Nitrile bioconversion by Microbacterium imperiale CBS 498-74 resting cells in batch and ultrafiltration membrane bioreactors

Cantarella, Maria; Cantarella, Laura; Gallifuoco, Alberto; Spera, Agata

doi:10.1007/s10295-004-0200-3

Cited by 18 publications

(5 citation statements)

References 30 publications

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“…This is most probably because the substrate was more stable at lower temperature and released less cyanide to the reaction mixture. Similar results were found when industrial scale production of acrylamide by microbial NHase was carried out at 4-10°C in order to improve enzyme stability and catalyst productivity [6,19,21,26]. On the other hand, it was reported that -aminonitriles were more stable at lower pH circumstance [5,8], however, R. boritolerans CCTCC M 208108 NHase activity was quite low in weakly acidic environment (for example, pH 6.0) in diVerent buVers.…”

Section: Discussionsupporting

confidence: 77%

Enzymatic production of 2-amino-2,3-dimethylbutyramide by cyanide-resistant nitrile hydratase

Lin

Zheng

Wang

et al. 2012

Journal of Industrial Microbiology and Biotechnology

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A novel enzymatic route for the synthesis of 2-amino-2,3-dimethylbutyramide (ADBA), important intermediate of highly potent and broad-spectrum imidazolinone herbicides, from 2-amino-2,3-dimethylbutyronitrile (ADBN) was developed. Strain Rhodococcus boritolerans CCTCC M 208108 harboring nitrile hydratase (NHase) towards ADBN was screened through a sophisticated colorimetric screening method and was found to be resistant to cyanide (5 mM). Resting cells of R. boritolerans CCTCC M 208108 also proved to be tolerant against high product concentration (40 g l(-1)) and alkaline pH (pH 9.3). A preparative scale process for continuous production of ADBA in both aqueous and biphasic systems was developed and some key parameters of the biocatalytic process were optimized. Inhibition of NHase by cyanide dissociated from ADBN was successfully overcome by temperature control (at 10°C). The product concentration, yield and catalyst productivity were further improved to 50 g l(-1), 91% and 6.3 g product/g catalyst using a 30/70 (v/v) n-hexane/water biphasic system. Furthermore, cells of R. boritolerans CCTCC M 208108 could be reused for at lease twice by stopping the continuous reaction before cyanide concentration rose to 2 mM, with the catalyst productivity increasing to 12.3 g product/g catalyst. These results demonstrated that enzymatic synthesis of ADBA using whole cells of R. boritolerans CCTCC M 208108 showed potential for industrial application.

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Section: Discussionsupporting

confidence: 77%

Enzymatic production of 2-amino-2,3-dimethylbutyramide by cyanide-resistant nitrile hydratase

Lin

Zheng

Wang

et al. 2012

Journal of Industrial Microbiology and Biotechnology

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“…Numerous microorganisms, especially bacteria, have been reported to degrade both aliphatic and aromatic nitriles in the literature, and a few of these are Arthrobacter sp. I-9 (Yamada et al 1980), Bacillus pallidus (Cramp et al 1997), Mucolate Actinomycetes (Brandao and Bull 2003), Microbacterium Imperiale CBS 498-74 (Cantarella et al 2006), Klebsiella oxytoca (Kao et al 2006), Cryptococcus sp. UFMG-Y28 (Rezende et al 2000), Bacillus sp.…”

Section: Discussionmentioning

confidence: 99%

Nitrilase gene detection and nitrile metabolism in two bacterial strains associated with waste streams in Lagos, Nigeria

et al. 2022

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Background The use of nitrile compounds is usually high, particularly in chemical industries, which calls for serious concern because of their relevance to the environment. The essential role of nitrilases in the bioremediation of harmful nitriles from environmental wastes cannot be overemphasized. The study aimed to unveil the biodegradative potentials of bacterial strains associated with the degradation of nitrile pollutants. Methods Bacterial strains capable of utilizing glutaronitrile as the sole source of carbon and nitrogen were isolated from solid waste leachates by a selective enrichment culture technique. The test organisms were grown in mineral salts medium (MSM), and the metabolic products were determined using gas chromatography-flame ionization detection (GC-FID). The nitrilase gene was amplified by polymerase chain reaction (PCR) and by using appropriate primers. Results The growth studies showed that the test organisms grew on the two nitriles. The doubling times of 12.16 d and 9.46 d (specific growth rate, µ=0.082 d−1, 0.106 d−1) were obtained for each pure culture of Bacillus sp. srain WOD8 and Corynebacterium sp. srain WOIS2 on glutaronitrile (as single substrate), respectively. While the same strains had doubling times of 11.11 d and 10.00 d (µ=0.090 d−1, 0.100 d−1) on benzonitrile (as single substrate). However, the mixed culture (comprising the two strains) had doubling times of 7.40 d and 7.75 d (µ=0.135 d−1, 0.129 d−1) on glutaronitrile (as single and mixed substrates), respectively. While doubling times of 8.09 d and 8.71 d (µ=0.124 d−1, 0.115 d−1) were obtained for the same mixed culture on benzonitrile (as single and mixed substrates). Based on gas chromatographic analysis, the residual glutaronitrile concentrations at day 16 for strains WOD8 and WOIS2 were 35.77 g L−1 (72.2%) and 9.30 g L−1 (92.5%), respectively, whereas the residual benzonitrile concentrations for the same strains were 27.39 g L−1 (78.8%) and 13.79 g L−1 (89.2%), respectively. For the mixed culture, residual glutaronitrile and benzonitrile concentrations at day 16 were 13.40 g L−1 (88.5%) and 10.42 g L−1 (91.5%), respectively, whereas for the mixed substrates (glutaronitrile and benzonitrile), 7.21 g L−1 (91.7%) and 4.80 g L−1 (94.2%) of residual glutaronitrile and benzonitrile concentrations were obtained by the same consortium. The gene for nitrilase involved in nitrile degradation was detected in the genome of the bacterial strains. The amplified nitrilase gene gave PCR products of sizes 1400 bp and 1000 bp, as expected for strains WOD8 and WOIS2, respectively. 4-Cyanobutyric acid (4CBA), glutaric acid (GA), and benzoic acid (BA) were obtained as metabolites following nitrile degradation in vitro. Conclusion These results revealed that strains WOD8, WOIS2 and the mixed culture (consisting of the two strains) have proven to have the capacity to metabolize nitriles (glutaronitrile and benzonitrile) as the carbon and nitrogen sources. However, the mixed culture had higher nitrile degradation rate as compared to each pure culture of the two test organisms. These results also provide insight into the evolutionary genetic origin of a nitrilase gene that encodes an enzyme that catalyzes nitrile degradation in these strains. Hence, the bacterial strains that harbor this kind of gene may be used as promising biological agents for the remediation of sites polluted with nitriles, thereby opening new perspectives for encouraging data for a bioremediation bioprocess.

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“…), as well as waste products generated from industrial processes that require subsequent remedial treatment (Nyska and Ghanayem ; Cantarella et al . ; Zhang et al . ).…”

Section: Introductionmentioning

confidence: 97%

“…Nitriles are important products or intermediates in the pharmaceutical, agricultural and chemical industries (Rezende et al 2003;Zheng et al 2008;Zhang et al 2009), as well as waste products generated from industrial processes that require subsequent remedial treatment (Nyska and Ghanayem 2003;Cantarella et al 2006;Zhang et al 2009). Nitriles can provide synthetic routes to synthesise enantiomerically pure b-hydroxy and b-amino acids, which form common structural motifs in many compounds of pharmaceutical importance (Ma et al 2008), including antimicrobial peptidomimetics (Godballe et al 2011).…”

Section: Introductionmentioning

confidence: 99%

Hydrolysis of nitriles by soil bacteria: variation with soil origin

et al. 2017

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Enzymes are typically substrate specific in their catalytic reactions, and this means that a wide diversity of enzymes is required to provide a comprehensive biocatalysis toolbox. This paper shows that the microbial diversity of nitrile hydrolysis activity can be targeted according to land utilization. Nitrile biocatalysis is a green chemical method for the enzymatic production of amides and carboxylic acids that has industrial applications, such as in the synthesis of acrylamide and nicotinamide. The biocatalysts discovered in this study may be applied to the synthesis of peptidomimetics which are an important class of therapeutic compounds.

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Nitrile bioconversion by Microbacterium imperiale CBS 498-74 resting cells in batch and ultrafiltration membrane bioreactors

Cited by 18 publications

References 30 publications

Enzymatic production of 2-amino-2,3-dimethylbutyramide by cyanide-resistant nitrile hydratase

Enzymatic production of 2-amino-2,3-dimethylbutyramide by cyanide-resistant nitrile hydratase

Nitrilase gene detection and nitrile metabolism in two bacterial strains associated with waste streams in Lagos, Nigeria

Hydrolysis of nitriles by soil bacteria: variation with soil origin

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