Enhanced catalytic efficiency of nitrilase from Acidovorax facilis 72W and application in bioconversion of 3-cyanopyridine to nicotinic acid

Li, He; Dong, Weiliang; Zhang, Yue; Liu, Kuan; Zhang, Wenming; Zhang, Min; Ma, Jiangfeng; Jiang, Min

doi:10.1016/j.molcatb.2017.03.010

Cited by 7 publications

(1 citation statement)

References 27 publications

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“…[ 32,33 ] Different technologies have been applied from resting cells harboring nitrilase to recombinant enzymes in various forms, purified, lysates or whole cells, in batches or immobilized forms. [ 34,35,36,37 ] Here, the reusability of immobilized nitrilase using various supports was investigated to select the most efficient immobilization method. At the same time, this study focused on the identification of a more robust enzyme that can remain stable for days.…”

Section: Introductionmentioning

confidence: 99%

Nitrilase immobilization and transposition from a micro‐scale batch to a continuous process increase the nicotinic acid productivity

Teepakorn

Zajkoska

Cwicklinski

et al. 2021

Biotechnology Journal

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In recent years, many biocatalytic processes have been developed for the production of chemicals and pharmaceuticals. In this context, enzyme immobilization methods have attracted attention for their advantages, such as continuous production and increased stability. Here, enzyme immobilization methods and a collection of nitrilases from biodiversity for the conversion of 3‐cyanopyridine to nicotinic acid were screened. Substrate conversion over 10 conversion cycles was monitored to optimize the process. The best immobilization conditions were found with cross‐linking using glutaraldehyde to modify the PMMA beads. This method showed good activity over 10 cycles in a batch reactor at 30 and 40°C. Finally, production with a new thermostable nitrilase was examined in a continuous packed bed reactor, showing very high stability of the biocatalytic process at a flow rate of 0.12 ml min–1 and a temperature of 50°C. The complete conversion of 3‐cyanopyridine was obtained over 30 days of operation. Future steps will concern reactor scale‐up to increase the production rate with reasonable pressure drops.

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Section: Introductionmentioning

confidence: 99%

Nitrilase immobilization and transposition from a micro‐scale batch to a continuous process increase the nicotinic acid productivity

Teepakorn

Zajkoska

Cwicklinski

et al. 2021

Biotechnology Journal

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A novel nitrilase from Ralstonia eutropha H16 and its application to nicotinic acid production

Fan

Chen

Sun

et al. 2017

Bioprocess Biosyst Eng

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A novel aliphatic nitrilase, REH16, was found in Ralstonia eutropha H16 and overexpressed in Escherichia coli BL21(DE3), and its enzymatic properties were studied. The temperature and pH optima were 37 °C and 6.6, respectively, and the best thermostability of the nitrilase was observed at 25 °C, which preserved 95% of activity after 120 h of incubation. REH16 has a broad hydrolytic activity toward aliphatic and heterocyclic nitriles and showed high tolerance of 3-cyanopyridine; this enzyme could hydrolyze as high as 100 mM 3-cyanopyridine completely. To improve the 3-cyanopyridine conversion efficiency in an aqueous reaction system, water-miscible organic solvents were tested, and ethanol (10% v/v) was chosen as the optimal co-solvent. Finally, under optimized conditions, using the fed-batch reaction mode, total of 1050 mM 3-cyanopyridine was hydrolyzed completely in 20.8 h with eight substrate feedings, yielding 129.2 g/L production of nicotinic acid and thus showing a potential for industrial application.

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Cloning, expression, and characterization of a novel nitrilase, PaCNit, from Pannonibacter carbonis Q4.6

Liu

Han

et al. 2019

Biotechnol Lett

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Enhanced catalytic efficiency of nitrilase from Acidovorax facilis 72W and application in bioconversion of 3-cyanopyridine to nicotinic acid

Cited by 7 publications

References 27 publications

Nitrilase immobilization and transposition from a micro‐scale batch to a continuous process increase the nicotinic acid productivity

Nitrilase immobilization and transposition from a micro‐scale batch to a continuous process increase the nicotinic acid productivity

A novel nitrilase from Ralstonia eutropha H16 and its application to nicotinic acid production

Cloning, expression, and characterization of a novel nitrilase, PaCNit, from Pannonibacter carbonis Q4.6

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