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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
58
Issue
3
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
Tags
•
Ethylbenzene
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