Cited by 21 publications

(10 citation statements)

References 29 publications

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“…Thus, whole cells expressing the enzyme of interest for the biosynthetic applications are advantageous [47]. Besides the cost effective and simpler handling of whole-cell biotransformations, an added advantage includes the utility of the enzyme production machinery of the fully functional living organism [48,49]. Also, the implementation of biocatalytic syntheses using whole-cell biotransformations is advantageous regarding the regeneration of the redox cofactors [50].…”

Section: Kinetic Resolution Of Racemic Amines Using E Coli Whole Celmentioning

confidence: 99%

Kinetic Resolution of Racemic Amines to Enantiopure (S)-amines by a Biocatalytic Cascade Employing Amine Dehydrogenase and Alanine Dehydrogenase

et al. 2019

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Amine dehydrogenases (AmDHs) efficiently catalyze the NAD(P)H-dependent asymmetric reductive amination of prochiral carbonyl substrates with high enantioselectivity. AmDH-catalyzed oxidative deamination can also be used for the kinetic resolution of racemic amines to obtain enantiopure amines. In the present study, kinetic resolution was carried out using a coupled-enzyme cascade consisting of AmDH and alanine dehydrogenase (AlaDH). AlaDH efficiently catalyzed the conversion of pyruvate to alanine, thus recycling the nicotinamide cofactors and driving the reaction forward. The ee values obtained for the kinetic resolution of 25 and 50 mM rac-α-methylbenzylamine using the purified enzymatic systems were only 54 and 43%, respectively. The use of whole-cells apparently reduced the substrate/product inhibition, and the use of only 30 and 40 mgDCW/mL of whole-cells co-expressing AmDH and AlaDH efficiently resolved 100 mM of rac-2-aminoheptane and rac-α-methylbenzylamine into the corresponding enantiopure (S)-amines. Furthermore, the applicability of the reaction protocol demonstrated herein was also successfully tested for the efficient kinetic resolution of wide range of racemic amines.

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Section: Kinetic Resolution Of Racemic Amines Using E Coli Whole Celmentioning

confidence: 99%

Kinetic Resolution of Racemic Amines to Enantiopure (S)-amines by a Biocatalytic Cascade Employing Amine Dehydrogenase and Alanine Dehydrogenase

et al. 2019

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“…CARs are frequently introduced into cascade reactions in vivo . In many cases, endogenous enzymes such as aldehyde reductases, decarbonylases and alcohol dehydrogenases within the expression hosts are being utilized e. g. to reduce the aldehyde to the corresponding alcohol, and CARs may become the limiting step in such reaction sequences . To create more variety for cascade applications, a repertoire of characterized key enzymes is of most importance.…”

Section: Introductionmentioning

confidence: 99%

Characterization of Type IV Carboxylate Reductases (CARs) for Whole Cell‐Mediated Preparation of 3‐Hydroxytyrosol

et al. 2019

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Fragrance and flavor industries could not imagine business without aldehydes. Processes for their commercial production raise environmental and ecological concerns. The chemical reduction of organic acids to aldehydes is challenging. To fulfill the demand of a mild and selective reduction of carboxylic acids to aldehydes, carboxylic acid reductases (CARs) are gaining importance. We identified two new subtype IV fungal CARs from Dichomitus squalens CAR (DsCAR) and Trametes versicolor CAR (Tv2CAR) in addition to literature known Trametes versicolor CAR (TvCAR). Expression levels were improved by the co‐expression of GroEL‐GroES with either the trigger factor or the DnaJ‐DnaK‐GrpE system. Investigation of the substrate scope of the three enzymes revealed overlapping substrate‐specificities. Tv2CAR and DsCAR showed a preferred pH range of 7.0 to 8.0 in bicine buffer. TvCAR showed highest activity at pH 6.5 to 7.5 in MES buffer and slightly reduced activity at pH 6.0 or 8.0. TvCAR appeared to tolerate a wider pH range without significant loss of activity. Type IV fungal CARs optimal temperature was in the range of 25–35 °C. TvCAR showed a melting temperature (Tm) of 55 °C indicating higher stability compared to type III and the other type IV fungal CARs (Tm 51–52 °C). Finally, TvCAR was used as the key enzyme for the bioreduction of 3,4‐dihydroxyphenylacetic acid to the antioxidant 3‐hydroxytyrosol (3‐HT) and gave 58 mM of 3‐HT after 24 h, which correlates to a productivity of 0.37 g L−1 h−1.

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“…For example, these include CYP52A13 and CYP52A17 (Craft et al, 2003; Eschenfeldt et al, 2003), CYP4 (Fer et al, 2008), CYP704B2 (Li et al, 2010), CYP102A1 (Xiao et al, 2018), CYP153 (Bordeaux et al, 2012), and the CYP153A M.aq. -CPR BM3 fusion protein (Scheps et al, 2013; Ahsan et al, 2018; Joo et al, 2019). Some of these enzymes can ω-oxidize terminal methyl groups and have been applied to ω-HFA production, but there is a limitation, in that most of these enzymes are specific for chain lengths of ≥12 (Picataggio et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of Medium-Chain ω-Hydroxy Fatty Acids by AlkBGT of Pseudomonas putida GPo1 With Native FadL in Engineered Escherichia coli

Bennett

San

et al. 2019

Front. Bioeng. Biotechnol.

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Hydroxy fatty acids (HFAs) are valuable compounds that are widely used in medical, cosmetic and food fields. Production of ω-HFAs via bioconversion by engineered Escherichia coli has received a lot of attention because this process is environmentally friendly. In this study, a whole-cell bio-catalysis strategy was established to synthesize medium-chain ω-HFAs based on the AlkBGT hydroxylation system from Pseudomonas putida GPo1. The effects of blocking the β-oxidation of fatty acids (FAs) and enhancing the transportation of FAs on ω-HFAs bio-production were also investigated. When fadE and fadD were deleted, the consumption of decanoic acid decreased, and the yield of ω-hydroxydecanoic acid was enhanced remarkably. Additionally, the co-expression of the FA transporter protein, FadL, played an important role in increasing the conversion rate of ω-hydroxydecanoic acid. As a result, the concentration and yield of ω-hydroxydecanoic acid in NH03(pBGT-fadL) increased to 309 mg/L and 0.86 mol/mol, respectively. This whole-cell bio-catalysis system was further applied to the biosynthesis of ω-hydroxyoctanoic acid and ω-hydroxydodecanoic acid using octanoic acid and dodecanoic acid as substrates, respectively. The concentrations of ω-hydroxyoctanoic acid and ω-hydroxydodecanoic acid reached 275.48 and 249.03 mg/L, with yields of 0.63 and 0.56 mol/mol, respectively. This study demonstrated that the overexpression of AlkBGT coupled with native FadL is an efficient strategy to synthesize medium-chain ω-HFAs from medium-chain FAs in fadE and fadD mutant E. coli strains.

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Biosynthesis of Nylon 12 Monomer, ω-Aminododecanoic Acid Using Artificial Self-Sufficient P450, AlkJ and ω-TA

Cited by 21 publications

References 29 publications

Kinetic Resolution of Racemic Amines to Enantiopure (S)-amines by a Biocatalytic Cascade Employing Amine Dehydrogenase and Alanine Dehydrogenase

Kinetic Resolution of Racemic Amines to Enantiopure (S)-amines by a Biocatalytic Cascade Employing Amine Dehydrogenase and Alanine Dehydrogenase

Characterization of Type IV Carboxylate Reductases (CARs) for Whole Cell‐Mediated Preparation of 3‐Hydroxytyrosol

Biosynthesis of Medium-Chain ω-Hydroxy Fatty Acids by AlkBGT of Pseudomonas putida GPo1 With Native FadL in Engineered Escherichia coli

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