Production of Catechol from Benzoate by the Wild Strain Ralstonia Species Ba-0323 and Characterization of Its Catechol 1, 2-Dioxygenase(Microbiology & Fermentation Technology)

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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 catechol (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 NH_2-terminal amino acid sequence of the enzyme was less similar to the other catechol 1, 2-dioxygenases than they are to each other.
社団法人日本農芸化学会の論文
2001-09-23