Production of Catechol from Benzoate by the Wild Strain Ralstonia Species Ba-0323 and Characterization of Its Catechol 1,2-Dioxygenase

Article abstract of DOI:10.1271/bbb.65.1957

Ralstonia sp. Ba-0323, a wild strain isolated from soil, produced catechol from benzoate and accumulated it outside the cells. The bacterium produced a maximal amount of calechol (1.6 mg/ml) from 3 mg/ml of sodium benzoate in a 20-h growing culture. The conversion rate of benzoate to catechol was 70% on a molar basis. The catechol production by the resting cells increased in the presence of glycerol, and the maximal amount of catechol produced from 3 mg/ml of sodium benzoate reached 1.9 mg/ml at the conversion rate of 83% after 8 h of incubation. Catechol 1,2-dioxygenase, which catalyzed the ring cleavage of catechol, was purified to homogeneity from a cell extract of Ralstonia sp. Ba-0323 growing on benzoate and characterized. The specific activity of the purified enzyme was much lower than those of the dioxygenases from other microorganisms reported. The K_m for catechol of the purified enzyme was much higher than those of other dioxygenases. In addition, the NH₂-terminal amino acid sequence of the enzyme was less similar to the other catechol 1,2-dioxygenases than they are to each other.

Full text of DOI:10.1271/bbb.65.1957

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Production of Catechol from Benzoate by the
Wild Strain Ralstonia Species Ba-0323 and
Characterization of Its Catechol 1,2-Dioxygenase
a
b
b
b
Chuan Lu WANG , Shinji TAKENAKA , Shuichiro MURAKAMI & Kenji AOKI
a
Division of Science of Biological Resources, The Graduate School of Science and
Technology, Kobe University
b
Laboratory of Applied Microbiology, Department of Biofunctional Chemistry, Faculty of
Agriculture, Kobe University
Published online: 22 May 2014.
To cite this article: Chuan Lu WANG, Shinji TAKENAKA, Shuichiro MURAKAMI & Kenji AOKI (2001) Production of Catechol
from Benzoate by the Wild Strain Ralstonia Species Ba-0323 and Characterization of Its Catechol 1,2-Dioxygenase,
Bioscience, Biotechnology, and Biochemistry, 65:9, 1957-1964, DOI: 10.1271/bbb.65.1957
To link to this article: http://dx.doi.org/10.1271/bbb.65.1957
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