Modulation of FAD-dependent monooxygenase activity from aromatic compounds-degrading Stenotrophomonas maltophilia strain KB2

• Autorzy: Wojcieszynska D. , Gren I. , Hupert-Kocurek K. , Guzik U.
• Języki publikacji: EN

Abstrakty

EN

The purpose of this study was purification and characterization of phenol monooxygenase from Stenotrophomonas maltophilia strain KB2, enzyme that catabolises phenol and its derivatives through the initial hydroxylation to catechols. The enzyme requires NADH and FAD as a cofactors for activity, catalyses hydroxylation of a wide range of monocyclic phenols, aromatic acids and dihydroxylated derivatives of benzene except for catechol. High activity of this monooxygenase was observed in cell extract of strain KB2 grown on phenol, 2-methylphenol, 3-metylphenol or 4-methylphenol. Ionic surfactants as well as cytochrome P450 inhibitors or 1,4-dioxane, acetone and n-butyl acetate inhibited the enzyme activity, while non-ionic surfactants, chloroethane, ethylbenzene, ethyl acetate, cyclohexane, and benzene enhanced it. These results indicate that the phenol monooxygenase from Stenotrophomonas maltophilia strain KB2 holds great potential for bioremediation.

Słowa kluczowe

EN

monooxygenase activity; aromatic compound; Stenotrophomonas maltophilia; KB2 strain; phenol; inhibitor; 2-aminophenol; 3-aminophenol; 4-aminophenol; 2-chlorophenol; 3-chlorophenol; 4-chlorophenol; 2-nitrophenol; 3-nitrophenol; 4-nitrophenol; 2-methylphenol; 3-methylphenol; 4-methylphenol

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2011
• Tom: 58
• Numer: 3
• Opis fizyczny: p.421-426,fig.,ref.

Twórcy

autor

Wojcieszynska D.

• Department of Biochemistry, University of Silesia in Katowice, Katowice, Poland

autor

Gren I.

autor

Hupert-Kocurek K.

autor

Guzik U.

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