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N2O production from hydroxylamine oxidation and corresponding hydroxylamine oxidoreductase involved in a heterotrophic nitrifier A. faecalis strain NR.

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Title: N2O production from hydroxylamine oxidation and corresponding hydroxylamine oxidoreductase involved in a heterotrophic nitrifier A. faecalis strain NR.
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]
Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: N<subscript>2</subscript>O production from hydroxylamine oxidation and corresponding hydroxylamine oxidoreductase involved in a heterotrophic nitrifier A. faecalis strain NR.
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  Data: <searchLink fieldCode="AR" term="%22Zhao%2C+Bin%22">Zhao, Bin</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Ran%2C+Xiao+Chuan%22">Ran, Xiao Chuan</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22An%2C+Qiang%22">An, Qiang</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> anqiang@cqu.edu.cn</i><br /><searchLink fieldCode="AR" term="%22Huang%2C+Yuan+Sheng%22">Huang, Yuan Sheng</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lv%2C+Qing+Hao%22">Lv, Qing Hao</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Dan%2C+Qiao%22">Dan, Qiao</searchLink><relatesTo>1</relatesTo> (AUTHOR)
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  Data: <searchLink fieldCode="JN" term="%22Bioprocess+%26+Biosystems+Engineering%22">Bioprocess & Biosystems Engineering</searchLink>. Dec2019, Vol. 42 Issue 12, p1983-1992. 10p.
– Name: Subject
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  Data: <searchLink fieldCode="DE" term="%22Oxidation%22">Oxidation</searchLink><br /><searchLink fieldCode="DE" term="%22Chemical+reactions%22">Chemical reactions</searchLink><br /><searchLink fieldCode="DE" term="%22Electrophiles%22">Electrophiles</searchLink><br /><searchLink fieldCode="DE" term="%22Hydroxylamine%22">Hydroxylamine</searchLink><br /><searchLink fieldCode="DE" term="%22Nitrification%22">Nitrification</searchLink>
– Name: Abstract
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  Data: 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]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Bioprocess & Biosystems Engineering is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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      – Type: doi
        Value: 10.1007/s00449-019-02191-w
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      – Code: eng
        Text: English
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      Pagination:
        PageCount: 10
        StartPage: 1983
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      – SubjectFull: Oxidation
        Type: general
      – SubjectFull: Chemical reactions
        Type: general
      – SubjectFull: Electrophiles
        Type: general
      – SubjectFull: Hydroxylamine
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      – SubjectFull: Nitrification
        Type: general
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      – TitleFull: N2O production from hydroxylamine oxidation and corresponding hydroxylamine oxidoreductase involved in a heterotrophic nitrifier A. faecalis strain NR.
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            NameFull: Ran, Xiao Chuan
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              M: 12
              Text: Dec2019
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              Y: 2019
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