• Title, Summary, Keyword: peroxidase

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Extraction Process and Stability Characteristics of Soybean Peroxidase (Soybean peroxidase의 추출공정 및 안정성 특성)

  • 서경림;이은규
    • KSBB Journal
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    • v.13 no.5
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    • pp.599-605
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    • 1998
  • Soybean peroxidase was extracted from soybean hulls and purified by ammonium sulfate precipitations (25% and 75% saturation), pl fractionation, and anionic exchange and gel filtration chromatographies (DEAE-Sephadex A-50 and Superose 12). Modlecular weight and pl value were estimated to be ca. 45 kD and 4.2, respectively. Purified soybean peroxidase had an RZ value of 0.43. Compared with horseradish peroxidase, it showed superior thermal and pH stability. Assuming the first-order kinetics, the thermal deactivation rate constant of soybean peroxidase at 80$^{\circ}C$ was about 8 times lower than that of horseradish peroxidase. Deactivation energy was calculated to be 69.3 kcal/mol. Soybean peroxidase showed about 10% higher H2O2 degradation capacity than horseradish peroxidase. Exploiting these advantages, the soybean peroxidase purified from the domestic soybean hull is expected to replace horseradish peroxidase in various applications.

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Enzymatic Determination of Glucose Using Soybean Sprouts Peroxidase. (콩나물 Peroxidase를 이용한 포도당의 효소적 분석)

  • 이민경
    • Journal of Life Science
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    • v.8 no.4
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    • pp.416-420
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    • 1998
  • Soybean sprouts peroxidase can be used for enzymatic determination of glucose. Peroxidase from soybean sprouts was purified by ammonium sulfate precipitation and DEAE Sephacel column chromatography. The glucose could be quantitatively assayed by using glucose oxidase and soybean sprouts peroxidase. The optimum pH and temperature for glucose assay were of pH 5.5 and $40^{\circ}C$, respectively. The relationship between absorbance and glucose concentration was linear. And also the relationship between absorbance and reaction time was linear. The reducing agents such as L-cysteine, dithiothreitol inhibited the glucose assay by glucose oxidase and soybean sprouts peroxidase.

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Distinct functional roles of peroxiredoxin isozymes and glutathione peroxidase from fission yeast, Schizosaccharomyces pombe

  • Kim, Ji-Sun;Bang, Mi-Ae;Lee, Song-Mi;Chae, Ho-Zoon;Kim, Kang-Hwa
    • BMB Reports
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    • v.43 no.3
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    • pp.170-175
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    • 2010
  • Chaperone;Glutathione peroxidase;Peroxiredoxin;Schizosaccharomyces pombe;Thioredoxin peroxidase;To investigate the differences in the functional roles of peroxiredoxins (Prxs) and glutathione peroxidase (GPx) of Schizosaccharomyces pombe, we examined the peroxidase and molecular chaperone properties of the recombinant proteins. TPx (thioredoxin peroxidase) exhibited a capacity for peroxide reduction with the thioredoxin system. GPx also showed thioreoxin-dependent peroxidase activity rather than GPx activity. The peroxidase activity of BCP (bacterioferritin comigratory protein) was similar to that of TPx. However, peroxidase activity was not observed for PMP20 (peroxisomal membrane protein 20). TPx, PMP20, and GPx inhibited thermal aggregation of citrate synthase at 43$^{\circ}C$, but BCP failed to inhibit the aggregation. The chaperone activities of PMP20 and GPx were weaker than that of TPx. The peroxidase and chaperone properties of TPx, BCP, and GPx of the fission yeast are similar to those of Saccharomyces cerevisiae. The fission yeast PMP20 without thioredoxin-dependent peroxidase activity may act as a molecular chaperone.

Peroxidase Activity in Leaf Tissue of Rice Infected by Pyricularia oryzae (도열병에 감염된 벼의 엽조직에서 Peroxidase의 활성)

  • Park Won Mok;Lee Yong Se;Park Sang Ho
    • Korean Journal Plant Pathology
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    • v.1 no.3
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    • pp.178-183
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    • 1985
  • The present researches were carried out to investigate the peroxidase activity in association with the reactions of the 4 cultivars of rice plant, Nagdong, Jinheung, Nongbaek and Taebaek to Pyricularia oryzae race KJ-I0l and KJ-301. Although the peroxidase activity was increased during the growth of the rice seedlings, the significant difference in the activity was not found among 4 cultivars. After inoculation of the fungus, the peroxidase activity was enhanced in diseased leaves, being considerably higher in the compatible than in the incompatible cultivars. The isozyme bands of peroxidases observed in mycelium of rice blast fungus were not found in the diseased leaves on the gel electrophoresis. The peroxidase activity was not affected by the increased application of nitrogenous fertilizer.

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Studies on Growth and Differentiation of Suspension-Cultured Carrot Cells I. Alterations in Peroxidase Activity, Polyamine Content and Ethylene Production during Somatic Embryogenesis (당근 현탁 배양세포의 생장과 분화에 관한 연구 I. 배형성 과정에서 Peroxidase 활성, Polyamine 함량 및 Ethylene 성성의 변화)

  • 김응식
    • Journal of Plant Biology
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    • v.33 no.4
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    • pp.259-269
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    • 1990
  • Changes of peroxidase activity, polyamine content and ethylene production during somatic embryogenesis in suspension-cultured carrot (Daucus carota L.) cells were investigated. As compared with nonembyrogenic cells and their medium, embryogenic cells and their medium were characterized by higher levels of peroxidase at all times of culture period. Peroxidase in embryogenic cells showed higher oxidation activity of IAA than in nonembryogenic cells at the torpedo stage, but the IAA oxidation activity of peroxidase released into embryogenic medium was lower than that of peroxidase released into nonembryogenic medium. Peroxidase patterns of embryogenic and nonembryogenic cells showed three cathodic bands, and one anodic band, while peroxidase patterns released into embryogenic and nonembryogenic media did not show any anodic bands and the isoelectric points of cathodic peroxidase were pH 7.7, 7.5 and 6.6. Compared with nonembryogenic cells, polyamine content in embryogenic cells was increased by 15% at the torpedo stage, but polyamine ratio was constant, and ethylene production was extremely low at all times of culture period. Therefore, it is suggested that the peroxidase in embryogenic cells is correlated with embryogenesis by regulating hormone ratios through IAA oxidation, while the peroxidase isozyme patterns may be used as a biochemical marker of embryogenesis. The increase of polyamine content and the decrease of ethylene production suggest an interaction between polyamine and ethlyene during embryogenesis.

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Existence of "25 kDa Thiol Peroxidase" in Retina: Evidence for An Antioxidative Role

  • Cha, Mee-Kyung;Kim, Il-Han
    • BMB Reports
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    • v.31 no.4
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    • pp.409-412
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    • 1998
  • We isolated and sequenced a human retina cDNA fragment that encodes 25 kDa thiol peroxidase. A search of a databank showed that the 25 kDa thiol peroxidase from retina is the same type of thiol peroxidase which exists in human brain and red blood cells. This type of tbiol peroxidase was distributed in all of the tested tissues including retina. This result suggests a physiological role for the 25 kDa thiol peroxidase as an important antioxidant.

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Peroxidase Activity of Cytochrome c

  • Kim, Nam-Hoon;Jeong, Moon-Sik;Choi, Soo-Young;Kang, Jung-Hoon
    • Bulletin of the Korean Chemical Society
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    • v.25 no.12
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    • pp.1889-1892
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    • 2004
  • The peroxidase activity of cytochrome c was studied by using a chromogen, 2,2'-azinobis-(2-ethylbenzthiazoline-6-sulfonate) (ABTS). Initial rate of ABTS oxidation formation was linear with respect to the concentration of cytochrome c between 2.5-10 ${\mu}$M and $H_2O_2$ between 0.1-0.5 mM. The optimal pH for the peroxidase activity of cytochrome c was 7.0-8.5. The peroxidase activity retained about 40% of the maximum activity when exposed at 60 $^{\circ}C$. for 10 min. The peroxidase activity showed a typical Michaelis-Menten kinetics for $H_2O_2$ which Km value was 29.6 mM. Radical scavengers inhibited the peroxidase activity of cytochrome c. The peroxidase activity was significantly inhibited by the low concentration of iron chelator, deferoxamine. The results suggested that the peroxidase activity was associated with iron in the heme of cytochrome c.

Rapid Screening Method of Peroxidase by Colorimetric Assay and Screening of 2, 4-DCP Degradable Strains (발색법에 의한 Peroxidase의 신속한 스크리닝법과 2, 4-DCP 분해균주의 스크리닝)

  • Ryu, Kang;Lee, Eun-Kyu
    • KSBB Journal
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    • v.23 no.6
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    • pp.484-488
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    • 2008
  • Chlorinated phenols are widely used by the chemical industry as intermediate products in synthesis and previously were frequently applied to various industry fields. Peroxidases catalyze the peroxide-dependent oxidation of a range of inorganic and organic compounds. Peroxidase was shown to mineralize a variety of recalcitrant aromatic compounds and to oxidize a number of polycyclic aromatic and phenolic compounds. Among monomeric phenolic and nonphenolic compounds, peroxidase is known to oxidize its compounds. In this study, a colorimetric assay was developed to quantitatively evaluate the peroxidase activity for rapid screening. Color products of different intensity were developed proportionally to the peroxidase activity on agar plate and 96-well plate. This method correlates well with the RP-HPLC result. Using this screening method, 12 colonies of strain was screened which survived at high concentration of 2,4-DCP (1000 ppm) and with peroxidase activity for the $7^{th}$ round screening step on agar plate. These strains were utilized 2,4-DCP as a sole carbon source and produced peroxidase. After the screening test, four of the bacteria have significant better effect of COD removal on dye waste-water. COD removal of these was from 44% to 61%, respectively.

Diversity in Activities of Peroxidase and Polyphenoloxidase in the Akagare or Helminthosporium-infected Rice Leaves (적고(赤枯) 및 호마엽고(胡麻葉枯) 수도엽중(水稻葉中) Peroxidase와 Polyphenoloxidase의 활성(活性))

  • Park, Hoon;Chun, Jae Kun
    • 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.

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Influences of Peroxidase on Lysozyme Activity (Peroxidase가 Lysozyme 활성에 미치는 영향)

  • Lee, Sang-Goo;Kim, Hyung-Il;Kho, Hong-Seop
    • 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.