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KMID : 0380020040190010050
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Korean Journal of Biotechnology and Bioengineering
2004 Volume.19 No. 1 p.50 ~ p.56
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Characterization of different Dioxygenases isolated from Delftia sp. JK-2 capable of degrading Aromatic Compounds. Aniline. Benzoate, and ρ-Hydroxybenzoate
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Oh Kye-Heon
Hwang Sun-Young
Chun Jae-Woo
Kang Hyung-Il
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Abstract
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The aim of this work was to investigate the purification and characterization dixoygenases isolated from Delftia sp. JK-2, which could utilize aniline, benzoate, and p-hydroxybenoate as sole carbon and energy source. Catechol 1,2-dioxygenase (C1, 2O), catechol 2,3-dioxygenase(C2, 3O), and protocatechuate 4,5-dioxygenase(4,5-PCD) were isolated by benzoate, aniline, and p-hydroxybenzoate. In initial experiments, several characteristics of C1 ,2O, C2, 3O, and 4,5-PCD separated with ammonium sulfate precipitation, DEAE-sepharose, and Q-sepharose were investigated. Specific activity of C1 ,2O, C2, 3O, and 4,5-PCD were approximately 3.3 unit/mg, 4.7 unit/mg, and 2.0 unit/mg. C1 ,2O and C2, 3O demonstrated their enzyme activities to other substrates, catechol and 4-methylcatechol. 4,5-PCD showed the specific activity to the only substrate, protocatechuate, but the substrates(e.g., catechol, 3-methylcatechol, 4-methylcatechol, 4-chlorocatechol, 4-nitrocatechol) did not show any specific activities in this work. The optimum temperature of C1, 2O, C2, 3O, and 4,5-PCD were 30, and the optimal pHs were approximately 8, 8, and 7, respectively. Ag+/, Hg+/, Cu2+/ showed inhibitory effect on the activity of C1, 2O and C2, 3O, but Ag+/, Hg+/, Cu2+/, Fe3+/ showed inhibitory effect on the activity of 4,5-PCD. Molecular weight of the C1, 2O, C2, 3O, and 4,5-PCD were determined to approximately 60 kDa,35 kDa, and 62 kDa by SDS-PAGE.
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KEYWORD
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Delftia sp. JK-2, aniline, benzoate, ρ-hydroxybenzoate, dioxygenases
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