Modulation of FAD-dependent monooxygenase activity from aromatic compounds-degrading Stenotrophomonas maltophilia strain KB2 | Health & Environmental Research Online (HERO)

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Citation
Tags

HERO ID

1257035

Reference Type

Journal Article

Title

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

Author(s)

Wojcieszyńska, D; Greń, I; Hupert-Kocurek, K; Guzik, U

Year

2011

Is Peer Reviewed?

Yes

Journal

Acta Biochimica Polonica
ISSN: 0001-527X

Book Title

Acta Biochimica Polonica

Volume

Issue

Page Numbers

421-426

Language

English

PMID

21927719

DOI

10.18388/abp.2011_2256

Web of Science Id

WOS:000295488300020

URL

https://ojs.ptbioch.edu.pl/index.php/abp/article/view/2256
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Abstract

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.

Keywords

Inhibitors; Monooxygenase; Phenols; Stenotrophomonas