N2O production from hydroxylamine oxidation and corresponding hydroxylamine oxidoreductase involved in a heterotrophic nitrifier A. faecalis strain NR.
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| Title: | N |
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| Authors: | Zhao, Bin1 (AUTHOR), Ran, Xiao Chuan1 (AUTHOR), An, Qiang1 (AUTHOR) anqiang@cqu.edu.cn, Huang, Yuan Sheng1 (AUTHOR), Lv, Qing Hao1 (AUTHOR), Dan, Qiao1 (AUTHOR) |
| Source: | Bioprocess & Biosystems Engineering. Dec2019, Vol. 42 Issue 12, p1983-1992. 10p. |
| Subjects: | Oxidation, Chemical reactions, Electrophiles, Hydroxylamine, Nitrification |
| Abstract: | N2O production from NH2OH oxidation involved in a heterotrophic nitrifier Alcaligenes faecalis strain NR was studied. 15N-labeling experiments showed that biological NH2OH consumption by strain NR played a dominant role in N2O production, although chemical reaction between NH2OH and O2 indeed existed. Hydroxylamine oxidoreductase (HAO) from strain NR was partially purified by (NH4)2SO4 fractionation and DEAE Cartridge chromatography. The maximum activity of HAO was 9.60 mU with a specific activity of 92.04 mU/(mg protein) when K3Fe(CN)6 was used as an electron acceptor. The addition of Ca2+ promoted the HAO activity, while the presence of Mn2+ inhibited the enzyme activity. The optimal temperature and pH for HAO activity were 30 °C and 8. Analysis of enzyme-catalyzed products demonstrated that NH2OH oxidation catalyzed by HAO from strain NR played significant role in the production of N2O. [ABSTRACT FROM AUTHOR] |
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| Database: | Engineering Source |
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| Abstract: | N2O production from NH2OH oxidation involved in a heterotrophic nitrifier Alcaligenes faecalis strain NR was studied. 15N-labeling experiments showed that biological NH2OH consumption by strain NR played a dominant role in N2O production, although chemical reaction between NH2OH and O2 indeed existed. Hydroxylamine oxidoreductase (HAO) from strain NR was partially purified by (NH4)2SO4 fractionation and DEAE Cartridge chromatography. The maximum activity of HAO was 9.60 mU with a specific activity of 92.04 mU/(mg protein) when K3Fe(CN)6 was used as an electron acceptor. The addition of Ca2+ promoted the HAO activity, while the presence of Mn2+ inhibited the enzyme activity. The optimal temperature and pH for HAO activity were 30 °C and 8. Analysis of enzyme-catalyzed products demonstrated that NH2OH oxidation catalyzed by HAO from strain NR played significant role in the production of N2O. [ABSTRACT FROM AUTHOR] |
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| ISSN: | 16157591 |
| DOI: | 10.1007/s00449-019-02191-w |
