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Potential application of catalase-peroxidase from Comamonas terrigena N3H in the biodegradation of phenolic compounds
Authors:Zámocký M  Godocíková J  Koller F  Polek B
Affiliation:(1) Institute of Microbiology, Slovak Academy of Sciences, "Scaron"tefánikova 3, SK-81434 Bratislava, Slovakia;(2) Institute of Biochemistry and Molecular Cell Biology, University of Vienna, and Ludwig Boltzmann Forschungsstelle für Biochemie, Dr. Bohrgasse 9, A-1030 Vienna, Austria
Abstract:Comamonas terrigena N3H is a gram-negative rod-shaped bacterium that was isolated from contaminated soil in Slovakia. This bacterium showed remarkable biodegradation properties. We investigated the expression and functioning of two catalase isozymes in this bacterium. The typical catalase could be induced by cadmium ions, whereas the catalase-peroxidase enzyme was constitutively expressed. Since C. terrigena lacks the key enzyme for complete degradation of phenols (phenolhydroxylase), we analysed the possible removal of phenol by the two catalases of this bacterium. Addition of phenol to the culture medium led to increased expression of the catalase-peroxidase. Applying oxidative stress prior to phenol administration markedly induced the expression of the typical catalase, irrespective of the nature of the added agent. Thus, the rate of phenol degradation is rather reduced under these conditions, while growth of the cells is not impaired. We concluded that phenol peroxidation in C. terrigena can be largely attributed to the action of a catalase-peroxidase. The potential application of this enzyme in the removal of phenol from the environment is discussed.
Keywords:biodegradation  catalase-peroxidase  Comamonas terrigena  phenol removal  typical catalase
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