Heterotrophic nitrogen removal in Bacillus sp. K5 : involvement of a novel hydroxylamine oxidase
An aerobic denitrifying bacterium isolated from a bio-trickling filter treating NOx, Bacillus sp. K5, is able to convert ammonium to nitrite, in which hydroxylamine oxidase (HAO) plays a critical role. In the present study, the performance for simultaneous nitrification and denitrification was inves...
| Veröffentlicht in: | Water science and technology : a journal of the International Association on Water Pollution Research. - 1986. - 76(2017), 11-12 vom: 09. Dez., Seite 3461-3467 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2017
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| Zugriff auf das übergeordnete Werk: | Water science and technology : a journal of the International Association on Water Pollution Research |
| Schlagworte: | Journal Article Ammonium Compounds Nitrites Hydroxylamine 2FP81O2L9Z Oxidoreductases EC 1.- hydroxylamine dehydrogenase EC 1.7.2.6 Nitrogen |
| Zusammenfassung: | An aerobic denitrifying bacterium isolated from a bio-trickling filter treating NOx, Bacillus sp. K5, is able to convert ammonium to nitrite, in which hydroxylamine oxidase (HAO) plays a critical role. In the present study, the performance for simultaneous nitrification and denitrification was investigated with batch experiments and an HAO was purified by an anion-exchange and gel-filtration chromatography from strain K5. The purified HAO's molecular mass was determined by SDS-PAGE and its activity by measuring the change in the concentration of ferricyanide, the electron acceptor. Results showed that as much as 87.8 mg L-1 ammonium-N was removed without nitrite accumulation within 24 hours in the sodium citrate medium at C/N of 15. The HAO isolated from the strain K5 was approximately 71 KDa. With hydroxylamine (NH2OH) as a substrate and potassium ferricyanide as an electron acceptor, the enzyme was capable of oxidizing NH2OH to nitrite in vitro when the pH varied from 7 to 9 and temperature ranged from 25 °C to 40 °C. This is the first time that an HAO has been purified from the Bacillus genus, and the findings revealed that it is distinctive in its molecular mass and enzyme properties |
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| Beschreibung: | Date Completed 03.05.2018 Date Revised 02.12.2018 published: Print Citation Status MEDLINE |
| ISSN: | 0273-1223 |
| DOI: | 10.2166/wst.2017.510 |