• Journal of Microbiology
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• v.34 no.4
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• pp.334-340
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• 1996

The enzyme, cis,cis-muconate lactonizing enzyme has been proposed to play a key role in the $\beta$-ketoadipate pathway of benzoate degradation. A 3.2-kb EcoRI fragment termed as pRSU2, isolated from a Pseudomonas cepacia genomic library was able to complement the catB defective mutant. Several relevant restriction enzyme sites were determined within the cloned fragment. In Pseudomonas putida SUC2 carrying pRSU2, the enzyme activity was relatively higher than those of the induced or partially induced state of wild type P. putida PRS2000. It was probably due to higher expression of P. cepacia catB in P. putida PRS2000. It was probably due to higher expression of P. cepacia catB in P. putida. One possible interpretation of these results is that the catB promoter in P. cepacia is recognized within P. putida, resulting in the almost same expression level.

• KSBB Journal
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• v.16 no.3
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• pp.286-289
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• 2001

A beterotrophic Pseudomonas putida B2 was used to treat of hydrogen sulfide containing gas. The experimental approach involved operating two indentical bench-scale biofilters with media consisting of a mixture of peatmoss, perlite and granular activated carbon(GAC). One column was seeded with Pseudomonas putida B2 and the other was left unseeded. The biofilter was operated for 16 days under EBRT for 20-40 sec, at a temperature of 25-30$^{\circ}C$ and a hydrogen sulfide concentration of 40-190 ppm. The biofilter inocculated with P.putida B2 exhibited high hydrogen sulfide removal efficiency, average of 95%, at a gydrogen sulfide concentration of 40-190 ppm (flow rate 3.6 L/min). However, at a shock loading of 190 ppm the biofiter showed a removal efficiency of 78.9% and the control only showed a removal efficiency of 31.6%. The critical load of this biofilter was 14.83 g/㎥hr, and the critical load of the control column was 4.93 g/㎥hr. These results suggest that P. putida B2 has the potential to be used as a $H_2S$ removal agent in a biofilter.

• KSBB Journal
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• v.13 no.5
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• pp.561-568
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• 1998

Two cometabolic trichloroethylene (TC) degraders, Pseudomonas putida F1 and Burkholderia (Pseudomonas) cepacia G4, were found to catabolize phenol, benzene, toluene, and ethylbenzene as carbon and energy sources. Resting cells of P. putida F1 and B. cepacia G4 grown in the presence of toluene and phenol, respectively, were able to degrade not only benzene, toluene and ethylenzene but also TCE and p-xylene. However, these two strains grown in the absence of toluene or phenol did not degrade TCE and p-xylene. Therefore, it was tentatively concluded that cometabolic degradation of TC and p-xylene was mediated by toluene dioxygenase (P. putida F1) or toluene-2-monooxygenase (B. cepacia G4). Maximal degradation rates of BTEX and TCE by toluene- and phenol-induced resting cells of P. putida F1 and B. cepacia G4 were appeared to be 4-530 nmol/(min$.$mg cell protein) when a single compound was solely served as a target substrate. In case of double substrates, the benzene degradation rate by P. putida F1 in the presence of toluene was decreased up to one seventh of that for the single substrate. TCE degradation rate was also linearly decreased as toluene concentration increased. On the other hand, toluene degradation rate was enhanced by benzene and TCE. For B. cepacia G4, degradation rates of TCE and toluene increased 4 times in the presence of 50 ${\mu}$M phenol. From these results, it was concluded that a degradation rate of a compound in the presence of another cosubstrate(s) could not be predicted by simply generalizing antagonistic or synergistic interactions between substrates.

• Korean Journal of Microbiology
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• v.38 no.4
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• pp.275-275
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• 2002

Pseudomonas sp. S-47 is capable of catabolizing 4-chlorobenzoate (4CBA) as carbon and energy sources under aerobic conditions via the mesa-cleavage pathway. 4CBA-dioxygenase and 4CBA-dihydrodiol dehydrogenase (4CBA-DD) catalyzed the degradation af 4CBA to produce 4-chlorocatechol in the pathway. In this study, the xylL gene encoding 4CBA-DD was cloned from the chromosomal DNA of Pseudomonas sp. S-47 and its nucleotide sequence was analyzed. The xylL gene was found to be composed of 777 nucleotide pairs and to encode a polypeptide of 28 kDa with 258 amino acid residues. The deduced amino acid sequence of the dehydrogenase (XylL) from strain S-47 exhibited 98% and 60% homologies with these of the corresponding enzymes, Pseudomonas putida mt-2 (XyIL) and Acinetobacter calcoaceticus (BenD), respectively. However, the amino arid sequences show 30% or less homology with those of Pseudomonas putida (BnzE), Pseudomonas putida Fl (TodD), Pseudomonas pseudoalcaligenes KF707 (BphB), and Pseudomonas sp. C18 (NahB). Therefore, the 4CBA-dihydrodiol dehdrogenase of strain S-47 belongs to the group I dehydrogenase involved in the degradation of mono-aryls with a carboxyl group.

• Environmental Engineering Research
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• v.15 no.4
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• pp.183-190
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• 2010

Biogenic Mn oxides are expected to have great potential in the control of water pollution due to their high catalytic activity, although information on biological Mn oxidation is not currently sufficient. In this study, the growth of a Mn oxidizing microorganism, Pseudomonas putida MnB1, was examined, with the Mn oxides formed by this strain characterized. The growth of P. putida MnB1 was not significantly influenced by Mn(II), but showed a slightly decreased growth rate in the presence of Pb(II) and EE2, indicating their insignificant adsorption onto the cell surface. Mn oxides were formed by P. putida MnB1, but the liquid growth medium and resulting biogenic solids were poorly crystalline, nano-sized particles. Biogenic Mn oxidation by P. putida MnB1 followed Michaelis-Menten kinetics, with stoichiometric amounts of Mn oxides formed, which corresponded with the initial Mn(II) concentration. However, the formation of Mn oxides was inhibited at high initial Mn(II) concentration, suggesting mass transfer obstruction of Mn(II) due to the accumulation of Mn oxides on the extracellular layer. Mn oxidation by P. putida MnB1 was very sensitive to pH and temperature, showing sharp decreases in the Mn oxidation rates outside of the optimum ranges, i.e. pH 7.43-8.22 and around 20-$26^{\circ}C$.

• Korean Journal of Microbiology
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• v.24 no.1
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• pp.51-56
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• 1986

Eight strains of the bacteria capable of growing on salicylate as the sole carbon source were isolated form soil and river water. Three of these isolates were identified as Acinetobacter calcoaceticus (AcBl), Pseuomonas putida biotype B (PpB2), and P. putida biotype A (PpB3). Effects of temperature, pH and C source concentration on biodegradation of salicylate by PpB3 were wxamined. The optimum conditions were as follows; $30^{\circ}C$ for temperature, 7.0 for pH, and 10mM for C source concentration. Ultraviolet scanning spectrum of the salicylate was measured. The spectrum has two peaks at 225nm and 292nm. The spectra of the culture filtrates indicate that ring degradation of salicylate is accomplished.

• Journal of Life Science
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• v.20 no.8
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• pp.1214-1220
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• 2010

Imipenem-resistant bacteria were isolated from clinical specimens taken from hospitalized patients in Suncheon, Korea. Fifty-four isolates were phylogenetically analyzed based on 16S rRNA gene and gyrB gene sequence comparisons. Isolates were affiliated with Pseudomonas aeruginosa (30 strains; 55.6%), Acinetobacter baumannii (21; 38.9%), Enterobacter hormaechei (2) and Pseudomonas putida (2). Twenty-two isolates produced metallo-$\beta$-lactamase (MBL); 12 Acinetobacter baumannii strains, 7 Pseudomonas aeruginosa strains, 2 P. putida strains and 1 Enterobacter hormaechei strain. Antibiotic susceptibility of the isolates was determined using the disc diffusion method and Vitek system. Strains producing metallo-$\beta$-lactamase (type IMP & VIM) were more resistant to antibiotics ceftazidime, aztreonam, amikacin and gentamicin than to strains producing OXA and SHV type of $\beta$-lactamase.

• Journal of Microbiology
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• v.41 no.2
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• pp.102-108
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• 2003

A 6.1 kb Sph I fragment from the genomic DNA of Pseudomonas putida SM 25 was cloned into the veetor pUC19. The open reading frame of catB was found to consist of 1,122 nucleotides. The sequence alignment of the catB gene products from different kinds of bacteria revealed an overall identity ranging from 40 to 98%. The catC gene contained an open reading frame of 96 codons, from which a protein with a molecular mass of about 10.6 kDa was predicted. The amino acids in the proposed activesite region of CatC were found to be almost conserved, including the charged residues. Since the catBC genes in P. putida SM25 were tightly linked, the could be regulated under coordinate transcription, and transcribed from a single promoter located upstream of the catB gene, as in P. putida RBI.

• Journal of Microbiology
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• v.38 no.4
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• pp.275-280
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• 2000

Pseudomonas sp. S-47 is capable of catabolizing 4-chlorobenzoate (4CBA) as rarbon and energy sources under aerobic conditions via the mesa-cleavage pathway. 4CBA-dioxygenase and 4CBA-dihydrodiol dehydrogenase (4CBA-DD) catalyzed the degradation af 4CBA to produce 4-chlorocatechol in the pathway. In this study, the xylL gene encoding 4CBA-DD was cloned from the chromosomal DNA of Pseudomonas sp. S-47 and its nucleotide sequence was analyzed. The xylL gene was found to be composed of 777 nucleotide pairs and to encode a polypeptide of 28 kDa with 258 amino acid residues. The deduced amino acid sequence of the dehydrogenase (XylL) from strain S-47 exhibited 98% and 60% homologies with these of the corresponding enzymes, Pseudomonas putida mt-2 (XyIL) and Acinetobacter calcoaceticus (BenD), respectively. However, the amino arid sequences show 30% or less homology with those of Pseudomonas putida (BnzE), Pseudomonas putida Fl (TodD), Pseudomonas pseudoalcaligenes KF707 (BphB), and Pseudomonas sp. C18 (NahB). Therefore, the 4CBA-dihydrodiol dehdrogenase of strain S-47 belongs to the group I dehydrogenase involved in the degradation of mono-aryls with a carboxyl group.

• Korean Journal of Microbiology
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• v.30 no.5
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• pp.410-414
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• 1992

Numerical identification was carried out for an isolate of Streptomyces strain producing the extracellular p-lactamase inhibitor. Fifty taxonomic unit characters were tested and the data were analyzed numerically using the TAXON program. The isolate was identified to the major cluster 5 of Streptomyces and it was best matched to Streptomyces omiyaensis which is a synonym of Streptomyces exfoliatus. Therefore, it was concluded that the isolate was identified to be a strain (SMF 19) of Streptomyces exjbliatus.