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Pseudomonas fluorescens-putida

Schwarz G, R Bauder, M Speer, TO Rommel, F Lingens 1989 Microbial metabolism of quinoline and related compounds 11. Degradation of quinoline by Pseudomonas fluorescens 3, Pseudomonas putida 86 and Rhodococcus spec. Bl.Biol Chem Hoppe-Seyler 370 1183-1189. [Pg.552]

Bossis, E. Lemanceau, R Latour, X. Gardan, L. The taxonomy of Pseudomonas fluorescens and Pseudomonas putida Current status and need for revision. Agronomie 2000, 20, 51-63. [Pg.16]

Schwarz, G. Bauder, R. Speer, M., et al., Microbial Metabolism of Quinoline and Related Compounds. II. Degradation of Quinoline by Pseudomonas Fluorescens 3, Pseudomonas Putida 86 and Rhodococcus Spec. Bl. Biol. Chem. Hoppe-Seyler, 1989. 370 pp. 1183-1189. [Pg.220]

Pseudomonas fluorescens, 1 732 11 4 Pseudomonas putida, 11 4 Pseudomonas testosteroni alcohol dehydrogenase, 3 672 Pseudopelletierine, 2 81-82 Pseudoplastic flow, 7 280t Pseudoplastic fluids, 11 768 Pseudoplasticity, 10 679 Pseudoplastic with yield stress flow, 7 280t Pseudopolymorphism, 8 69... [Pg.771]

All bacteria where nitrate ester degradation has been characterized have very similar enzymes. The enzymes eatalyze the nicotinamide cofactor-dependent reductive eleavage of nitrate esters that produces alcohol and nitrite. Purification of the PETN reduetase from Enterobacter cloacae yielded a monomerie protein of around 40 kilo Daltons, which required NADPH as a co-faetor for aetivity. Similar enzymes were responsible for the nitrate ester-degrading activity in Agrobacterium radiobacter (Snape et al. 1997) - nitrate ester reductase - and in the strains of Pseudomonas fluorescens and Pseudomonas putida (Blehert et al. 1999) - xenobiotic reduetases . All utilize a non-covalently bound flavine mononucleotide as a redox eofactor. [Pg.213]

Beiderbeck H (1997) Untersuchung der Pyoverdine aus Pseudomonas aeruginosa ATCC 15152, Pseudomonas fluorescens CFBP 2392 und Pseudomonas putida 2461. Diplomar-beit, Universitat zu Koln, and unpublished results... [Pg.55]

Beiderbeck H, Taraz K, Meyer JM (1999) Revised Structures of the Pyoverdins from Pseudomonas putida CFBP 2461 and from Pseudomonas fluorescens CFBP 2392. BioMe-tals 12 331-338... [Pg.55]

Budzikiewicz H, Kilz S, Taraz K, Meyer JM (1997) Identical Pyoverdines from Pseudomonas fluorescens 9AW and from Pseudomonas putida 9BW. Z Naturforsch 52c 721 Budzikiewicz H, Miinzinger M, Taraz K, Meyer JM (1997) Schizokinen, the Siderophore of the Plant Deleterious Bacterium Ralstonia (Pseudomonas) solanacearum ATCC 11969. Z Naturforsch 52c 496... [Pg.56]

Meyer JM, Stintzi A, Coulanges V, Shivaji S, Voss JA, Taraz K, Budzikiewicz H (1998) Siderotyping of Fluorescent Pseudomonads Characterization of Pyoverdines of Pseudomonas fluorescens and Pseudomonas putida Strains from Antarctica. Microbiology 144 3119... [Pg.66]

Incubation of Pseudomonas putida with anthracene-labeled carbon-base ferrichrome analog Fe(lll) complex 173 resulted in cellular iron uptake and the appearance of anthracene fluorescence in the culture medium identical to the Fe-ferrichrome uptake. Incubation with the alanyl analog 174 failed to show any significant iron uptake or fiuorescence. This is consistent with the tests described above on the unlabeled analogs. Remarkably, other strains such as Pseudomonas fluorescens S680 or WCS3742 also did not show any iron uptake or culture fluorescence. [Pg.795]

Acenaphchene Beijerinckia sp., Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas cepacia. Pseudomonas sp. 1-Acenaphchenol, l-acenaphthenone, acenaphthene-r -l,2-dihydrodiol, 1.2- acenaphthened ione, 1.2- di hydroxyacenaphchy lene, 7.8- diketonaphthyl-l-acetic acid, 1.8- naphthalenedicarboxylic acid, and 3-hydroxyphthalic acid, Chapman (1979), Scliocken Gibson (1984), Ellis et al. (1991), Komacsu et al. (1993), Selifonov et al. (1993). [Pg.138]

Pseudomonas fluorescens 3, Pseudomonas putida 86 and Rhodococcus sp. Bl. Biol. Chem. Hoppe-Seyler 370 1183-1189. [Pg.680]

Shim H., Yang S.T. 1999. Biodegradation of benzene, toluene. Ethylbenzene, and o-xylene by a coculture of Pseudomonas putida and Pseudomonas fluorescens immobilized in a fibrous-bed bioreactor, J. Biotechnol., 67, 99-112... [Pg.197]

Pseudomonas aeruginosa, Pseudomonas putida. Pseudomonas fluorescens, and Pseudomonas mendocina Serratia marcescens Yersinia enterocolitica... [Pg.680]

Figure 4, Minimum detectable concentrations of toluene and naphthalene as a function of integration time for the prototype BBIC containing either the Pseudomonas putida TVA8 (toluene) or Pseudomonas fluorescens 5RL (naphthalene) bioluminescent bioreporters. Figure 4, Minimum detectable concentrations of toluene and naphthalene as a function of integration time for the prototype BBIC containing either the Pseudomonas putida TVA8 (toluene) or Pseudomonas fluorescens 5RL (naphthalene) bioluminescent bioreporters.
Table 3 summarizes properties of intradiol-cleaving dioxygenases. 1,2-CTD was first isolated and purified from Pseudomonas fluorescens [3] and characterized as a dioxygenase by Hayaishi et al. [1] (2 g atoms of iron/mol, Mr 80 kDa). 1,2-CTD has been purified from Pseudomonas fluorescens by Nakazawa et al. (2 g atoms of iron/mol, Mr 100 kDa) [5], from Pseudomonas arvilla C-1 by Kojima et al. (2 g atoms of iron (ferric)/mol, Mr 90 kDa) [4] and by Nakai et al. (1 g atom of iron/mol, Mr 63 kDa, aP subunits), from Brevibacterium fuscum p-13 (1 g atom of iron/mol) [23], and from Pseudomonas putida mt-2 (1.1 g of iron/mol, Mr 65 kDa, aa subunits) [19]. Nakai et al. found that three isozymes of 1,2-CTD exist in Pseudomonas arvilla C-1 and are formed by combinations of two nonidentical subunits as dimers, aa, aP, PP [20]. Amino acid composition and sequence of 1,2-CTD were analyzed by Nakai et al. [8,19, 20]. [Pg.28]


See other pages where Pseudomonas fluorescens-putida is mentioned: [Pg.334]    [Pg.334]    [Pg.210]    [Pg.334]    [Pg.334]    [Pg.210]    [Pg.169]    [Pg.434]    [Pg.170]    [Pg.9]    [Pg.548]    [Pg.138]    [Pg.56]    [Pg.256]    [Pg.407]    [Pg.208]    [Pg.220]    [Pg.235]    [Pg.131]    [Pg.263]    [Pg.110]    [Pg.360]    [Pg.203]    [Pg.279]   
See also in sourсe #XX -- [ Pg.210 ]




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