• Microbiology and Biotechnology Letters
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• v.25 no.5
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• pp.459-463
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• 1997

A bacterium DGUM 2011 has been selected from various samples of industrial wastewater and soil. Based on the morphological and physiological characteristics, the isolate DGUM 2011 was identified as Rhodococcus sp. and named as Rhodococcus sp. DGUM 2011. The optimal temperature and pH for the cell growth of Rhodococcus sp. DGUM 2011 were 37$\circ$C and 7.6, respectively. When phenol was added to the minimal media as a sole source of carbon and energy, the concentrations of maximum and optimum for cell growth was 0.10% and 0.08%, respectively. When 0.05% phenol was given in the minimal media, Rhodococcus sp. DGUM 2011 completely utilize it within 24 hrs. The isolate could utilize benzoic acid, p-hydroxybenzoate, p-cresol, tyrosine and phloroglucinol. The isolate possessed both catechol 1,2-dioxygenase and 2,3-dioxygenase activity. However, the activity of catechol 1,2-dioxygenase was much higher than that of 2,3-dioxygenase, which suggests that the isolate might degrade phenol via both ortho- and meta-cleavage, mainly via ortho-cleavage.

• KSBB Journal
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• v.18 no.3
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• pp.174-179
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• 2003

The bacterium NFQ-1 capable of utilizing quinoline (2,3-benzopyridine) as the sole source of carbon, nitrogen and energy was enriched and isolated from soil samples of dead coal pit areas. Strain NFQ-1 was identified as Pseudomonas nitroreducens NFQ-1 by BIOLOG system, and assigned to Pseudomonas sp. NFO-1. Pseudomonas sp. NFQ-1 was used with the concentration range of 1 to 10 mM quinoline. Strain NFQ-1 could degrade 2.5 mM quinoline within 9 hours of incubation. Initial pH 8.0 in the culture was reduced to 6.8, and eventually 7.0 as the incubation was proceeding. 2-Hydroxyquinoline, the first intermediate of the degradative pathway, accumulated transiently in the growth medium. The highest concentration of quinoline (15 mM) in this work inhibited cell growth and quinoline degradation. Pseudomonas sp. NFQ-1 was able to utilize various quinoline derivatives and aromatic compounds including 2-hydroxyquinoline, p-comaric acid, benzoic acid, p-cresol, p-hydroxybenzoate, protocatechuic acid, and catechol. The specific activity of catechol oxygenases was determined to approximately 184.7 unit/㎎ for catechol 1.2-dioxygenase and 33.19 unit/㎎ for catechol 2,3-dioxygenase, respectively. As the result, it showed that strain NFQ-1 degraded quinoline via mainly orthp-cleavage pathway, and in partial meta-cleavage pathway.

• Current Research on Agriculture and Life Sciences
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• v.3
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• pp.21-27
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• 1985

A bacterium which utilizes ${\varepsilon}$-caprolactam as a sole source of carbon and nitrogen was isolated from sludge of Shinchun river in Taegu and identified as Arthrobacter globiformis N-2-l. The growth medium for the optimum culture condition was composed of 0.4% ${\varepsilon}$-caprolactam, 0.02% $K_2HPO_4$, 0.05% $KH_2PO_4$, 0.02% $MgSO_4{\cdot}7H_2O$, 0.01% $FeCl_3{\cdot}6H_2O$ and 0.05% yeast extract. The optimum pH and temperature for growth were 7.0 and $30^{\circ}C$ respectively. The bacterial growth on the ${\varepsilon}$-caprolactam medium did not require any other organic nitrogen source such as yeast extract, although it was remarkably stimulated by the yeast extract. The bacteria utilized wide range of sugars and organic acids such as ${\alpha}$-ketoglutarate, adipate and P-hydroxybenzoate. The bacteria could use all kind of amino acids, ${\varepsilon}$-Caprolactam in the medium was consumed completely in the timecourse culture at $30^{\circ}C$ for 60 hr on the shaker by the bacteria. Decomposition product of ${\varepsilon}$-caprolactam by Arthrobacter globiformis N-2-1 was ${\varepsilon}$-aminocaproic acid.

• Microbiology and Biotechnology Letters
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• v.13 no.1
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• pp.71-77
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• 1985

A bacterium which grows on cyclohexanol as sole carbon and energy source was isolated from sludge of industrial areas in Taegu and identified as Acinetobacter calcoaceticus C-15. The growth medium for the optimal culture condition was composed of 0.2% cyclohexanol, 0.11% $NH_4Cl$, 0.05% $KH_2PO_4$, 0.2% $K_2HPO_4$, 0.02% $MgSO_4{\cdot}7H_2O$, and 0.05% yeast extracts. The optimal pH value and temperature for the growth were 7.2 and $33^{\circ}C$, respectively. Specific growth rate of A. calcoaceticus C-15 at $33^{\circ}C$ on the cyclohexanol and cyclohexanone was $0.27hr^{-1}$ and $0.15hr^{-1}$, respectively. Growth yield for cyclohexanol was 1.0. The bacteria utilized ethanol, 1-butanol, 1-pentanol, and cyclohexanol as a carbon source but not methanol, 1-hexanol, m-cresol, glycerol, and cyclohexane. The bacteria grew on benzoate, adipate, acetate, and citrate, but did not on salicylate, phthalate, p-hydroxybenzoate, and gluconate. A calcoaceticus C-15 did not utilize all kind of sugars other than xylose. Cell-free extracts contained $NAD^+$-linked cyclohexanol dehydrogenase which catalized the oxidation of cyclohexanol to cyclohexanone.

• Fibers and Polymers
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• v.1 no.2
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• pp.83-91
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• 2000

Thermotropic liquid crystalline polymer made up of poly(p-hydroxybenzoate) (PHB)-poly(ethylene terephthalate)(PET) 8/2 copolyester, poly(ethylene 2,6-naphthalate) (PEN) and PET were mechanically blended to pursue the liquid crystalline phase of ternary blends. Complex viscosities of blends decreased with increasing temperature and PHB content. DSC thermal analysis indicated that glass transition temperature (Tg) and melting temperature (Tm) of blends increased with increasing PHB content. Both tensile strength and initial modulus increased with raising PHB content and take-up speed of monofilaments. In the WAXS diagram, only PEN crystal reflection at 2Θ=$15.5^{\circ}C$ appeared but PET crystal reflection was not shown in all compositions. The degree of transesterification and randomness of blends increased with blending time but sequential length of both PEN and PET segment decreased.

• Journal of Microbiology and Biotechnology
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• v.31 no.7
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• pp.999-1010
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• 2021

Polycyclic aromatic hydrocarbons (PAHs) are ubiquitous in the environment. They are highly toxigenic and carcinogenic. Probiotic bacteria isolated from fermented foods were tested to check their ability to degrade and/or detoxify PAHs. Five probiotic bacteria with distinct morphologies were isolated from a mixture of 26 fermented foods co-cultured with benzo(a)pyrene (BaP) containing Bushnell Haas minimal broth. Among them, B. velezensis (PMC10) significantly reduced the abundance of BaP in the broth. PMC10 completely degraded BaP presented at a lower concentration in broth culture. B. velezensis also showed a clear zone of degradation on a BaP-coated Bushnell Haas agar plate. Gene expression profiling showed significant increases of PAH ring-hydroxylating dioxygenases and 4-hydroxybenzoate 3-monooxygenase genes in B. velezensis in response to BaP treatment. In addtion, both live and heat-killed B. velezensis removed BaP and naphthalene (Nap) from phosphate buffer solution. Live B. velezensis did not show any cytotoxicity to macrophage or human dermal fibroblast cells. Live-cell and cell-free supernatant of B. velezensis showed potential anti-inflammatory effects. Cell-free supernatant and extract of B. velezensis also showed free radical scavenging effects. These results highlight the prospective ability of B. velezensis to biodegrade and remove toxic PAHs from the human body and suggest that the biodegradation of BaP might be regulated by ring-hydroxylating dioxygenase-initiated metabolic pathway.

• Journal of Life Science
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• v.25 no.5
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• pp.487-495
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• 2015

We carried out pH stability, chemical inhibition, chemical modification, and pH-dependent kinetic parameter assessments to further characterize protocatechuate 3,4-dioxygenase from Pseudomonas pseudoalcaligenes KF707. Protocatechuate 3,4-dioxygenase was stable in the pH range of 4.5~10.5. L-ascorbate and glutathione were competitive inhibitors with $K_{is}$ values of 0.17 mM and 0.86 mM, respectively. DL-dithiothreitol was a noncompetitive inhibitor with a $K_{is}$ value of 1.57 mM and a $K_{ii}$ value of 8.08 mM. Potassium cyanide, p-hydroxybenzoate, and sodium azide showed a noncompetitive inhibition pattern with $K_{is}$ values of 55.7 mM, 0.22 mM, and 15.64 mM, and $K_{ii}$ values of 94.1 mM, 8.08 mM, and 662.64 mM, respectively. $FeCl_{2}$ was the best competitive inhibitor with a $K_{is}$ value of $29{\mu}M$. $FeCl_{3}$, $MnCl_{2}$, $CoCl_{2}$, and $AlCl_{3}$ were also competitive inhibitors with $K_{is}$ values of 1.21 mM, 0.85 mM, 3.98 mM, and 0.21 mM, respectively. Other metal ions showed noncompetitive inhibition patterns. The pH-dependent kinetic parameter data showed that there may be at least two catalytic groups with pK values of 6.2 and 9.4 and two binding groups with pK values of 5.5 and 9.0. Lysine, cysteine, tyrosine, carboxyl, and histidine were modified by their own specific chemical modifiers, indicating that they are involved in substrate binding and catalysis.

• Applied Biological Chemistry
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• v.13 no.3
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• pp.197-205
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• 1970

Inositols are cyclohexanehexol and they have been known to be nine stereomers. Scyllo-inositol, epi-inositol and muco-inositol could be synthesized from myo-inositol. Scyllo-inositol and epi-inositol were obtained by oxidation and reduction process from myo-inositol. Myo-inositol and epi-inositol were oxidized by treatment, in solution, with dilute hydrogen peroxide. In all cases, only axial hydroxyl groups were oxidized and monoketons were obtained. Reduction of myo-inosose-2 with sodium boron hydride was carried out in $pH2{\sim}3.$ The reduction products were equatorial alcohol but: reduction of DL-epi-inosose-2 by catalytic reduction produced axial alcohol obtained. Inositol could be esterified. Hexa-O-(p-hydroxy benzoyl)-esters of myo-inositol, scyllo-inositol, epi-inositol and muco-inositol were synthesized and their antimicrobial action on microbes were tested for application to food industry. As the results, it was found that the activities of muco-inositol ester was more vigorous than others.

• Microbiology and Biotechnology Letters
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• v.23 no.3
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• pp.255-262
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• 1995

Intact cells of Acinetobacter sp. T5-7 completely degraded trichloroethylene (TCE) following growth with phenol. This strain could grow on at least eleven aromatic compounds, e.g., benzaldehyde, benzene, benzoate, benzylalochol, catechol, caffeic acid, 2.4-D, p-hydroxybenzoate, phenol, protocatechuate and salicylate, and did grow on alkane, such as octane. But except phenol, other aromatic compounds did not induced TCE degradation. Phenol biotransformation products, catechol was identified in the culture media. However, catechol-induced cells did not degrade TCE. So we assumed that phenol hydroxylase was responsible for the degradation of TCE. The isolate T5-7 showed growth in MM2 medium containing sodium lactate and catechol rather than phenol, but did not display phenol hydroxyalse activity, suggesting induction of enzyme synthesis by phenol. Phenol hydroxylase activity was independent of added NADH and flavin adenine dinucleotide but was dependent on NADPH addition. Degradation of phenol produced catechols which are then cleaved by meta-fission. We identified catechol-2.3-dioxygenase by active staining of polyacrylamide gel.

• Applied Biological Chemistry
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• v.39 no.6
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• pp.472-476
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• 1996

The major portions of two DNA fragments, one from degradative plasmid, pRA4000 from Pseudomonas putida NCIMB 9866, and the other from degradative plasmid, pRA500 from P. putida NCIMB 9869, which harbor the structural genes for the flavoprotein (pchF) and cytochrome (pchC) subunits of p-cresol methylhydroxylase (PCMH), have been sequenced. The DNA and deduced amino acid sequences for pchC and pchF have been published. In these fragments, a coding region (dhal) for an aldehyde dehydrogenase has been identified. It is proposed that this gene encodes for the aldehyde dehydrogenase which converts p-hydroxybenzyaldehyde to p-hydroxybenzoate. p-Hydroxybezealdehyde is the product of oxidation of p-cresol by PCMH. The fragment from P. putida 9869 also harbors the genes for the ${\alpha}$ (pcaG) and ${\beta}$ (pcaH) subunits of protocatechuate 3,4-dioxigenase. The fragment from 9866 does not have any portion of these genes in the corresponding region A possible open reading frame (ORF) between pchC and pchF is seen for both clones, and a second putative open reading frame (ORF') also exists in the 9866 clone. The gene organizations are dhal-pchC-ORF-pchF-pcaGH for the DNA fragment from 9869, and ORF-dhal-pchC-ORF-pchF for the DNA fragment from 9866.