Enhancement of (S)-2,3-dichloro-1-propanol production by recombinant whole-cell biocatalyst in n-heptane–aqueous biphasic system

Zou, Shu-Ping; Zheng, Yu‐Guo; Du, Er-Hong; Hu, Zhong-Ce

doi:10.1016/j.jbiotec.2014.08.014

Cited by 23 publications

(13 citation statements)

References 39 publications

(46 reference statements)

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“…When the substrate concentration was increased to 80 mM, as shown in Table , the ECH concentration reached a maximum level of 73.4 mM at 70 min, with a ECH yield of 91.7% and a volumetric productivity of 5.82 g/L/h in RPBR with ISPR. However, the maximal level of ECH concentration only reached 52.3 mM at 60 min, with the ECH yield of 65.4% in RPBR without ISPR, as a result of the inhibitor of ECH accumulation in the medium . These results indicated that the application of resin‐based ISPR techniques to the biotransformation of 1,3‐DCP in RPBR improve product concentration greatly and facilitate the further downstream processing of the product.…”

Section: Resultsmentioning

confidence: 95%

Covalent immobilization of halohydrin dehalogenase for efficient synthesis of epichlorohydrin in an integrated bioreactor

Zou

Zheng

2018

Biotechnology Progress

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Halohydrin dehalogenase (HHDH)-mediated dehalogenation of 1,3-dichloro-2-propanol (1,3-DCP) is a key step in the chemoenzymatic synthesis of epichlorohydrin (ECH) from glycerol. In this study, a covalent immobilization strategy was employed to enhance the stability of Agrobacterium tumefaciens HHDH using epoxy resin ES-103B as a carrier. Under optimal conditions, the activity recovery of ES-103B-immobilized HHDH (HHDH@ES-103B) was 62.4% and the specific activity was 1604 U/g. The HHDH@ES-103B exhibited excellent thermostability, with a half-life of 68.6 days at 40°C, which is 8.0-times higher than that of the free HHDH. A semicontinuous biotransformation of 1,3-DCP to ECH was performed using HHDH@ES-103B as biocatalyst in a recirculating packed bed reactor (RPBR), resulting in an ECH yield of 94.2%, with an average productivity of 5.2 g/L/h. The RPBR system exhibited a high operational stability and even after 50 cycles of reaction, it retained > 90% of the initial conversion. Furthermore, an integrated bioprocess based on in situ product recovery (ISPR) was developed in RPBR to overcome product inhibition. The integrated bioreactor equipped with an external macroporous adsorption resin HZD-9 column led to another 1.6-fold increase in ECH productivity to 8.46 g/L/h. This improved stability and reusability of HHDH@ES-103B demonstrated its potential for the biotransformation of 1,3-DCP to ECH. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:784-792, 2018.

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Section: Resultsmentioning

confidence: 95%

Covalent immobilization of halohydrin dehalogenase for efficient synthesis of epichlorohydrin in an integrated bioreactor

Zou

Zheng

2018

Biotechnology Progress

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“…b, the v o / v b value was optimized to be 2 : 8, at which the c value of rac ‐ m ‐NSO and the yield of ( R )‐ m ‐NPED reached the maximum values of 95·5 and 87·0%, respectively, at 25°C for 12 h. Nevertheless, when the v o / v b value was elevated to 6:4, the c and yield dramatically decreased to 46·7 and 41·0%, respectively. Reportedly, the elevation of v o / v b value would slow down the diffusion rate of the unreacted substrate from organic phase into aqueous phase, thereby reducing its inhibition on biocatalyst, but on the other hand definitely raise frequency of the interaction of organic solvent with biocatalyst, making the molecular and interfacial toxicities severe (He et al ; Zou et al ).…”

Section: Resultsmentioning

confidence: 99%

Enantioconvergent hydrolysis of m ‐nitrostyrene oxide at an elevated concentration by Phaseolus vulgaris epoxide hydrolase in the organic/aqueous two‐phase system

Wen

Zhao

Liu

et al. 2020

Lett Appl Microbiol

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Significance and Impact of the Study: Epoxide hydrolases play a crucial role in producing enantiopure epoxides and/or vicinal diols. However, numerous biocatalytic reactions of organic compounds, such as epoxides, in aqueous phase suffered various restrictions. Herein, the enantioconvergent hydrolysis of rac-m-NSO in two reaction systems was investigated using the whole cells of Escherichia coli/pCold-pve-h2. As a result, the concentration of rac-m-NSO and the space-time yield of (R)-m-NPED in organic/aqueous two-phase system were significantly increased, when compared with those in aqueous phase. To our knowledge, this is the first report about the production of (R)-m-NPED from rac-m-NSO at an elevated concentration by PvEH2 in the two-phase system. Abstract(R)-m-Nitrophenyl-1,2-ethanediol (m-NPED) is a versatile and highly valueadded chiral building block for the synthesis of some bioactive compounds, such as (R)-Nifenalol. To efficiently produce (R)-m-NPED through the enantioconvergent hydrolysis of racemic (rac-) m-nitrostyrene oxide (m-NSO) using the whole resting cells of Escherichia coli/pCold-pveh2 intracellularly expressing PvEH2, an epoxide hydrolase from Phaseolus vulgaris, two reaction systems were investigated. In the Na 2 HPO 4 ÀNaH 2 PO 4 buffer (50 mmol l À1 , pH 7Á0) system, merely 15 mmol l À1 rac-m-NSO was successfully subjected to enantioconvergent hydrolysis, producing (R)-m-NPED with 86Á0% enantiomeric excess (ee p ) and 177Á6 mg l À1 h À1 space-time yield (STY). The experimental result indicated that there is inhibitory effect of rac-m-NSO at high concentration on PvEH2. To efficiently increase the concentration of racm-NSO and the STY of (R)-m-NPED, petroleum ether was first selected to construct an organic/aqueous two-phase system. Then, both the volume ratio (v o /v b ) of petroleum ether to phosphate buffer and the weight ratio (w c /w s ) of E. coli/pCold-pveh2 dry cells to rac-m-NSO were optimized as 2 : 8 and 5 : 1, respectively. In the optimized petroleum ether/phosphate buffer two-phase system, the enantioconvergent hydrolysis of rac-m-NSO at 40 mmol l À1 (6Á6 mg ml À1 ) was carried out at 25°C for 12 h using 33Á0 mg ml À1 vacuum freeze-dried cells of E. coli/pCold-pveh2, producing (R)-m-NPED with 87Á4% ee p , 82Á3% yield and 502Á4 mg l À1 h À1 STY.

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“…In this degradation pathway, the reaction intermediate (S)-2,3-DCP was accumulated in the system due to the low activity of HheC on (S)-2,3-DCP, and a prolonged reaction time was needed to completely degrade it. However, (S)-2,3-DCP is an important chiral compound which has many applications in pharmaceuticals and fine chemical processing [8,9]. Alternatively, van Leeuwen and co-workers tried to degrade TCP to a highly enantioenriched (R)-or (S)-2,3-DCP by using enantio-complementary haloalkane dehalogenase variants obtained by directed evolution [10].…”

Section: Introductionmentioning

confidence: 99%

“…Halohydrin dehalogenase (HheC) has been used for the kinetic resolution of optically pure haloalcohols [8,11,12]. By modifying and optimizing the biodegradation pathway used by Dvorak and co-workers [2], it is possible to produce pure (S)-2,3-DCP through this system.…”

Section: Introductionmentioning

confidence: 99%

Biodegradation of 1,2,3-Trichloropropane to Valuable (S)-2,3-DCP Using a One-Pot Reaction System

et al. 2019

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1,2,3-trichloropropane (TCP) being one of the important environmental pollutants, has drawn significant concern due to its highly toxic and carcinogenic effects. In this study, we built a one-pot reaction system in which immobilized haloalkane dehalogenase (DhaA31) and halohydrin dehalognase (HheC) were used to catalyze the recalcitrant TCP to produce 2,3-dichloro-1-propanol (2,3-DCP) by removing epichlorohydrin (ECH). Since HheC displays a high R enantiopreference toward 2,3-DCP, the production of enantiopure (S)-2,3-DCP was expected. However, the enantioselective resolution of (R,S)-2,3-DCP by HheC was greatly inhibited by the circular reaction occurring between the product ECH and 1,3-dichloro-2-propanol (1.3-DCP). To resolve this problem, HZD-9 resin-based in situ product removal was implemented. Under the optimized conditions, TCP was completely consumed, resulting in optically pure (S)-2,3-DCP with enantiomer excess (e.e) > 99% and 40% yield (out of the 44% theoretical maximum). The scale-up resin-integrated reaction system was successfully carried out in 0.5 L batch reactor. Moreover, the system could be reused for 6 rounds with 64% of original activity retained, showing that it could be applied in the treatment of large volumes of liquid waste and producing enantiopure (S)-2,3-DCP.

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Enhancement of (S)-2,3-dichloro-1-propanol production by recombinant whole-cell biocatalyst in n-heptane–aqueous biphasic system

Cited by 23 publications

References 39 publications

Covalent immobilization of halohydrin dehalogenase for efficient synthesis of epichlorohydrin in an integrated bioreactor

Covalent immobilization of halohydrin dehalogenase for efficient synthesis of epichlorohydrin in an integrated bioreactor

Enantioconvergent hydrolysis of m ‐nitrostyrene oxide at an elevated concentration by Phaseolus vulgaris epoxide hydrolase in the organic/aqueous two‐phase system

Biodegradation of 1,2,3-Trichloropropane to Valuable (S)-2,3-DCP Using a One-Pot Reaction System

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