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Degradation of 2,5-dimethylpyrazine by Rhodococcus Erythropolis Strain DP-45 Isolated From a Waste Gas Treatment Plant of a Fishmeal Processing Company

Degradation of 2,5-dimethylpyrazine by Rhodococcus Erythropolis Strain DP-45 Isolated From a Waste Gas Treatment Plant of a Fishmeal Processing Company

Sugima Rappert, Renjie Li, Mariya Kokova, Mathias Antholz, Stephanie Nagorny, Wittko Francke, Rudolf Müller

Biodegradation. 2007 Oct;18(5):585-96.

PMID: 17120096

Abstract:

A bacterium, strain DP-45, capable of degrading 2,5-dimethylpyrazine (2,5-DMP) was isolated and identified as Rhodococcus erythropolis. The strain also grew on many other pyrazines found in the waste gases of food industries, like 2,3-dimethylpyrazine (2,3-DMP), 2,6-dimethylpyrazine (2,6-DMP), 2-ethyl-5(6)-dimethylpyrazine (EMP), 2-ethylpyrazine (EP), 2-methylpyrazine (MP), and 2,3,5-trimethylpyrazine (TMP). The strain utilized 2,5-DMP as sole source of carbon and nitrogen and grew optimally at 25 degrees C with a doubling time of 7.6 h. The degradation of 2,5-DMP was accompanied by the growth of the strain and by the accumulation of a first intermediate, identified as 2-hydroxy-3,6-dimethylpyrazine (HDMP). The disappearance of HDMP was accompanied by the release of ammonium into the medium. No other metabolite was detected. The degradation of 2,5-DMP and HDMP by strain DP-45 required molecular oxygen. The expression of the first enzyme in the pathway was induced by 2,5-DMP and HDMP whereas the second enzyme was constitutively expressed. The activity of the first enzyme was inhibited by diphenyliodonium (DPI), a flavoprotein inhibitor, methimazole, a competitive inhibitor of flavin-containing monooxygenases, and by cytochrome P450 inhibitors, 1-aminobenzotriazole (ABT) and phenylhydrazine (PHZ). The activity of the second enzyme was inhibited by DPI, ABT, and PHZ. Sodium tungstate, a specific antagonist of molybdate, had no influence on growth and consumption of 2,5-DMP by strain DP-45. These results led us to propose that a flavin-dependent monooxygenase or a cytochrome P450-dependent monooxygenase rather than a molybdenum hydroxylase catalyzed the initial hydroxylation step and that a cytochrome P450 enzyme is responsible for the transformation of HDMP in the second step.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP123320	2,5-Dimethylpyrazine		123-32-0	Price
AP5910894	2,3-Dimethylpyrazine		5910-89-4	Price

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