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KMID : 0366119910190050470
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Korean Journal of Applied Microbiology & Bioengineering
1991 Volume.19 No. 5 p.470 ~ p.476
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Purification and Characterization of Peroxidase from Chinese Cabbage
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Lee Hae-Ik
Park Kyung-Suk
Choi Yong-Soon
Lee Sang-Young
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Abstract
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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℃. 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 ㎚ and this result indicate that the enzyme contained heme as a prosthetic group. The immurochemical and electrophoretic properties of purified peroxidase from Chinese cabbage were very similar to horseradish peroxidase.
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KEYWORD
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Chinese cabbage, peroxidase
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