Academic literature on the topic 'Rhodococcus rhodochrous'

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Journal articles on the topic "Rhodococcus rhodochrous"

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Jones, Amanda L., June M. Brown, Vachaspati Mishra, John D. Perry, Arnold G. Steigerwalt, and Michael Goodfellow. "Rhodococcus gordoniae sp. nov., an actinomycete isolated from clinical material and phenol-contaminated soil." International Journal of Systematic and Evolutionary Microbiology 54, no. 2 (March 1, 2004): 407–11. http://dx.doi.org/10.1099/ijs.0.02756-0.

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The taxonomic relationships of two actinomycetes provisionally assigned to the genus Rhodococcus were determined using a polyphasic taxonomic approach. The generic assignment was confirmed by 16S rRNA gene similarity data, as the organisms, strains MTCC 1534 and W 4937T, were shown to belong to the Rhodococcus rhodochrous subclade. These organisms had phenotypic properties typical of rhodococci; they were aerobic, Gram-positive, weakly acid-fast actinomycetes that showed an elementary branching-rod–coccus growth cycle and contained meso-diaminopimelic acid, arabinose and galactose in whole-organism hydrolysates, N-glycolated muramic acid residues, dehydrogenated menaquinones with eight isoprene units as the predominant isoprenologue and mycolic acids that co-migrated with those extracted from the type strain of R. rhodochrous. The strains had identical phenotypic profiles and belong to the same genomic species, albeit one distinguished from Rhodococcus pyridinivorans, with which they formed a distinct phyletic line. They were also distinguished from representatives of all of the species classified in the R. rhodochrous 16S rRNA gene tree using a set of phenotypic features. The genotypic and phenotypic data show that the strains merit recognition as a novel species of Rhodococcus. The name proposed is Rhodococcus gordoniae sp. nov., with the type strain W 4937T (=DSM 44689T=NCTC 13296T).
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RASTIMESINA, Inna, Olga POSTOLACHI, and Valentina JOSAN. "Dissociation of Rhodococcus rhodochrous Population after the Whole Cells Immobilization." Bulletin of University of Agricultural Sciences and Veterinary Medicine Cluj-Napoca. Agriculture 78, no. 1 (May 14, 2021): 28. http://dx.doi.org/10.15835/buasvmcn-agr:2020.0043.

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Six agricultural organic wastes and three inorganic matrices were selected for rhodococci whole cells immobilization. The degree of immobilization of rhodococci cells varied from 6.20% to 34.30% on organic matrices. A high level of Rhodococcus rhodochrous CNMN-Ac-05 cells immobilization was demonstrated on inorganic matrices, it was from 69.25% to 97.30%. After the contact with support the strain dissociated, forming, in addition to original S type, rough (R) and altercolour smooth (S) types. Immobilization of rhodococci cells on organic supports led to the appearance of phenotypic heterogeneity from 0.34% to 3.26%. On inorganic matrices the variability of rhodococci was 0.88-1.05%.
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Nagasawa, Toru, Marco Wieser, Tetsuji Nakamura, Hitomi Iwahara, Toyokazu Yoshida, and Kunihiko Gekko. "Nitrilase of Rhodococcus rhodochrous J1." European Journal of Biochemistry 267, no. 1 (January 2000): 138–44. http://dx.doi.org/10.1046/j.1432-1327.2000.00983.x.

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Shim, Sang Hee. "Diketopiperazines from Cultures of Rhodococcus rhodochrous." Chemistry of Natural Compounds 52, no. 6 (October 25, 2016): 1157–59. http://dx.doi.org/10.1007/s10600-016-1894-y.

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Deng, Y., I. Beadham, M. Ghavre, M. F. Costa Gomes, N. Gathergood, P. Husson, B. Légeret, B. Quilty, M. Sancelme, and P. Besse-Hoggan. "When can ionic liquids be considered readily biodegradable? Biodegradation pathways of pyridinium, pyrrolidinium and ammonium-based ionic liquids." Green Chemistry 17, no. 3 (2015): 1479–91. http://dx.doi.org/10.1039/c4gc01904k.

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Krum, Jonathan G., and Scott A. Ensign. "Heterologous Expression of Bacterial Epoxyalkane:Coenzyme M Transferase and Inducible Coenzyme M Biosynthesis in Xanthobacter Strain Py2 andRhodococcus rhodochrous B276." Journal of Bacteriology 182, no. 9 (May 1, 2000): 2629–34. http://dx.doi.org/10.1128/jb.182.9.2629-2634.2000.

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ABSTRACT Coenzyme M (CoM) (2-mercaptoethanesulfonic acid) biosynthesis is shown to be coordinately regulated with the expression of the enzymes of alkene and epoxide metabolism in the propylene-oxidizing bacteriaXanthobacter strain Py2 and Rhodococcus rhodochrous strain B276. These results provide the first evidence for the involvement of CoM in propylene metabolism by R. rhodochrous and demonstrate for the first time the inducible nature of eubacterial CoM biosynthesis.
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Clark, Daniel D., and Scott A. Ensign. "Evidence for an Inducible Nucleotide-Dependent Acetone Carboxylase in Rhodococcus rhodochrousB276." Journal of Bacteriology 181, no. 9 (May 1, 1999): 2752–58. http://dx.doi.org/10.1128/jb.181.9.2752-2758.1999.

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ABSTRACT The metabolism of acetone was investigated in the actinomyceteRhodococcus rhodochrous (formerly Nocardia corallina) B276. Suspensions of acetone- and isopropanol-grownR. rhodochrous readily metabolized acetone. In contrast,R. rhodochrous cells cultured with glucose as the carbon source lacked the ability to metabolize acetone at the onset of the assay but gained the ability to do so in a time-dependent fashion. Chloramphenicol and rifampin prevented the time-dependent increase in this activity. Acetone metabolism by R. rhodochrous was CO2 dependent, and 14CO2 fixation occurred concomitant with this process. A nucleotide-dependent acetone carboxylase was partially purified from cell extracts of acetone-grownR. rhodochrous by DEAE-Sepharose chromatography. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis suggested that the acetone carboxylase was composed of three subunits with apparent molecular masses of 85, 74, and 16 kDa. Acetone metabolism by the partially purified enzyme was dependent on the presence of a divalent metal and a nucleoside triphosphate. GTP and ITP supported the highest rates of acetone carboxylation, while CTP, UTP, and XTP supported carboxylation at 10 to 50% of these rates. ATP did not support acetone carboxylation. Acetoacetate was determined to be the stoichiometric product of acetone carboxylation. The longer-chain ketones butanone, 2-pentanone, 3-pentanone, and 2-hexanone were substrates. This work has identified an acetone carboxylase with a novel nucleotide usage and broader substrate specificity compared to other such enzymes studied to date. These results strengthen the proposal that carboxylation is a common strategy used for acetone catabolism in aerobic acetone-oxidizing bacteria.
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Postolachi, O., I. Rastimesina, V. Josan, and T. Gutul. "Viability and Colony Morphology Variation of Rhodococcus rhodochrous CNMN-Ac-05 in the Presence of Magnetite Nanoparticles." Mikrobiolohichnyi Zhurnal 83, no. 4 (August 17, 2021): 35–42. http://dx.doi.org/10.15407/microbiolj83.04.035.

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In recent decades the use of nanotechnologies in the remediation of xenobiotic substances has proven its effectiveness, but not its safety. Nanoparticles often accumulate in the remedied environment, having, over time, toxic effects on living organisms. In this context, research on the vital activity of microorganisms and their interaction with nanoparticles is of major importance. Aim of the research was to determine the influence of Fe3O4 nanoparticles, obtained by different ways (laboratory method and synthesis in the reactor) on the viability and colony morphology of Rhodococcus rhodochrous CNMN-Ac-05 strain. Methods. Encapsulated magnetite (Fe3O4) nanoparticles were synthesized by chemical co-precipitation method, using iron(II) sulfate and iron(III) chloride in the presence of poly-N-vinylpyrrolidone, used as a stabilizer. Fe3O4 SR (Synthesis in the Reactor) was produced in the multifunctional reactor VGR-50, at the same conditions. Cell biomass was determined on the spectrophotometer by the optical density at 540 nm,with subsequent recalculation to cell dry weight according to the calibration curve. The cell dry weight was determined by gravimetric method. The morphological features of the rhodococci colonies were described according to the standard microbiological method. Results. It was established that magnetite nanoparticles in concentrations of 1–100 mg/L were not toxic to the R. rhodochrous strain, had a positive effect on the viability of rhodococci by stimulating the growth of biomass, regardless of their concentration and the method of their synthesis. In the presence of Fe3O4 nanoparticles the population dissociated to S1, S2, R1, R2 forms, and S-R type of colonies, while the basic morphological features of R. rhodochrous colonies corresponded to type S1. Conclusions. The optimal concentration of magnetite nanoparticles, which stimulated the growth and development of R. rhodochrous was 25 mg/L for Fe3O4 and 50 mg/L Fe3O4 SR. At all concentration of Fe3O4 nanoparticles the main colony morphotype of the rhodococci was smooth S1-type; the new types of colonies represented only 0.1–0.6% of the population, and the lowest degree of variability corresponded with the highest colony-forming units index.
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Hoyle, Alison J., Alan W. Bunch, and Christopher J. Knowles. "The nitrilases of Rhodococcus rhodochrous NCIMB 11216." Enzyme and Microbial Technology 23, no. 7-8 (November 1998): 475–82. http://dx.doi.org/10.1016/s0141-0229(98)00076-3.

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Haroune, Nicolas, Bruno Combourieu, Pascale Besse, Martine Sancelme, Achim Kloepfer, Thorsten Reemtsma, Heleen De Wever, and Anne-Marie Delort. "Metabolism of 2-Mercaptobenzothiazole by Rhodococcus rhodochrous." Applied and Environmental Microbiology 70, no. 10 (October 2004): 6315–19. http://dx.doi.org/10.1128/aem.70.10.6315-6319.2004.

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ABSTRACT 2-Mercaptobenzothiazole, which is mainly used in the rubber industry as a vulcanization accelerator, is very toxic and is considered to be recalcitrant. We show here for the first time that it can be biotransformed and partially mineralized by a pure-culture bacterial strain of Rhodococcus rhodochrous. Three metabolites, among four detected, were identified.
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Dissertations / Theses on the topic "Rhodococcus rhodochrous"

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Strachan, Philip. "Catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259." Thesis, University of Glasgow, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337527.

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Harris, Randall. "Degradation of dichloroalkanes by Rhodococcus rhodochrous and Pseudomonas oleovorans." Thesis, McGill University, 2005. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=98965.

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The degradation of C8-C16 alpha,beta-dichloroalkanes by Rhodococcus rhodochrous ATCC 13808 and Pseudomonas oleovorans ATCC 29347 was studied. The carbon chain length of the alpha,beta-dichloroalkane influenced the degradation rates of these compounds and the observed trends were species-dependent. R. rhodochrous exhibited faster rates towards the longer-chained compounds whereas P. oleovorans most rapidly degraded the shorter-chained compounds. This observation is consistent with the chain-length specificity of the hydroxylase enzymes responsible for initiating the degradation of alkanes by each organism. Studies conducted in a cyclone batch reactor indicated that alpha,beta-dichloroalkanes are modified to chlorinated metabolites prior to the dechlorination step. This indicates that the degradation of alpha,beta-dichloroalkanes is initiated by a hydroxylase acting on the non-chlorinated end of the molecule.
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Ashraf, William. "The genetics and biochemistry of a propane-utilizing "Rhodococcus rhodochrous"." Thesis, University of Warwick, 1990. http://wrap.warwick.ac.uk/3991/.

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The pathways of terminal and subterminal propane oxidation have been investigated in a propane-utilizing R. rhodochrous PNKbl. NTG-generated pleiotrophic mutants, characterized by their inability to utilize propane have been isolated. Several classes of mutants have been obtained which are unable to metabolize potential propane oxidation intermediates, e. g. propanol (alcA- or alcB-), propanal (ald-), acetone (ket-), propanoate (oate-) and acetate (ace-). Only ket- mutants retained the ability to metabolize propane. Mutants defective in the first step of propane metabolism (aik-), were also unable to metabolize acetol (a potential subterminal intermediate). Mutant analysis suggests that propane is oxidized via terminal and subterminal pathways in R. rhodochrous PNKbl. However, acetone (a potential subterminal intermediate) does not appear to have a role in propane metabolism. A propane-specific 86 kDa NAD+-dependent secondary alcohol dehydrogenase has been purified to homogeneity. This enzyme oxidizes a range of primary and secondary aliphatic alochols (C2 to C8). It is also responsible for both propan-l-ol and propan-2-ol dehydrogenase activities measured in cell-free extracts of propane-grown cells. Western-blot analysis has shown that it is induced during growth on propane, propan-2-ol, acetol and acetate (subterminal intermediates); but not propan-l-ol, propanal propanoate (terminal intermediates) or acetone. This technique has also demonstrated that a conserved NAD+-dependent alcohol dehydrogenase was induced in Rhodococcus - Nocardia bacteria after growth on propane. SDS-PAGE revealed proteins specific to cells grown on propane and acetol, which may be components of a novel propane/acetol oxygenase system. Oxygenase activity, as demonstrated by the epoxidation of propene, was induced after growth on propane and acetol. NADPHdependent acetol oxygenase activity was also detected. These results suggest a relationship between the metabolism of propane and acetol. Mutants unable to utilize propan-l-ol or propan-2-ol (aicA- and aicB- respectively) were examined by assaying for NAD+-dependent propan-l-ol and propan-2-ol dehydrogenase activities, by using SDS-PAGE analysis of cell-free extracts and comparing the pattern and distribution of pol peptides with the wild-type, and by Western-blot analysis of the NAD -dependent secondary alcohol dehydrogenase synthesized by aicmutants. Results demonstrated the aic- mutants had generally lower NAD+-dependent alcohol dehydrogenase activities altered polypeptide patterns and that alcB mutants synthesized NAD-dependent secondary alcohol dehydrogenase which had altered electrophoretic mobility after non-denaturing PAGE. The latter result may explain the inability of these mutants to utilize propan-2-ol as a growth substrate. The development of a plasmid transformation and gene transfer system for R. rhodochrous PNKbl based on previously published methods has also been assessed. Finally, a model for the pathway of propane oxidation in R. rhodochrous PNKbl is also presented showing oxidation via terminal and subterminal carbon atoms.
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Paylor, Michael Mark. "Biotransformation of organosulfides with the bacterium Rhodococcus rhodochrous ATCC 19067." Thesis, University of Exeter, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.245300.

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Dadd, Michael Richard. "Chiral biotransformations of cylclic nitrile compounds." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365818.

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Drago, Gene K. "Studies Directed to the Optimization of Fermentation of Rhodococcus sp. DAP 96253 and Rhodococcus rhodochrous DAP 96622." Digital Archive @ GSU, 2007. http://digitalarchive.gsu.edu/biology_diss/24.

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Studies Directed to the Optimization of Fermentation of Rhodococcus sp. DAP 96253 and Rhodococcus rhodochrous DAP 96622 by GENE KIRK DRAGO Under the Direction of George E. Pierce ABSTRACT Bench- and pilot plant scale fed-batch fermentations were performed in stirred-tank bioreactors (STBR) with Rhodococcus sp. DAP 96253 and R. rhodochrous DAP 96622 in an attempt to elucidate parameters that may affect the optimization of a fermentation process for high biomass production and high inducible expression of cobalt-high-molecular-mass nitrile hydratase (Co-H-NHase. The effects of these factors on amidase (AMDase) activity were also investigated. Biomass and NHase production were inhibited by a total addition of acetonitrile and acrylonitrile (AC / AN) at 500 ppm during a 48 h run. Biomass and enzyme activity were uncoupled when the inoculum mass was increased from 4 g (wet weight) to ¡Ý 19 g. Other factors that allowed for the uncoupling of biomass production from enzyme activity were the reduction of the AC / AN feed rate from a step-addition at 2500 ¦Ìl / min to a continuous addition at 80 ¨C 120 ¦Ìl / min, and the delay to 18 h post-inoculation the time of initial inducer addition. The inhibition of both biomass production and NHase activity was relieved when both the total concentration of AC / AN was reduced to ¡Ü 350 ppm and the AC / AN feedrate was reduced. The factors with the greatest influence were shown to be the inducer, the inducer concentration, inoculum mass and source as well as the major carbohydrate and nitrogen source. In addition, this lab is the first to report high AN-specific NHase induction by asparagine (1300 ppm) in a fed-batch fermentation system. Prior to this program, 250 mg of cells (wet weight) per liter could be provided in 4 ¨C 10 days with an activity of 1 U NHase per mg of cells (dry weight). Current production is > 50 g / L in 48 h with an NHase activity > 150 U / mg of dry cell weight. INDEX WORDS: Amidase, Asparagine, Biodetoxification, Fermentation, Nitrile, Nitrile Hydratase, Rhodococcus
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Mihdhir, Alaa. "The physiology, biochemistry and genetics of propane metabolism in Rhodococcus rhodochrous PNKB1." Thesis, University of Warwick, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.387396.

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Bui, Soi. "Characterisation of the RDX-degrading XplA/XplB redox system from Rhodococcus rhodochrous." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/characterisation-of-the-rdxdegrading-xplaxplb-redox-system-from-rhodococcus-rhodochrous(9355f6f0-62e8-4e07-ad16-786f00a957af).html.

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Hexahydro-1,3,5-trinitro-1,3,5-triazene (RDX) is a military explosive that has become a recalcitrant environmental pollutant over the last few decades owing to its production, storage and use. CYP177A1 (XplA) is a biotechnologically interesting and novel class of P450-flavodoxin fusion enzyme identified from Rhodococcus rhodochrous strain 11Y that catalyses the breakdown of RDX. Its redox partner is a NAD(P)H-dependent FAD-binding flavodoxin reductase (XplB). This study reports the biochemical, biophysical and structural properties of these two enzymes which form a novel P450 redox system with unique domain organisation. These reveal novel features for a P450 enzyme with non-standard UV/Visible spectroscopic features and unusual ligand binding properties. Unexpectedly, XplA’s affinity for imidazole is exceptionally high (Kd = 1.57 μM), explaining previous reports of a red- shifted XplA Soret band in pure enzyme. XplA’s true Soret maximum is at 417 nm. Similarly, the XplA flavodoxin domain displays unusually weak FMN binding (Kd = 1.09 μM), necessitating its reconstitution with the FMN cofactor. Ligand binding data demonstrate XplA’s constricted active site, which can only accommodate RDX and small inhibitory ligands (e.g. 4-phenylimidazole and morpholine) while discriminating against larger azole drugs. The crystal structure identifies a high affinity imidazole binding site, consistent with its low Kd, and shows active site penetration by PEG, perhaps indicative of an evolutionary lipid metabolising function for XplA. The substrate-free heme iron potential (-268 mV vs. NHE) is positive for a low spin P450, consistent with the predominantly reductive role of XplA. The elevated potential of the FMN semiquinone/hydroquinone couple (-172 mV) is also consistent with this functional adaptation. The XplB reductase partner could not be isolated with the FAD cofactor incorporated to make holoprotein. However, the protein was isolated in a soluble and homogenous state which demonstrated very weak FAD affinity. XplB’s ability to interact with XplA and a pyridine nucleotide coenzyme was demonstrated, indicating the enzyme was functional in the presence of FAD. XplA’s unusual molecular selectivity, structural and thermodynamic properties likely reflect its evolution as a specialised RDX reductase catalyst.
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Chorao, Charlène. "Etude du métabolisme de Rhodococcus rhodochrous lors de la photobiodégradation du 2-aminobenzothiazole." Phd thesis, Université Blaise Pascal - Clermont-Ferrand II, 2008. http://tel.archives-ouvertes.fr/tel-00731145.

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La biodégradation du 2-aminobenzothiazole (ABT) a été comparée entre des bactéries en suspension dans l'eau et des bactéries immobilisées sur un support d'alginate. Trois processus de dégradation de l'ABT ont été étudiés : la photodégradation sous lumière solaire en présence du complexe Fe(III)-acide nitrilotriacétique (FeNTA), la biodégradation par la bactérie aérobie stricte Rhodococcus rhodochrous et la combinaison de ces deux processus. Le métabolisme de R. rhodochrous a été étudié par RMN in vivo du 31P et du 13C : des informations importantes sur le métabolisme phosphoré et carboné ont été obtenues. La réponse de la bactérie face à divers stress a été évaluée et a montré sa capacité d'adaptation aux variations environnementales. La spéciation du fer pour son rôle important dans l'activation de la biodégradation d'ABT a été etudiée : complexes organiques, oxydes et oxy(hydr)oxydes de fer ont été testés pour connaître les formes biodisponibles pour R. rhodochrous
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Zhang, Jie. "Biofiltration of Acrylonitrile by Rhodococcus Rhodochrous DAP 96622 on a Trickling Bed Bioreactor." Digital Archive @ GSU, 2009. http://digitalarchive.gsu.edu/biology_diss/64.

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Acrylonitrile (AN) is a major volatile waste generated in the production of acrylamide and often associated with aromatic contaminants (toluene and styrene) in plant effluents. We examined Rhodococcus rhodochrous DAP 96622 to determine if it could be adapted to efficient biodegradation of acrylonitrile (AN) in a bioreactor. A model bioreactor with granular activated carbon (GAC) as a substratum for Rhodococcus with AN as sole carbon or in combination with toluene was established. The kinetics of AN biodegradation by immobilized and planktonic cells were evaluated and compared. Inlet load and empty retention time were varied to test the removal efficiency in fed-batch and single-pass mode reactor. In addition, the three dimensional structure and characteristics of the biofilm were followed using confocal scanning laser microscopy (CSLM) and relative software. Immobilized cells in the bioreactor, at starting concentrations of AN up to 1150 mg l-1 in the presence of Tol, had at least 13 fold higher AN degradation rates than that seen of planktonic cells. A near steady state of AN degradation was maintained at 75-85% for AN and 80%-90% for Tol within the parameter of EBRT=8 min and AN and Tol inlet loads between 50-200 mg l-1 h-1 and 200-500 mg l-1h-1, respectively. However, when the inlet load of AN was increased to more than 200mg l-1 h-1 and 500 mg l-1 h-1 for Tol, a reduction in efficiency of AN degradation was observed. Biofilms with discrete microcolonies interspersed with voids and channels were observed. Precise measurement of biofilm characteristics agreed with the assumption that the biomass and thickness of the biofilm increased along the carbon column depth. With a porous attachment material like GAC, substrate diffusion is most likely not a limiting factor for AN degradation. Rhodococcus rhodochrous DAP 96622 in a non-sterile activated charcoal column showed efficient degradation of AN in the presence of Tol. The Rhodococcus bioreactor may provide a potential practical waste gas and water treatment system.
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Books on the topic "Rhodococcus rhodochrous"

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Ashraf, William. The genetics and biochemistry of a propane-utilizing "rhodococcus rhodochrous". [s.l.]: typescript, 1990.

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Mihdhir, Alaa. The physiology, biochemistry and genetics of propane metabolism in Rhodococcus rhodochrous PNKb1. [s.l.]: typescript, 1993.

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Book chapters on the topic "Rhodococcus rhodochrous"

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Sinolitsky, M. K., S. M. Rogacheva, S. V. Poltavskaya, A. A. Sintin, and S. P. Voronin. "Purification and Characterization of Nitrile Hydratase from Rhodococcus rhodochrous M8." In Environmental Biotechnology, 96–104. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-017-1435-8_9.

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Bhalla, Tek Chand, Akira Miura, Akiko Wakamoto, Yoichi Ohba, Miho Aoshima, Ryo Muramatsu, and Keizo Furuhashi. "Purification and Characterization of Nitrilase Catalyzing Asymmetric Hydrolysis of Aminonitriles from Rhodococcus rhodochrous PA-34." In Biochemical Engineering for 2001, 225–27. Tokyo: Springer Japan, 1992. http://dx.doi.org/10.1007/978-4-431-68180-9_61.

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Hamilton, John T. G., Orla Flynn, Michael J. Larkin, and David B. Harper. "Incorporation of haloalkanes into long chain fatty acids by the chloroalkane-degrading bacterium Rhodococcus rhodochrous NCIMB 13064." In Environment & Chemistry, 213–20. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0061-8_18.

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Takaichi, Shinichi, and Jun-ichi Ishidsu. "[34] Carotenoid glycoside ester from Rhodococcus rhodochrous." In Methods in Enzymology, 366–74. Elsevier, 1992. http://dx.doi.org/10.1016/0076-6879(92)13138-n.

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Ashraf, W., and J. C. Murrell. "[5] Propane-specific alcohol dehydrogenase from Rhodococcus rhodochrous PNKb 1." In Hydrocarbons and Methylotrophy, 21–26. Elsevier, 1990. http://dx.doi.org/10.1016/0076-6879(90)88007-w.

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Conference papers on the topic "Rhodococcus rhodochrous"

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Eneh, Kennedy, Setu Patolia, Marie Frances Schmidt, Neerja Gulati, Mehjabin Zahir, Maximus Mora, Fadi Hammoudeh, Narayan neupane, Mohammed perwaiz, and Danilo Enriquez. "Rare Case Of Disseminated Rhodococcus Rhodochrous Infection In An Immunocompromised Host." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5702.

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"Functioning of unique nitrile-detoxifying system in soil xenobiotic degrader Rhodococcus rhodochrous: a whole-genome transcriptomic approach." In Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-031.

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Suryanti, Venty, Sri Hastuti, and Dwi Pujiastuti. "Evaluation of biosurfactants grown in corn oil by Rhodococcus rhodochrous on removing of heavy metal ion from aqueous solution." In PROCEEDINGS OF INTERNATIONAL SEMINAR ON MATHEMATICS, SCIENCE, AND COMPUTER SCIENCE EDUCATION (MSCEIS 2015). AIP Publishing LLC, 2016. http://dx.doi.org/10.1063/1.4941482.

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Reports on the topic "Rhodococcus rhodochrous"

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Kilbane, J. J., and B. A. Bielaga. Molecular biological enhancement of coal biodesulfurization. [Rhodococcus rhodochrous]. Office of Scientific and Technical Information (OSTI), July 1990. http://dx.doi.org/10.2172/6089976.

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Kilbane, J. J. II. Microbial strain improvement for organosulfur removal from coal. [Rhodococcus rhodochrous]. Office of Scientific and Technical Information (OSTI), January 1991. http://dx.doi.org/10.2172/5792238.

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Ho, N. W. Y. Characterization of the organic-sulfur-degrading enzymes. [IGTS8: a derivative of Rhodococcus rhodochrous]. Office of Scientific and Technical Information (OSTI), January 1991. http://dx.doi.org/10.2172/5792251.

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Srivastava, V. J. The effect of moderate coal cleaning on microbial removal of organic sulfur. [Rhodococcus rhodochrous]. Office of Scientific and Technical Information (OSTI), January 1991. http://dx.doi.org/10.2172/5986967.

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Kayser, K. J., B. A. Bielaga, K. Jackowski, O. Oduson, and J. II Kilbane. Characterization of carbon-sulfur bond cleavage by axenic and mixed cultures of Rhodococcus rhodochrous IGTS8. Office of Scientific and Technical Information (OSTI), December 1992. http://dx.doi.org/10.2172/10177078.

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Srivastava, V. J. The effects of moderate coal cleaning on the microbial removal of organic sulfur. [Rhodococcuc rhodochrous]. Office of Scientific and Technical Information (OSTI), January 1991. http://dx.doi.org/10.2172/6012831.

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