摘要

The strains of Stenotrophomonas maltophilia KB2 and Pseudomonas putida N6 are characterized by an enhanced capacity for degrading aromatic compounds: within five hours of incubation both the strains were found to provide a complete degradation of phenol (3 mmol/dm(3)). Upon induction with phenol, catechol 2,3-dioxygenase, an enzyme responsible for the meta-cleavage of aromatic compounds, was detected in the Stenotrophomonas maltophilia KB2 strain, whereas in the Pseudomonas putida N6 strain the presence was revealed of catechol 1,2-dioxygenase, an enzyme characteristic of the pathway for the ortho-fission of the aromatic ring. Tests on the sensitivity of the enzymes to metal ions have demonstrated that Zn2+ ions activated catechol 2,3-dioxygenase in the KB2 strain. The other metal ions were found to be inhibitors of this enzyme. Among the metal ions tested, the Cu2+ ion was the strongest inhibitor of the two isolated dioxynases. Slightly weaker was the inhibition of catechol 1,2-dioxygenase induced by Cd2+ and Zn2+ ions in the N6 strain. The activity of this enzyme increased in the presence of Co2+ ions. The other ions had no significant influence on the activity of the catechol 1,2-dioxygenase isolated from the N6 strain. The partial activity of both dioxygenases observed upon the application of metal salts suggests that both the strains, Stenotrophomonas maltophilia KB2 and Pseudomonas putida N6, may contribute much to the remediation of an environment polluted with aromatic compounds.

  • 出版日期2010