• Proceedings of the Korea Environmental Mutagen Society Conference
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• 2003.10a
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• pp.182-182
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• 2003

• Proceedings of the Korea Environmental Mutagen Society Conference
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• 2003.10a
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• pp.188-188
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• 2003

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1978.04a
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• pp.98.2-98
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• 1978

호기성 발효에 있어서, 산소와 charge transfer complex를 형성할 수 있는 phenol 유도체인 guai-acol, vanillin, O-v-anillin 등과 catechol 유도체인 resorcine, adrenaline, dopamin 등이 산소와의 반응에 의하여 효과적인 산소공급 촉진제로서 이용될 수 있는가를 알아보기 위하여 합성배지중에서 나타내는 산소이동계수(KLQ)를 측정 비교하여 발효공학에의 응용가능성을 검토하였다.

• Proceedings of the PSK Conference
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• 2003.04a
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• pp.218.2-219
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• 2003

2-Hydroxymuconic semialdehyde dehydrogenase catalyzes the conversion of 2-hydroxymuconic semialdehyde (HMS) to an enol form of 4-oxalocrotonate which is a step in the catechol-meta cleavage pathway. A tomC gene encoding 2-HMS dehydrogenase of Burkholderia cepacia G4, a soil bacterium that can grow on toluene, cresol, phenol or tricholoro ethylene, is identified in between catechol 2,3-dioxygenase gene and HMS hydrolase gene, its sequence is analysed and the enzyme is characterised. (omitted)

• Proceedings of the Korean Society of Toxicology Conference
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• 2003.10b
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• pp.188-188
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• 2003

2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD), a prototype of halogenated aromatic hydrocarbons, is a persistent environmental contaminant and one of the most powerful tumor promoters. The molecular mechanism underlying induction of tumor promotion by TCDD has not been elucidated.(omitted)

• Korean Journal of Pharmacognosy
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• v.31 no.4
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• pp.426-429
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• 2000

Five compounds have been isolated from the rhizomes of Polygonum bistorta. On the basis of spectral evidences, these compounds were identified as catechol, 4- hydroxybenzaldehyde, umbelliferone, scopoletin and pyrogallol.

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.549-551
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• 2001

The heavy use of petroleum products in modern livings has brought ubiquitous environmental contaminants of aromatic compounds, which persist in aquatic and geo-environment without the substantial degradation. The persistence and accumulation of the aromatic compounds, which include xylene, phenol, toluene, phthalate, and so on are known to cause serious problems in our environments. Some of soil and aquatic microorganisms facilitate their growth by degrading aromatic compounds and utilizing degrading products as growth substrates, the biodegradation helps the reentry of carbons of aromatic compounds, preventing their accumulation in our environments. The metabolic studies on the degradation of aromatic compounds by microoganisms were extensively carried out along with their genetic studies. A Rhodococcus sp. EL-GT isolated in activated sludges has shown the excellent ability to grow on phenol as a sole carbon source. In the present study investigated a gene encoding phenol-degrading enzymes from a Rhodococcus sp. EL-GT.

• Korean Journal of Environmental Agriculture
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• v.17 no.3
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• pp.239-245
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• 1998

To investigate the formation of bound residue with soil organic materials by oxidative coupling, nitroaromatics and their reduced metabolites, the insecticide parathion and the herbicide asulam were incubated with oxidoreductase, laccase or horseradish peroxidase, in the presence or absence of humic monomers. Most of aminotoluenes and amino-nitrophenols were completely transformed while most of nitrotoluenes and nitrophenols remained unchanged by a lactase or horseradish peroxidase in the presence or absence of humic monomers. Amino-nitrotoluenes were not transformed without humic monomers, but the addition of various humic monomers caused a considerable difference in the transformation of amino-nitrotoluenes by a lactase or horseradish peroxidase. Amino-nitrotoluenes were most transformed in the presence of catechol, syringaldehyde and protocatechuic acid. The insecticide parathion with nitro group and its metabolite were not mostly transformed in the presence or absence of humic monomers. The herbicide asulam with amino group remained unchanged without humic monomers as well, but the stimulating effect on the transformation of asulam was caused by the addition of catechol, syringaldehyde, protocatechuic acid or caffeic acid with a lactase.

• Journal of Microbiology and Biotechnology
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• v.28 no.9
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• pp.1447-1456
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• 2018

The amylosucrase encoding gene from Deinococcus geothermalis DSM 11300 (DgAS) was codon-optimized and expressed in Escherichia coli. The enzyme was employed for biosynthesis of three different dihydroxybenzene glucosides using sucrose as the source of glucose moiety. The reaction parameters, including temperature, pH, and donor (sucrose) and acceptor substrate concentrations, were optimized to increase the production yield. This study demonstrates the highest ever reported molar yield of hydroquinone glucosides 325.6 mM (88.6 g/l), resorcinol glucosides 130.2 mM (35.4 g/l) and catechol glucosides 284.4 mM (77.4 g/l) when 400 mM hydroquinone, 200 mM resorcinol and 300 mM catechol, respectively, were used as an acceptor substrate. Furthermore, the use of commercially available amyloglucosidase at the end of the transglycosylation reaction minimized the gluco-oligosaccharides, thereby enhancing the target productivity of mono-glucosides. Moreover, the immobilized DgAS on Amicogen LKZ118 beads led to a 278.4 mM (75.8 g/l), 108.8 mM (29.6 g/l) and 211.2 mM (57.5 g/l) final concentration of mono-glycosylated product of hydroquinone, catechol and resorcinol at 35 cycles, respectively, when the same substrate concentration was used as mentioned above. The percent yield of the total glycosides of hydroquinone and catechol varied from 85% to 90% during 35 cycles of reactions in an immobilized system, however, in case of resorcinol the yield was in between 65% to 70%. The immobilized DgAS enhanced the efficiency of the glycosylation reaction and is therefore considered effective for industrial application.

• Food Science and Preservation
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• v.12 no.5
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• pp.489-495
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• 2005

Polyphenol oxidase (PPO) from Burdock (Arctium lappa L.) was purified and characterized. Purification of polyphenol oxidase was achieved by ammonium sulfate precipitation, Phenyl-sepharose CL-4B hydrophobic chromatography and Sephadex G-100 gel filtration chromatography. The molecular mass of the purified PPO was estimated to be 30 kDa by SDS polyacrylamide gel electrophoresis. In a substrate specificity, maximum activity was achieved with chlorogenic acid, followed by catechol and catechin. Whereas, there was low activity with hydroquinic acid, resorcinol or tyrosine. The optimum pH and temperature for enzyme activity were 7.0 and 35$\circC$ with catechol, respectively. The enzyme was most stable at pH 7.0 while unstable at acidic and alkaline pH. The enzyme was stable when heated to 40$\circC$. But heating at 50$\circC$ for more than 30 min caused 50% loss of activity. Ascorbic acid, L-cystein and $Cu^{2+}$ inhibited the activity of pholyphenol oxidase.