Journal of Microbiology

The Microbiological Society of Korea (한국미생물학회)
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Characteristics of Catechol 2,3-Dioxygenase Produced by 4-Chlorobenzoate-degrading Pseudomonas sp. S-47

  • Kim, Ki-Pil (Department of Microbiology, Chungbuk National University) ;
  • Seo, Dong-In (Department of Microbiology, Chungbuk National University) ;
  • Min, Kyung-Hee (Research Center for Molecular Microbiology, Seoul National University) ;
  • Ka, Jong-Ok (Research Center for Molecular Microbiology, Seoul National University) ;
  • Park, Yong-Keun (Research Center for Molecular Microbiology, Seoul National University) ;
  • Kim, Chi-Kyung (Department of Microbiology, Chungbuk National University)
  • Published : 1997.01.01
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Abstract

Pseudomonas sp. S-47 is capable of transforming 4-chlorobenzoate to 4-chlorocatechol which is subsequently oxidized bty meta-cleavage dioxygenase to prodyce 5-chloro-2-hydroxymuconic semialdehyde. Catechol 2,3-dioxygenase (C23O) produced by Pseudomonas sp. S-47 was purified and characterized in this study. The C23O enzyme was maximally produced in the late logarithmic growth phase, and the temperature and pH for maximunm enzyme activity were $30{\sim}35^{\circ}C$ and 7.0, respectively. The enzyme was purified and concentrated 5 fold from the crude cell extracts through Q Sepharose chromatography and Sephadex G-100 gel filtration after acetone precipitation. The enzyme was identified as consisting of 35 kDa subunits when analyzed by SDS-PAGE. The C23O produced by Pseudomonas sp. S-47 was similar to Xy1E of Pseudomonas putida with respect to substrate specificity for several catecholic compounds.

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