| Title | Characteristics of Catechol 2,3-dioxygenase Produced by 4-Chlorobenzoate-degrading Pseudomonas sp. S-47 |
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| Author | Kim, Ki Pil · Seo, Dong In · Min, Kyung Hee¹ · Ka, Jong Ok¹ · Park, Yong Keun¹ · Kim, Chi Kyung¹ |
| Address | Departmemt of Microbiology, Chungbuk National University; ¹Research Center for Molecular Microbiology, Seoul National University |
| Bibliography | Journal of Microbiology, 35(4),295-299, 1997, |
| DOI | |
| Key Words | Catechol 2,3-dioxygenase (C23O), 4-chlorobenzoate degradation, Pseudomonas sp. S-47 |
| 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 30~35℃ 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. |
| Download PDF | Eng_350409_295-299p.pdf |