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한국생태학회 / v.21, no.1, 1998년, pp.73-80 
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지렁이 Peroxidase의 특성 및 페녹시계 제초제의 분해
( characteristics of Peroxidase from the Earthworm, Lumbricus rubellus and Degradation of Phenoxyherbicides ) |
| 이미영;김윤경; 순천향대학교 생명과학부;순천향대학교 생명과학부;
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| 초 록 |
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| Peroxidase has been isolated to apparent homogeneity from earthworm, Lumbricus rubellus, using ammonium sulfate fractionation, Sephacryl S-2000 gel filtration, CM-cellulose cation exchange chromatography and native-PAGE elution. Some of its enzymatic characteristics were examined. The optimum pH for gruaiacol oxidation of earthworm peroxidase was determined to be 6.0, and the $K_{m}$ values against guaiacol and $H_2O_2$ were 1.25 mM and 3.4mM, respectively. When various compounds were tested as the possible substrates of the enzyme, o-dianisidine was used as the substrate. However, earthworm peroxidase could not oxidize esculetin and ferulic acid as substrates, suggesting the different characteristics of the enzyme from plant peroxidases. The optimum pH for veratryl alcohol and $H_2O_2$ oxidation was determined to be 2.5 when lignin peroxidation activity was examined. The $K_{m}$ values for veratryl alcohol and $H_2O_2$ were 0.02 mM and 0.13 mM, respectively. Furthermore, the earthworm peroxidase could oxidize phenoxyherbicides such as 2,4-D, 2,4-DP and MCPA as substrates. The optimum pHs for 2,4-D, 2,4-DP and MCPA were determined to be 4.0, 2.0 and 2.0, respectively. The most available substrate was 2,4-DP, followed by MCPA and 2,4-D when their peroxidation activities were compared. |
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| 키워드 |
| Earthworm;Lumbricus rubellus;Peroxidase;Chracteristics;Phenoxyherbicides; |
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The Korean Journal of Ecology / v.21, no.1, 1998년, pp.73-80
한국생태학회
ISSN : 1225-0317
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO199811919962976)
언어 : 한국어 |
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| 논문 제공 : KISTI 한국과학기술정보연구원 |
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