• 한국식품영양학회지
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• 제15권2호
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• pp.158-164
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• 2002

본 실험은 벌꿀이 항균활성에 미치는 영향을 규명하기 위해 국내산 벌꿀인 밤꿀, 잡화, 아카시아, 재래종 벌꿀과 외국산 벌꿀인 마누카, 클로버, 캐놀라 벌꿀 그리고 인공벌꿀을 각각 12.5%, 25.0%, 50%의 희석액으로 조제하여 catalase무첨가 또는 첨가한 경우에 있어서 벌꿀의 Staphylococcus aureus에 대한 항균활성을 agar well diffusion assay로 비교한 바 다음과 같은 결과를 얻었다. Catalase 무첨가의 경우 12.5%희석한 벌꿀은 마누카꿀 > 밤꿀이, 25.0%로 희석한 벌꿀은 마누카 꿀 > 밤꿀 > 잡화꿀 > 재래종꿀 > 클로버 꿀 > 아카시아꿀이, 50.0%로 희석한 벌꿀은 마누카꿀 > 밤꿀 > 캐롤라꿀 > 재래종꿀 > 잡화꿀>클로버꿀 > 아카시아꿀 순으로 항균활성이 인정되었다(p>0.01). Catalase 무첨가의 경우 12.5%, 25.0%, 50.0%로 희석한 벌꿀의 생육억제환은 각각 5.85∼6.60mm, 4.26∼8.27 mm, 5.24∼11.49mm 범위였다. Catalase 첨가의 경우 12.5%로 희석한 벌꿀은 마누카꿀에서 만 항균활성을 나타냈다. 25.0%로 희석한 벌꿀은 마누카꿀이 밤꿀보다 항균활성이 더 높게 나타냈다.(p > 0.01). 50.0%로 희석한 벌꿀은 마누카꿀 > 밤꿀>클로버꿀)캐롤라꿀>재래종꿀 순으로 항균활성이 높았으며 마누카꿀, 밤꿀, 클로버꿀, 캐롤라꿀, 재래종꿀 사이에서 유의성이 인정되었다(p > 0.01). Catalase 첨가의 경우 12. 5%, 25.0%, 50.0%로 희석한 벌꿀의 생육억제환은 각각 5.89mm, 5.01∼6.84mm, 3.10 ∼8.28mm범위였다.

• Tuberculosis and Respiratory Diseases
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• 제41권3호
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• pp.222-230
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• 1994

연구배경 : Paraquat는 광범위 제초제로서 널리 사용하고 있으나, 중독시 치명적인 중독 증상을 일으킨다. 특히 폐에서는 진행성 불가역성 폐섬유종을 일으키는데, 이의 기전으로 산소유리기와 관계가 있으나 아직은 생화학적 기전이 명확하지 않다. paraquat에 의한 산소유리기가 생기면 glutathione의 변화와 G6PDH, SOD, catalase 및 glutathione peroxidase등의 효소 활성의 변화가 생길 것으로 생각되며, 특히 catalase가 많이 관여할 것으로 생각되어진다. 방법 : Catalase 억제제인 aminotriazole을 사용하여 paraquat만 쓰는 것과 paraquat와 aminotriazole을 같이 투여할때 생쥐의 생존율을 알아보고, 실험군을 정상대조군, Group A(aminotriazole투여군), Group B(paraquat 투여군), Group C(paraquat와 amino-triazole 병합투여군) 4군으로 나누어 폐조직에서 glutathione량, G6PDH, SOD, catalase 및 glutathione peroxidase활성도를 측정하여 비교했다. 결과 : Paraquat와 aminotriazole 병합 투여군의 생존율이 paraquat투여군보다 현저히 감소하였고, paraquat 투여로 인하여 폐 glutathione량은 정상대조군에 비해 20%정도 감소 되었으나, aminotriazole의 투여로 인한 폐 glutathione량의 변화는 없었다. Paraquat투여로 폐 SOD, catalase 및 glutathione peroxidase활성이 모두 유의한 감소를 나타냈는데, 특히 catalase가 가장 큰 효소활성 감소를 나타냈으며, paraquat와 aminotriazole병합투여군에서는 catalase와 glutathione peroxidase활성이 paraquat단독투여군에 비하여 유의한 효소활성감소를 나타냈고, SOD는 효소활성의 변화가 감지되지 않았다. 결론 : Paraquat투여시 catalase활성이 유의하게 감소되는 점으로 보아 paraquat독성이 catalase활성과 밀접하게 연관되는 것으로 사료되며, 또한 paraquat의 독성이 aminotriazole의 병합 투여로 더욱 증가되어 나타나는데, 이러한 결과는 aminotriazole투여로 catalase활성의 감소가 크게 나타나나 glutathione량의 변화는 없는 점으로 보아 aminotriazole투여에 의한 paraquat독성의 증가는 총 폐 glutathione량의 변화에 의한 영향보다는 catalase활성감소에 의한 결과로 생각된다. Paraquat와 aminotriazole를 병합 투여하여 catalase활성이 억제되면 증가된 과산화수소로 hydroxyl radicals이 생성되고, 이에 의한 폐 세포손상이 유발되어 나타나는 것으로 사료된다.

• 한국미생물·생명공학회지
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• 제16권3호
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• pp.193-198
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• 1988

Aspergillus niger KUF-04에서 얻은 catalase는 gel 여과를 포함하여 5단계를 걸쳐 정제하였으며, 9% 회수율로 64배 정제되었다. 본 효소는 406, 503, 625nm에서 흡광을 나타내었으며, 특히 406nm에서 뚜렷한 흡수대를 보여주었다. 이 효소 활성의 최적 pH와 온도는 각각 7.0과 6$0^{\circ}C$이었다. 이 효소는 pH4.0과 8.0 사이에서 안정했으며 열에 대한 안정성은 2$0^{\circ}C$에서 5$0^{\circ}C$까지는 안정했으나, 8$0^{\circ}C$에서 20분간 반응시켰을 때 효소의 활성이 전부 소실되었다. 이 효소의 활성은 주로 hydroxylamine, potassium cyanide, sodium azide에 의해 저해되었다.

• 한국분말재료학회지
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• 제12권1호
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• pp.51-55
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• 2005

$Cu_2O$ nano cubes with high catalase activity were synthesized by reduction of freshly prepared Cu in distilled water at $40^{\circC}$ and their catalase activities of $H_2O_2$ were studied. Transmission electron microscopy (TEM) observation showed that most of these nanocubes were uniform in size, with the average edge length of 30 nm. Selected area electron diffraction of TEM revealed that the nanocube consisted of single crystalline $Cu_2O$, but it changed to CuO phase. The catalase activity depends on the amount of both cuprite phase and surface area.

• 한국동물위생학회지
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• 제30권3호
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• pp.291-304
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• 2007

Mutants of an obligate aerobic bacterium, Vitreoscilla, that have deficiency in heat-labile catalase-peroxidase hydroperoxidase I (HPI) were created by EMS treatment. The catalase-peroxidase HPI-deficient mutant showed substantially lower peroxidase activity in exponential and mid-stationary phase compared with the wild type strain. In late stationary phase, the mutant exhibited no peroxidase activity. Peroxidase deficiency in the mutant was revealed by polyacrylamide gels stained for peroxidase activity. Characteristically, catalase levels in the mutant increased about 14- and 8-fold during growth in the exponential and stationary phases, respectively, compared to those in the wild type, suggesting a compensatory effect for protection from $H_2O_2$ toxicity. The mutant showed differences in physiology from the wild type: retardation in growth rate and decrease in oxygen consumption. Both the wild type and the catalase-peroxidase HPI-deficient mutant of Vitreoscilla had lower growth rates in media containing increasing $H_2O_2$ concentrations. However, the mutant exhibited an additionally decreased growth rate after 6 to 8 h of growth compared to the wild type. The wild type was resistent up to 20 mM $H_2O_2$, whereas the mutant was very sensitive to high concentrations of exogenous $H_2O_2$. Although elevated catalase levels would provide protection of the bacteria from the deleterious effect of $H_2O_2$, it did not appear to be complete. Cell-free extracts of the mutant showed decreased NADH oxidation rates and higher accumulation of $H_2O_2$ during this oxidation. These results may account for the impaired growth and earlier onset of death phase by the catalase-peroxidase HPI-deficient mutant of Vitreoscilla.

• Journal of Microbiology
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• 제39권3호
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• pp.168-176
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• 2001

Five different types of catalases from photosynthetic bacterium Rhodospirillum rubrum S1 grown aerobically in the dark were found in this study, and designated Catl (350 kDa), Cat2 (323 kDa), Cat3 (266 kDa), Cat4 (246 kDa), and Cat5 (238 kDa). Analysis of native PAGE revealed that Cat2, Cat3, and Cat4 were also produced in the cells anaerobically grown in the light. It is notable that only Cat2 was expressed much more strongly in response to the anaerobic condition. Enzyme activity staining demonstrated that Cat3 and Cat4 had bifunctional catalase-peroxidase activities, while Catl, Cat2, and Cat5 were typical monofunctional catalases. S1 cells grown aerobically in the presence of malate as the sole source of carbon exhibited an apparent catalase Km value of 10 mM and a Vmax of about 705 U/mg protein at late stationary growth phase. The catalase activity of Sl cells grown in the anaerobic environment exhibited a much lower Vmax of about 109 U/mg protein at late logarithmic growth phase. The catalytic activity was stable in the broad range of temperatures (30$\^{C}$-60$\^{C}$), and pH (6.0-10.0). R. rubrum S1 was much more resistant to H$_2$O$_2$in the stationary growth phase than in the exponential growth phase regardless of growth conditions. Cells of stationary growth phase treated with 15 mM H$_2$O$_2$for 1 h showed 3-fold higher catalase activities than the untreated cells. In addition, L-glutamate induced an 80-fold increase in total catalase activity of R. rubrum S1 compared with magic acid. Through fraction analyses of S1 cells, Cat2, Cat3, Cat4 and Cat5 were found in both cytoplasm and periplasm, while Catl was localized only in the cytoplasm.

• BMB Reports
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• 제33권4호
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• pp.344-348
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• 2000

The logarithmically growing Schizosaccharomyces pombe cells were subjected to high heat ($40^{\circ}C$), hydrogen peroxide, and heavy metals such as mercuric chloride and cadmium chloride. Then, the stress responses of catalase, glutathione S-transferase and thioltransferase were investigated. The high heat and cadmium chloride enhanced the catalase activity. The glutathione S-transferase activity of S. pombe cells was increased after treatments with heavy metals. The thioltransferase activity of S. pombe cells was completely abolished by mercuric chloride. Hydrogen peroxide caused no effect on the activities of glutathione S-transferase and thioltransferase. These results suggest that the response of S. pombe cells against oxidative stress is very complicated.

• Journal of Microbiology and Biotechnology
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• 제20권7호
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• pp.1101-1106
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• 2010

Pulsed electric field (PEF) of 1Hz, 1.5 kV, and 1ms increased the activities of catalase and inulinase over the whole range of applied Se concentrations compared with the non-treated cultures. A significant effect of selenium concentration (in the range of 5-14 ${\mu}g/ml$) on both intra- and extracellular enzyme activities was noted. At a Se concentration of 10 ${\mu}g/ml$, the activities of intra- and extracellular inulinases and extracellular catalase in the PEF-treated cultures reached the maximum of 71 U/g d.m., 46 U/g d.m., and approx. 8 U/ml, respectively. The maximum activity of intracellular catalase of approx. 6 U/ml (with and without PEF) was recorded at 5 ${\mu}g$ Se/ml. Further increasing of selenium concentration caused a decrease in the activity of the enzymes.

• Bulletin of the Korean Chemical Society
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• 제22권4호
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• pp.362-366
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• 2001

To show the effects of metallothionein (MT) on the activity of enzymes involved in the removal of reactive oxygen species, MT has been added to the assay systems of superoxide dismutase (SOD), catalase and peroxidase. We have used assay systems of SOD based on NADPH oxidation and nitrite formation from hydroxylammonium chloride as an assay of superoxide breakdown rate. The two assay systems showed different results at the high concentration of MT. MT showed the scavenging of superoxide in the SOD assay system in the presence and absence of SOD. MT added to the SOD assay system behaved as an activator of SOD, but apo-MT behaved as an inhibitor. When MT was added to the assay system in the presence of a fixed amount of SOD, the breakdown rate of superoxide increased. The effects of MT on the decomposition of hydrogen peroxide and the activity of catalase and peroxidase decomposing hydrogen peroxide were evaluated. MT decreased the activities of catalase and peroxidase. We have concluded that the function of MT as an antioxidant might effect the level of superoxide scavenging and not the level of hydrogen peroxide.

• Journal of Microbiology and Biotechnology
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• 제17권9호
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• pp.1460-1468
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• 2007

In this study, an approx. 2.5-kb gene fragment including the catalase gene from Rhodospirillum rubrum S1 was cloned and characterized. The determination of the complete nucleotide sequence revealed that the cloned DNA fragment was organized into three open reading frames, designated as ORF1, catalase, and ORF3 in that order. The catalase gene consisted of 1,455 nucleotides and 484 amino acids, including the initiation and stop codons, and was located 326 bp upstream in the opposite direction of ORF1. The catalase was overproduced in Escherichia coli UM255, a catalase-deficient mutant, and then purified for the biochemical characterization of the enzyme. The purified catalase had an estimated molecular mass of 189 kDa, consisting of four identical subunits of 61 kDa. The enzyme exhibited activity over a broad pH range from pH 5.0 to pH 11.0 and temperature range from $20^{\circ}C$ to $60^{\circ}C$C. The catalase activity was inhibited by 3-amino-1,2,4-triazole, cyanide, azide, and hydroxylamine. The enzyme's $K_m$ value and $V_{max}$ of the catalase for $H_2O_2$ were 21.8 mM and 39,960 U/mg, respectively. Spectrophotometric analysis revealed that the ratio of $A_{406}$ to $A_{280}$ for the catalase was 0.97, indicating the presence of a ferric component. The absorption spectrum of catalase-4 exhibited a Soret band at 406 nm, which is typical of a heme-containing catalase. Treatment of the enzyme with dithionite did not alter the spectral shape and revealed no peroxidase activity. The combined results of the gene sequence and biochemical characterization proved that the catalase cloned from strain S1 in this study was a typical monofunctional catalase, which differed from the other types of catalases found in strain S1.