• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.390-392
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• 2003

Organic solvent tolerant bacterium, Pseudomonas savastanoi BCNU 106 could utilize trichloroacetic acid, monochloroacetic acid, trichloroethylene, p-dichlorobenzene as a sole carbon source. But Pseudomonas savastanoi BCNU 106 didn't have tolerance about trichloroacetic acid, monochloroacetic acid, trichloroethylene, p-dichlorobenzene. Strain BCNU 106 could utilize to the extend of 30 mM trichloroacetic acid as a sole carbon source on mineral salt medium.

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.386-389
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• 2003

Organic solvent tolerance bacteria, Pseudomonas savastanoi BCNU 106 could utilize a high contentration of benzene, toluene, ethylbenzene, xylene isomers (BTEX) as a sole carbon source. It was founded that strain BCNU 106 transformed o-xylene to 2-methylbenzyl alcohol, 2-methylbenzoic acid through direct oxygenation of methyl residue on GC-MS analysis.

• Proceedings of the Korean Society of Life Science Conference
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• 2007.10a
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• pp.67.1-67.1
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• 2007

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• Journal of Microbiology and Biotechnology
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• v.28 no.9
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• pp.1502-1510
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• 2018

Organic solvent-tolerant (OST) enzymes are widely applied in various industries for their activity and stability in organic solvents, for their higher substrate solubility, and for their greater stero-selectivity. However, the criteria for identifying OST enzymes largely remain undefined. In this study, we compared the amino acid composition of 19 OST esterases with that of 19 non OST esterases. OST esterases have increased the ratio of Ala and Arg residues and decreased the ratio of Asn, Ile, Tyr, Lys, and Phe residues. Based on our amino acid composition analysis, we cloned a carboxylesterase (EstSP2) from a psychrophilic bacterium, Sphingomonas glacialis PAMC 26605, and characterized its recombinant protein. EstSP2 is a substrate specific to p-nitrophenyl acetate and hydrolyzed aspirin, with optimal activity at $40^{\circ}C$; at $4^{\circ}C$, the activity is approximately 50% of its maximum. As expected, EstSP2 showed tolerance in up to 40% concentration of polar organic solvents, including dimethyl sulfoxide, methanol, and ethanol. The results of this study suggest that selecting OST esterases based on their amino acid composition could be a novel approach to identifying OST esterases produced from bacterial genomes.

• Proceedings of the Membrane Society of Korea Conference
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• 1991.10a
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• pp.9-16
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• 1991

The current status of reverse osmosis and ultrafiltration membranes are reviewed with the view for the future. In the case of reverse osmosis (RO) membranes, as examples, new crosslinked aromatic polyamide membranes exhibited the superior separation performance with the sufficient water permeability, the high tolerance for oxidizing agents and chemicals. Ultrafiltration (UF) membrane based on poly(phenylene sulfide sulfone) (PPSS) also exibited the superior separation performance with the high solvent, heat and fouling resistance.

• Applied Biological Chemistry
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• v.36 no.1
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• pp.38-44
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• 1993

1) OBT7 mutant was isolated by W light-butanol tolerance from Clostridium saccharoperbutylacetonicm ATCC 13564 (N1-4 strain). The mutant produced 16.5 g/l (1.4-fold increase) of n-butanol, 4.65 g/l (1.5-fold increase) of acetone, and 21.5 g/l of total solvent. It was suggested that clostridial bacteria producing n-butanol does not have a poor effect on misrepair via an error-prone pathway by UV light-butanol tolerance. 2) Compared to glucose fermentation, in mannitol fermentation, OBT7 mutant did not produce acetone and acetic acid. And the ratios of n-butanol and ethanol to total solvents increased by 10.3% and 10.5%, respectively, totalling 20.8%, while the ratio of acetone was decreased by 21.2%. Also the maximum ratio of n-butanol to total solvents reached 94.8%. These results indicated that oxidized compound (acetone, acetic acid, and butyric acid) was converted to the reduced compounds (n-butanol, and ethanol). Therefore, mannitol can be used to eliminate by-products of oxidized compound.

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.801-806
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• 2003

Pseudomonas sp. BCNU 106 accumulated approximately 4.12 mM trehalose after cultivation of 12 hr probably by the arising action of trehalose-6-phosphate synthase/phosphatase. The cDNA clones of trehalose-6-phosphate synthase/ phosphatase were isolated from Pseudomonas sp. BCNU 106, and named as PsTPS and PsTPP(Pseudomonas sp. BCNU 106 trehalose-6-phosphate synthase/phosphatase). The two mRNA levels of trehalose-6-phosphate synthase/ phosphatase peaked at 12 hr after exposure to toluene, and thereafter were declined slightly These results support an important role of trehalose accumulation by expressions of PsTPS and PsTPP in toluene-tolerance of Pseudomonas sp. BCNU 106.

• Journal of Life Science
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• v.30 no.1
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• pp.88-95
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• 2020

Using a random arbitrarily primed polymerase chain reaction, messenger RNA expression levels were assessed after exposure to 10% (v/v) toluene for 8 hr in solvent-tolerant Pseudomonas sp. BCNU 106. Among the 100 up-expressed products, 50 complementary DNA fragments were confirmed to express repeatedly; these were cloned and then sequenced. Blast analysis revealed that toluene stimulated an adaptive increase in the gene expression level in association with transcriptions such as LysR family of transcriptional regulators and RNA polymerase factor sigma-32. The expression of catalase and Mn2+/Fe2+ transporter genes functionally associated with inorganic ion transport and metabolism increased, and the increased expression of type IV pilus assembly PilZ and multi-sensor signal transduction histidine kinase genes, functionally categorized into signal transduction and mechanisms, was also demonstrated under toluene stress. The gene expression level of beta-hexosaminidase in association with carbohydrate transport and metabolism increased, and those of DNA polymerase III subunit epsilon, DNA-3-methyladenine glycosylase II, DEAD/DEAH box helicase domain-containing protein, and ABC transporter also increased after exposure to toluene in DNA replication, recombination, and repair, and even in defense mechanism. In particular, the RNAs corresponding to the ABC transporter, Mn2+/Fe2+ transporter, and the β-hexosaminidase gene were confirmed to be markedly induced in the presence of 10% toluene. Thus, defense mechanism, cellular ion homeostasis, and biofilm formation were shown as essential for toluene tolerance in Pseudomonas sp. BCNU 106.

• Journal of Microbiology and Biotechnology
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• v.18 no.4
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• pp.663-669
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• 2008

The solvent-tolerant bacterium Enterobacter sp. VKGH12 is capable of utilizing n-butanol and contains an $NAD^+$-dependent n-butanol dehydrogenase (BDH). The BDH from n-butanol-grown Enterobacter sp. was purified from a cell-free extract (soluble fraction) to near homogeneity using a 3-step procedure. The BDH was purified 15.37-fold with a recovery of only 10.51, and the molecular mass estimated to be 38 kDa. The apparent Michaelis-Menten constant ($K_m$) for the BDH was found to be 4 mM with respect to n-butanol. The BDH also had a broad range of substrate specificity, including primary alcohols, secondary alcohols, and aromatic alcohols, and exhibited an optimal activity at pH 9.0 and $40^{\circ}C$. Among the metal ions studied, $Mg^{2+}$ and $Mn^{2+}$ had no effect, whereas $Cu^{2+},\;Zn^{2+}$, and $Fe^{2+}$ at 1 mM completely inhibited the BDH activity. The BDH activity was not inhibited by PMSF, suggesting that serine is not involved in the catalytic site. The known metal ion chelator EDTA had no effect on the BDH activity. Thus, in addition to its physiological significance, some features of the enzyme, such as its activity at an alkaline pH and broad range of substrate specificity, including primary and secondary alcohols, are attractive for application to the enzymatic conversion of alcohols.

• Biotechnology and Bioprocess Engineering:BBE
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• v.5 no.1
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• pp.53-56
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• 2000

A thermostable esterase from the hyper thermophilic archaeon Sulfolobus solfataricus was partially purified 590-fold with $16.2\%$ recovery. The partially purified esterase had a specific activity of $29.5\;{\mu}mol\;min^{-1}mg^{-1}$ when the enzyme activity was determined using p-nitrophenyl butyrate as a substrate. The apparent molecular weight was about 100 kDa, while the optimum temperature and pH for esterase were $75^{\circ}C$ and 8.0, respectively. The enzyme showed high thermal stability and solvent tolerance in comparison to its mesophilic counterpart. The enzyme also showed chiral resolution activity for (S)-ibuprofen, indicating that S. solfataricus esterase can be used for the production of commercially important chiral drugs.