• Natural Product Sciences
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• v.27 no.3
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• pp.208-215
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• 2021

𝛽-Patchoulene (𝛽-PAE) is a tricyclic sesquiterpene which performed many potential bioactivities and can be found in patchouli oil but in very low concentration. This study aimed to obtained 𝛽-PAE in high concentration by conversion of patchouli alcohol (PA) in patchouli oil under acid catalyzed reaction. Patchouli oil was fractinated by vacuum distillation at 96 kPa to get the fraction with the highest PA content. H₂SO₄ and ZnCl₂ were used respectively as homogeneous and heterogeneous acid catalysts in the conversion reaction of the selected fraction. Patchouli oil, the fractions and the products were analysed by using GC-MS and FTIR instruments. Moreover, the interaction of 𝛽-PAE to COX-2 protein was studied to understand the antiinflammation activity of 𝛽-PAE. The results showed that patchouli oil contains 25.3% of PA. The selected fraction which has the highest PA content (70.3%) was distilled at 151 - 152 ℃. The application of ZnCl₂ catalyst in conversion reaction did not succeed. In contrast, H₂SO₄ as a catalyst in acetic acid solvent succeeded in converting the overall fraction of PA to 𝛽-PAE. Furthermore, the molecular docking study of 𝛽-PAE against COX-2 enzyme showed van der Waals and alkyl-alkyl stacking interactions on ten amino acid residues.

• Korean Journal of Microbiology
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• v.26 no.3
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• pp.207-214
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• 1988

A cytosine deaminase from the cell-free extract of an isolate was examined after ethyl alcohol reactionation. The enzyme catalyzed the conversion of 5-fluorocytosine to 5-fluorouracil by the possession of specificity to the substrate. The optimum temperature and storage time on the stability of the enzyme were at below $50^{\circ}C$ and near 2 days in tris-HCl buffer. The maximum activity was also presented ar 9.0 in pH and $45^{\circ}C$ in temperature. The pHs and temperatures for the enzyme activity ranged from 8.5-9.5 and from 40-$50^{\circ}C$, respectively. the presence of $Ag^{+}, Hg^{2+}, Zn^{2+}$ in the reaction mixture resulted in the marked inhibition in the activity, but 1mM of $Fe^{3+}, K^{+}$, or $Na^{+}$ increased the enzyme activity. The enzyme preparation was vot affected by inhibitors used except N-ethylmaleimide of 1 and 10mM, and considerably activated by 1mM of pyrophosphate and 10mM of phosphate.

• Microbiology and Biotechnology Letters
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• v.47 no.1
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• pp.139-147
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• 2019

Glutamate decarboxylase catalyzes the conversion of glutamate to gamma-aminobutyric acid (GABA), contributing to pH homeostasis through proton consumption. The reaction is the first step toward the GABA shunt. To date, the enzymes involved in the glutamate metabolism of Photobacterium damselae subsp. piscicida have not been elucidated. In this study, an open reading frame of P. damselae subsp. piscicida, showing homology to the glutamate decarboxylase or putative pyridoxal-dependent aspartate 1-decarboxylase genes, was isolated and cloned into an expression vector to produce the recombinant enzyme. Preliminary gas chromatography-mass spectrometry characterization of the purified recombinant enzyme revealed that it catalyzed not only the decarboxylation of glutamate but also the transamination of GABA. This enzyme of P. damselae subsp. piscicida could be bifunctional, combining decarboxylase and transaminase activities in a single polypeptide chain.

• The Korean Journal of Food And Nutrition
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• v.6 no.3
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• pp.169-177
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• 1993

The conversion of glutamate by glutamine synthetase Is the endergonic reaction that demands ATP as its energy source. In order to supply efficiently ATP that is demanded in the conversion of glutamate to glutamine, the ATP- generating system by acetate kinase partially purified from Escherichia coli K-12 was coupled with glutamine synthetase partially purified 5. coli K-12 Pgln6. The optinum conditions of the coupled reaction were investigated. As the result, the highest conversion of glutamate to glutamine was shown In the reaction mixture containing 100mM glutamate, 100mM NHtCl, 50M acetyl phosphate, 5mM ADP, 40M MgCl2, 300mM potassium phosphate buffer (pH 7.5), 5mM MnCl2, Under this condition, the most effective concentrations of enzyme were 70unit/ml glutamine synthetase and 99unit/ml acetate kinase. Under the optinum conditions, 98% of 100mM glutamate was converted to glutamine within 6 hours.

• BMB Reports
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• v.28 no.6
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• pp.490-493
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• 1995

We investigated the effect of hydrogen peroxide-treated metallothionein on the hepatic xanthine oxidase activity in vitro. When the metallothionein was preincubated with 1 mM of hydrogen peroxide, the activity of xanthine oxidase and type conversion were elevated dose-dependently by the addition of metallothionein into the reaction mixture. While increasing the treatment of hydrogen peroxide to the $50{\mu}g$of metallothionein, the xanthine oxidase activity and type conversion ratio were remarkably elevated dose dependently compared to the control. When cadmium ion was added to the reaction mixture, the increasing pattern of the enzyme activity was similar to the effect of hydrogen peroxide-treated metallothionein. DTT or penicillamine restored the increasing activity and type conversion of xanthine oxidase by the cadmium ion to the control level.

• Journal of Environmental Health Sciences
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• v.31 no.4 s.85
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• pp.241-245
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• 2005

Laccase catalyzes the oxidation and polymerization of aromatic compounds in the presence of molecular oxygen. Studies were conducted to characterize the use of polyethylene glycol (PEG) as an additive to keep up the enzymatic stability. The enzymatic activities highly remained and bisphenol A (BPA) was rapidly converted in the presence of 5 mg/l of PEC. These effects were accomplished with PEG of molecular weight 3,350. A linear relationship was found between the quantity of BPA to be converted $(10-120\;{\mu}M)$ and the optimum dose of PEC required for greater than $95\%$ conversion. This result suggests that it is the interaction between the PEG and the reaction products. In the optimum dose of PEG, the aeration of reaction mixture neither enhanced the conversion of BPA nor retarded the inactivation of the enzyme.

• Bulletin of the Korean Chemical Society
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• v.21 no.6
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• pp.567-570
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• 2000

Bovine liver catalase was exposed to cysteine, as a natural inactivator metabolize, causing autoxidation-generating $H_2O_2$ continuously. The catalase species concentrations and activity measurement were done by spectrophotometry in phosphate buffer 10mM, pH 6.5, and 27 $^{\circ}C$. The activity of catalase decreased continuously due to the conversion of active ferricatalase species, E-Fe (III), to an inactive enzyme species, E-Fe (IV). This conversion is related to the slow production of $H_2O_2generated$ by autoxidation of cysteine. The free SH-group of cysteine has an essential role in production of $H_2O_2$ and hence inactivation of catalase. NADPH can protect catalase against inactivation due to the conversion of inactive form of E-Fe (IV) to ferricatalase species, E-Fe (III).

• KSBB Journal
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• v.15 no.3
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• pp.313-317
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• 2000

In this paper enantioselective production of levofloxacin by porcine liver esterase was investigated, To enhance the produc0-tivity various factors which affect the enzyme activity and the enantioselectivity were optimized, In terms of temperature and pH 45$^{\circ}C$ and 4.8 were found to be the best conditions for enzyme reaction. Addition of ofloxacin butyl ester the substrate at the concentration of 5 g/L was desirable to avoid the product inhibition and the activity of porcine liver esterase was maintained up to 72 hours.In addition to enhance the availability of substrate effect of solvent was also examined. It was found that the application of 5% (v/v) of acetone acetonitrile and dimethylsulfoxide did not increase the conversion of substrate and the presence of 5%(v/v) butanol inhibited the enzyme activity significantly.

• The Journal of Korean Medicine
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• v.17 no.2 s.32
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• pp.191-202
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• 1996

Cervus elaphus for herb-acupuncture solution(CEHAS) was tested for the effects of free radical generating enzyme and lipid peroxidation in rat's liver. In vitro, levels of lipid peroxide in tissues of liver were proportionally decreased to concentration of CEHAS. They were much more decreased. when lipid peroxidation was induced with ferrous iron $(Fe^{-2})$. Also, enzyme activities of xanthine oxidase were decreased. The ratio of type conversion of xanthine oxidase was lowered, too. But, here was not special changes on enzyme activities of aldehyde oxidase. These results suggest that CEHAS decrease the activities of free radical generating enzymes such as xanthine oxidase which form lipid peroxide.

• Korean Journal of Oriental Medicine
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• v.2 no.1
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• pp.192-204
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• 1996

Cervus elaphus for herb-acupuncture solution (CEHAS) was tested for the effects of free radical generating enzyme and lipid peroxidation in rat's kidney. In vitro, levels of lipid peroxide in tissues of kidney were proportionally decreased to concentration of extracts prepared from CEHAS. They were much more decreased, when lipid peroxidation was induced with ferrous iron (FeII). Also, enzyme activities of xinthine oxidase were decreased. The ratio of type conversion of xanthine oxidase was lowered, two. But, it was not seen changes on enzyme activities of aldehyde oxidase. These results suggest that CEHAS decrease the activities of free radical generating enzymes such as xanthine oxidase which form lipid peroxide.