• Korean Journal of Soil Science and Fertilizer
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• v.6 no.1
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• pp.27-28
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• 1973

The activities of peroxidase and polyphenoloxidase were investigated in the rice leaves(the upper halves) diseased with Akagare or Helminthosporium oryzae. The activity of polyphenoloxidase was slightly lower than that of peroxidase in the healthy leaves but it increased 56% in the diseased leaves while peroxidase decreased 35%. It was expected that polyphenoloxidase is dominant in the oxidation of polyphenols, and hydrogen peroxide may accumulate to harmful level due to the decrease of peroxidase activity resulting in non-enzymatic oxidation of polyphenols in the diseased leaves.

• Journal of Industrial Technology
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• v.21 no.A
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• pp.343-349
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• 2001

This study characterizes the growth of white rot fungi Phanerochaete chrysosporium IFO 31249) and lignin peroxidase(LiP) activity in different submerged culture media. P. chrysosporium was grown in the form of pellet of various sizes from a spore inoculum under shaking liquid culture condition. While the growth of mycelia was higher under the nitrogen-sufficient culture than under the nitrogen-limited culture, ligninase activity was relatively lower. The lignin peroxidase appeared in nitrogen-limited culture and was suppressed by excess nitrogen. High level(40U/l) of lignin peroxidase activity was obtained in the growth medium containing 1.5mM veratryl alcohol, a secondary metabolite of P. chrysosporium. Lignin peroxidase production was not observed under conditions of nitrogen sufficiency or in balanced media, suggesting that control parameters could increase the activity by manipulating the secondary metabolism.

• Journal of Pharmaceutical Investigation
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• v.29 no.4
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• pp.287-293
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• 1999

Transport study of horseradish peroxidase and transferrin-horseradish peroxidase conjugate was performed using an in vitro Caco-2 cell cultured monolayer grown on a polycarbonate membrane of $Transwell^{\circledR}$, Horseradish peroxidase was not transported across Caco-2 cell monolayer. Transferrin-horseradish peroxidase conjugate was transported through Caco-2 cell monolayer. The apparent membrane permeability coefficient $(P_{app})$ of transferrin horseradish peroxidase conjugate was $6.54{\times}10^{-7}\;cm/sec$. The $P_{app}$ value of transferrin-horseradish peroxidase conjugate across Caco-2 cell monolayer was increased to $11.9{\times}10^{-7}\;cm/sec$ in the presence of $50\;{mu}g/ml$ brefeldin-A. These results suggest the transferrin receptor mediated transcytosis of transferrin-horseradish peroxidase conjugate across Caco-2 cell monolayer.

• Journal of Environmental Health Sciences
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• v.23 no.4
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• pp.121-126
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• 1997

Peroxidase as one of the organic enzyme catalyst is useful for the oxidation treatment of various aromatic compounds such as phenols. The peroxidase content of Oenanthe javanica was 24.85 unit/g-fw in leaf, 5.74 unit/g-fw in stem, and 34.69 unit/g-fw in root respectively. The crude peroxidase extracted from Oenanthe javanka can be kept under low temperature (-70$\circ$C) condition for 6 months with the maximum 1% activity reduction. The optimum conditions of removal for 100 ppm phenol was pH 6, hydrogen peroxide 3.5 mM, peroxidase activity 8 unit/ml, temperature 20$\circ$C respectively. In the wide range of concentration from 50 ppm to 750 ppm phenol reveals average 54% removal rate under the same peroxidase activity (8 unit/ml) and different amount of hydrogen peroxide proportional to phenol concentration. Especially at the concentration of 100 ppm the maximum phenol removal rate was 72%.

• Journal of Oral Medicine and Pain
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• v.33 no.1
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• pp.1-8
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• 2008

It is well known that many antimicrobial proteins in saliva interact with each other. The purpose of the present study was to investigate the interactions of lysozyme with peroxidase in the aspects of enzymatic activity in vitro. The interactions of lysozyme with peroxidase were examined by incubating hen egg-white lysozyme(HEWL) with bovine lactoperoxidase(bLP). The influence of peroxidase system on lysozyme was examined by subsequent addition of potassium thiocyanate and hydrogen peroxide. Lysozyme activity was determined by turbidity measurement of a Micrococcus lysodeikticus substrate suspension. Peroxidase activity was determined with an NbsSCN assay. The Wilcoxon signed rank test was used to analyze the changes of enzymatic activities compared with their controls. bLP at physiological concentrations enhanced the enzymatic activity of HEWL(P < 0.05) and its effect was dependent on the concentration of peroxidase. However, HEWL did not affect the enzymatic activity of bLP. Thiocyanate did not affect the enzymatic activity of HEWL, either. The addition of potassium thiocyanate and hydrogen peroxide did not lead to additional enhancement of the enzymatic activity of HEWL. The changes of hydrogen peroxide concentration in the peroxidase system did not affect the enzymatic activity of HEWL. Collectively, despite an in vitro nature of our study, the results of the present study provide valuable information on the interactions of lysozyme and peroxidase in the aspects of enzymatic activity in oral health care products and possibly in the oral cavity.

• International Journal of Industrial Entomology and Biomaterials
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• v.12 no.1
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• pp.21-28
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• 2006

Peroxidase activity was measured in brown leaf spot pathogen (Myrothecium roridum) inoculated potted mulberry (Morus alba) during pre-symptomatic to various symptom development stages and compared with corresponding healthy leaf tissues. The enzyme showed a pH optimum of 7.0 and the activity was linearly increased up to 15 min of incubation. The peroxidase had a broad substrate specificity and the rates of oxidation were in the rank of pyrogallol> guaiacol> ascorbate at pH 7.0. Catechol at 10 mM inhibited 89% of guaiacol-peroxidase and 76% pyrogallol-peroxidase activities, indicated higher non-specific peroxidation in pyrogallol dependent assay system in mulberry than guaiacol. The optimum requirement for the guaiacol dependent assay was 0.2 ml (${\approx}40-60{\mu}g$ equivalent of protein) of crude enzyme source. Excepting the 8th leaf from the apex, the peroxidase activity did not vary appreciably in different leaf positions. In pre-symptomatic phases, an initial (1 to 5 min) rise of peroxidase activity was noticed in inoculated leaves, and then maintained a plateau up to 300 min. In contrary, non-infected tissue showed a slightly increased trend of enzyme level up to 420 min. In infected tissue, a sharp transient increase (3.1 fold) of peroxidase activity appeared between 300 - 420 min post infections. Afterwards, significantly different but steady maintenance of enzyme levels were observed in two treatments. On the other hand, during symptom development, a sharp increase in peroxidase activity was noticed up to 4th grade of lesion appearance (25.1 % to 50% of leaf area infection), and then declined slightly. However, in non-infected but same age healthy leaves, such huge fluctuations of enzyme level did not apparent. A high positive correlation $(R^2=0.92)$ between peroxidase activity and leaf spot development grades was also marked. The result implies that pre-symptomatic burst (between 1 - 5 and 300 - 420 min) and subsequent increased trend of guaiacol peroxidase activity may require for the symptomatic manifestation of Myrothecium leaf spot in mulberry.

• KSBB Journal
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• v.15 no.4
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• pp.342-345
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• 2000

A novel pre-purification method was developed for producing peroxidase to guarantee high purity and yield from plant cell cultures in large-scale process. This method was a simple and efficient procedure for the isolation and pre-purification of peroxidase from the biomass consisting of active clay treatment followed by cationic exchange chromatography. The use of active clay in the pre-purification process allows for rapid and efficient separation of peroxidase from interfering compounds and dramatically increases yield and purity of crude peroxidase for purification steps compared to alternative processes. This pre-purification process serves to minimize the buffer usage size and complexity of the HPLC operations for peroxidase purification. This process is readily scalable to a pilot plant and eventually to a production environment where mass production of material are expected to be produced.

• Korean Journal of Microbiology
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• v.39 no.3
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• pp.201-205
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• 2003

Laccase, lignin- and manganese peroxidase are implicated in the lignin degradation. The nucleotide sequences of four copper-binding domains in fungal laccases, and heme-binding domains of lignin- and manganese peroxidases are well conserved, and therefore these short fragments can be used for the PCR for the gene amplification. We synthesized several PCR primers according to their sequences, and run PCR to amplifiy the lignin degrading genes of Trametes versicolor isolated in Korea. PCR products were cloned with pGEM-T vector in order to determine their nucleotide sequences. A laccase fragment (1.3 kb) showed 65-97％ homologies, lignin peroxidase fragment (185 bp) showed 80-95％ homologies, and manganese peroxidase fragment (443 bp) showed 61-83％ homologies when compared with other white-rot fungal enzymes.

• Korean Journal of Environmental Biology
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• v.29 no.4
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• pp.258-264
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• 2011

Glutathione (GSH) has important roles in cellular defense against oxidative stress, 1) direct scavenging of reactive oxygen species (ROS), and 2) coenzyme of ROS scavenging enzyme like glutathione peroxidases (GPx). GSH peroxidase reduces free hydrogen peroxide to water using 2GSH. $N$-acetyl-L-cysteine (NAC), one of the antioxidants, is used as a precursor for intracellular GSH. In this study, relation of GSH, NAC, and GSH peroxidase was investigated through transcriptional expression of $GPX1$ and $GPX2$, which are GSH peroxidase encoding genes, in yeast cells treated with 0 mM to 20 mM of NAC or in combination with 100 Gy gamma-rays. The transcriptional expression of $GPX1$ and $GPX2$ was induced by NAC and 100 Gy gamma-rays. The gene expression of both GSH peroxidases was decreased with increasing concentrations of NAC in irradiated yeast cells. These results suggest that elevation of intracellular GSH by NAC and oxidative stress and ROS generated from gamma-rays induces expression of GSH peroxidase genes, and that NAC can protect the yeast cells against ROS generated from gamma-rays through direct scavenging of ROS and transcriptional activation of GSH peroxidase.

• Korean Journal of Weed Science
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• v.10 no.3
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• pp.233-239
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• 1990

The effect of alachlor treatment on peroxidase synthesis in oat root tips was studied. Alachlor caused increase in the amount of soluble peroxidase in oat root tips, peroxidase activity increase as the rate of alachlor application increased, Alachlor treatment of oats with $1{\times}10^{-6}M$, peroxidase activity increased 0.20 unit higher than that of nontreatment. After 12hr, 65mM of peroxide treatment of oats inhibited 16% root growth, and 130 mM peroxide treatment caused 59% inhibition. With PAGE of peroxidase extracted from normal root tips, PAGE give 4 species($P_2$, $P_3$, $P_4$, and $P_5$ band) of peroxidase. Alachlor significantly activated isoperoxidase. Three isoperoxidase($P_1$, $P_6$, and $P_7$) are synthesized at a increased concentration of alachlor, SDS-PAGE analysis of proteins extracted from oat root tips showed that they were made up of subunits blow 100 kD polypeptide.