• Journal of Oral Medicine and Pain
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• v.43 no.1
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• pp.1-7
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• 2018

Purpose: The purpose of the study was to investigate the influences of hyaluronic acid on the candidacidal activities of lysozyme, the peroxidase system, and the glucose oxidase-mediated peroxidase (GO-PO) system at different concentrations of antimicrobial enzymes. Methods: Hyaluronic acid was used at a final concentration of 0.5 mg/mL. Hen egg-white lysozyme (HEWL) was used at concentrations ranging from 10 to $100{\mu}g/mL$. The peroxidase system included bovine lactoperoxidase (bLPO), potassium thiocyanate (KSCN, 1 mM), and hydrogen peroxide ($100{\mu}M$). The GO-PO system included bLPO, KSCN (1 mM), glucose oxidase (10 units/mL), and glucose ($30{\mu}g/mL$). The final concentration of bLPO in the peroxidase and GO-PO systems ranged from 12.5 to $100{\mu}g/mL$. Candida albicans strains ATCC 10231, 11006, and 18804 were utilized. Candidacidal activities of antimicrobials and the influence of hyaluronic acid on their candidacidal activities were determined based on colony forming units. Results: Candidacidal activities of the peroxidase and GO-PO systems increased with increasing concentrations of bLPO. This tendency was the same in the presence or absence of hyaluronic acid. Candidacidal activity of HEWL was not significantly concentration-dependent. Candidacidal activities of the GO-PO system were higher than those of the corresponding peroxidase system. Candidacidal activity was inhibited in the presence of hyaluronic acid in the following order: HEWL, the peroxidase system, and the GO-PO system. Conclusions: Hyaluronic acid inhibited the candidacidal activities of HEWL, the peroxidase system, and the GO-PO system. The GO-PO system exhibited better candidacidal activity than HEWL and the peroxidase system both in the presence and absence of hyaluronic acid.

• Microbiology and Biotechnology Letters
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• v.19 no.5
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• pp.470-476
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• 1991

The distribution of peroxidase activity in 9 kinds of cruciferous plants was investigated. Among the plants examined, peroxidase activity was found to be high levels in roots of Chinese cabbage. One kind of peroxidase was purified approximately 56-fold from crude extracts of Chinese cabbage roots. The molecular weight of the enzyme was 50, 000 and consisted oif a single polypeptide chain, as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and Sephadex G-150 gel column chromatography. The enzyme showed optimum activity at pH 7.0 and $50^{\circ}C$. Phenol and phenol derivatives serves as substrates of the enzyme and Km value for $H_2O_2$ was 1.6 mM toward pyrogallol. The enzyme showed a Soret band at 406 nm and this result indicate that the enzyme contained heme as a prosthetic group. The immunochemical and electrophoretic properties of purified peroxidase from Chinese cabbage were very similar to horseradish peroxidase.

• Biotechnology and Bioprocess Engineering:BBE
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• v.1 no.1
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• pp.26-31
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• 1996

Since biosynthesis of lignin peroxidase from Phanerochaete chrysosporium was known to be sensitive to shear, it is interesting to understand the effects of the shear sensitivity for the overproduction of lignin peroxidase. In stirred-tank fermentor, the shear-sensitivity in lignin peroxidase biosynthesis was quantified by using Kolmogorov length scale. It was found that agitation at 80$\mu$m Kolmogorov length scale is advantageous for the production of lignin peroxidase from P. chrysosporium. To overcome the shear sensitivity in lignin peroxidase biosynthesis caused by the agitation,P. chrysosporium was immobilized on various solid carriers. The nylon-immobilized P. chrysosporium was chosen in the present study as a way to overcome the shear sensitivity at the ranges of above 50$\mu$m Kolmogorov length scale. The adhesion force between immobilized cell and carrier can be predicted by thermodynamic approach and used as a criteria to select an adequate carrier materials for immobilization.

• Proceedings of the Ginseng society Conference
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• 2004.12a
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• pp.48-49
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• 2004

A peroxidase[E.C.1.11.1.7] is very important enzymes,e.g., as preventive antioxidants. The function is connected with growth and specialization of plant. It makes from the peroxidase and other product to save itself When a plant have been under stress of environment. A class III peroxidase cDNA was isolated from the flower bud of Panax ginseng C.A. Meyer and named PgPrx3. The PgPrx3 is an ORF(open reading frame) of 1,065 bp and a amino acid of 355 residue. Used BioEdit software to compare the PgPrx3 amino acid sequence with other plants which have already known a result of Identity was Spinacia oleracea(70%), vigna angularis(71%), Nicotiana tabacum(69%) and Linum usitatissimym(65%). The peroxidase of Vigna angularis has high homology relationship with ginseng. for that reason, the PgPx3 is a member of class III peroxidase.

• Journal of Ginseng Research
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• v.17 no.1
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• pp.29-34
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• 1993

This study was undertaken to investigate the effect of red ginseng extract (5.5 mg/mouse ip) on the activities of superoxide dismutase (SOD), peroxidase and catalase in the liver of the gamma ray irradiated male mice. The experimental groups consisted of control, red ginseng extract injection group, irradiation (8 $Gy^{60}$Co) group and red ginseng extract injection after irradiation group. in red ginseng extract injection group, SOD, peroxidase and catalase activities were similar to that in the control group. In irradiation group SOD, peroxidase and catalase activities increased progressively until the 2nd day after the treatment and then decreased thereafter, whereas red ginseng extract injection after irradiation group recovered more rapidly than irradiation group. The above results suggested that red ginseng extract injection after irradiation group have the recovery effects on the activities of SOD, peroxidase and catalase after radiation injury in the liver of male mice.

• Archives of Pharmacal Research
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• v.8 no.4
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• pp.197-203
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• 1985

It was attempted to observe the effect of garlic on the hepatic glutathione s-transferase and glutathione peroxidase activity in this study. Glutathione s-transferase (EC 2.5.1.18) are thought to play a physiological role in initiating the detoxication of potential alkylating agents, inclnding pharmacologically active compounds. Glutathione peroxidase (EC 1. 11. 1. 9) might play an important role in the protection of cellular structures against oxidative challenge. The activities of glutathione s-transferase and glutathione peroxidase in rat liver were increased by the treatment of garlic juice. Allicin fraction, heat-treated allicin fraction and garlic butanol fraction markedly inhibited glutathione s-transferase activity in vitro, whereas glutathione peroxidase activity was significantly increased in heat-treated allicin fraction and garlic butanol fraction.

• The Korean Journal of Ecology
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• v.20 no.5
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• pp.315-321
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• 1997

Peroxidase activities and isozyme patte군 of the pine needles (Pinus densiflora) were examined and compared in the coastal regions of Anmyum-Do(Choongnam, Taean-Gun) and inland regions of Shinchang-Myun(Choongnam, Asan-City). The pine needle peroxidase from Anmyum-Do showed approximately three times higher specfic activity than Shinchang pine needle peroxidase. The pine needle extracts of Anmyun-Do and Shinchang contained three anionic isoperoxidases, named A1, A2 and A3, when subjected to starch gel electrophoresis at pH 7.0. Cjationic isoperoxidases could not be found in both extracts., However, there existed unique isoperoxidase An only from the extracts of Anmyun-Do pine needles under the salinary environment. Moreover, the specific activities of catalase and glucose-6-phosphate dehydrogenase from Anmyun-Do, known for the inducible enzymes under the stress condition, were about 1.8 times higher than those of Shinchang pine needles. However, the specific activities of other enzymes did not show great differences between the two regions. Considering the above results of the higher specific activity of peroxidase and the unique expression of isoperoxidase An, pine needle peroxidase might involve in the defence mechanism against the salinary stress of Anmyun-Do.

• Applied Biological Chemistry
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• v.22 no.1
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• pp.24-27
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• 1979

A study was carried out about the effect of free fatty acids and lecithin on the thermal inactivation of horseradish peroxidase. In presence of lecithin peroxidase was inactivated very rapidly at $70^{\circ}C$ and pH 7.0, and showed also a rapid inactivation curve at $0^{\circ}C$ and pH 4.0. Linoleic acid was more effective in an $O_2-stream$ than in a $N_2-stream$, but oleic acid showed a similar tendency in the presence of $O_2-and\;N_2$ stream. From the results of the experiment we suggested that the opening of the heme crevis of peroxidase in the presence of lecithin and the produced lipidperoxide from linoleic acid may accelerate the thermal inactivation of horseradish peroxidase respectively.

• Clean Technology
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• v.23 no.4
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• pp.408-412
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• 2017

Pigment red 53:1 is a dye used in various products as a component of the inks, suspected of being carcinogenic. Thus, the environmental and occupational issues related to it are important. The enzyme-based approach with reusability has advantages to consume less energy and generate less harsh side- products compared to the conventional strategies including separations, microbe, and electrochemical treatment. The degradation of Pigment red 53:1 by the lignin peroxidase immobilized on the surface of magnetic particles has been studied. The immobilization of the peroxidase was conducted on magnetic particle surface with the treatment of polyethyleneimine, glutaraldehyde, and the peroxidase, in sequence. The immobilization was confirmed using X-ray photon spectroscopy. The absorbance peak of the pigment was monitored at 495 nm of UV/Vis spectrum with respect to time to calculate the catalytic activities of the pigment for the immobilized lignin peroxidase. For the comparison, the absorbance of the lignin peroxidase free in solution was also monitored. The catalytic rate constant values for the free lignin peroxidases and the immobilized those were 0.51 and $0.34min^{-1}$, respectively. The reusable activity for the immobilized lignin peroxidase was kept to 92% after 10 cycles. The stabilities for heat and storage were also investigated for both cases.

• BMB Reports
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• v.31 no.6
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• pp.572-577
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• 1998

A soluble protein from Saccharomyces cerevisiae provides protection against a thiol-containing oxidation system but not against an oxidation system without thiol. This 25-kDa protein acts as a peroxidase but requires the NADPH-dependent thioredoxin system or a thiol-containing intermediate, and was thus named thioredoxin peroxidase. The protective role of thioredoxin peroxidase against ionizing radiation, which generates reactive oxygen species harmful tocellular function, was investigated in wild-type and mutant yeast strains in which the tsa gene encoding thioredoxin peroxidase was disrupted by homologous recombination. Upon exposure to ionizing radiation, there was a distinct difference between these two strains in regard to viability and the level of protein carbonyl content, which is the indicative marker of oxidative damage to protein. Activities of other antioxidant enzymes, such as catalase, superoxide dismutase, glucose-6-phosphate dehydrogenase, and glutathione reductase were increased at 200-600 Gy of irradiation in wild-type cells. However, the activities of antioxidant enzymes were not significantly changed by ionizing radiation in thioredoxin peroxidase-deficient mutant cells. These results suggest that thioredoxin peroxidase acts as an antioxidant enzyme in cellular defense against ionizing radiation through the removal of reactive oxygen species as well as in the protection of antioxidant enzymes.