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Substrate specificity and sensitiveness of phenol monooxygenase from Stenotrophomonas maltophilia strain KB2 versus their potential application to bioremediation of the environment

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Wojcieszynska D., Gren I., Labuzek S., Respondek M.
|
2007
|
issue 2
181-191
EN
Phenol monooxygenase, isolated from Stenotrophomonas maltophilia strain KB2, was sensitive to sodium azide, metals salts except for iron (II) sulfate at concentration of 1 mM, chelate compounds, sulfhydryl agents, lauroylsarcosine Na-salt, SDS and hydrogen peroxide. Slight increase of the enzyme activity was observed in the presence of hexane and ether. The presence of ascorbic acid caused an increase of the enzyme activity. Phenol monooxygenase activity changed significantly depending on the tested aromatic substrate in the reaction mixture and the type of the applied inductor.
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