View in EDS PDF Full Text

Identification and characterization of a novel 2R,3R-Butanediol dehydrogenase from Bacillus sp. DL01.

Saved in:
Bibliographic Details
Title: Identification and characterization of a novel 2R,3R-Butanediol dehydrogenase from Bacillus sp. DL01.
Authors: Elmahmoudy, Mostafa1, Elfeky, Nora1,2, Pu Zhongji1, Yue Zhang1, Yongming Bao1,3 biosci@dlut.edu.cn
Source: Electronic Journal of Biotechnology. Jan2021, Vol. 49, p56-63. 8p.
Subjects: Butanediol, Diacetyl, NAD (Coenzyme), Identification, Bacillus subtilis, Hydroxyl group, Acetoin, NADH dehydrogenase
Abstract: Background: 2R,3R-butanediol dehydrogenase (R-BDH) and other BDHs contribute to metabolism of 3R/3S-Acetoin (3R/3S-AC) and 2,3-butanediol (2,3-BD), which are important bulk chemicals used in different industries. R-BDH is responsible for oxidizing the hydroxyl group at their (R) configuration. Bacillus species is a promising producer of 3R/3S-AC and 2,3-BD. In this study, R-bdh gene encoding R-BDH from Bacillus sp. DL01 was isolated, expressed and identified. Results: R-BDH exerted reducing activities towards Diacetyl (DA) and 3R/3S-AC using NADH, and oxidizing activities towards 2R,3R-BD and Meso-BD using NAD+, while no activity was detected with 2S,3S-BD. The R-BDH showed its activity at a wide range of temperature (25°C to 65°C) and pH (5.0-8.0). The R-BDH activity was increased significantly by Cd2+ when DA, 3R/3S-AC, and Meso-BD were used as substrates, while Fe2+ enhanced the activity remarkably at 2R,3R-BD oxidation. Kinetic parameters of the R-BDH from Bacillus sp. DL01 showed the lowest Km, the highest Vmax, and the highest Kcat towards the racemic 3R/3S-AC substrate, also displayed low Km towards 2R,3R-BD and Meso-BD when compared with other reported R-BDHs. Conclusions: The R-BDH from Bacillus sp. DL01 was characterized as a novel R-BDH with high enantioselectivity for R-configuration. It considered NAD+ and Zn2+ dependant enzyme, with a significant affinity towards 3R/3S-AC, 2R,3R-BD, and Meso-BD substrates. Thus, R-BDH is providing an approach to regulate the production of 3R/3S-AC or 2,3-BD from Bacillus sp. DL01. [ABSTRACT FROM AUTHOR]
Copyright of Electronic Journal of Biotechnology is the property of Pontificia Universidad Catolica de Valparaiso 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.)
Database: Engineering Source
FullText Links:
  – Type: pdflink
Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 148177387
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Identification and characterization of a novel 2R,3R-Butanediol dehydrogenase from Bacillus sp. DL01.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Elmahmoudy%2C+Mostafa%22">Elmahmoudy, Mostafa</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Elfeky%2C+Nora%22">Elfeky, Nora</searchLink><relatesTo>1,2</relatesTo><br /><searchLink fieldCode="AR" term="%22Pu+Zhongji%22">Pu Zhongji</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Yue+Zhang%22">Yue Zhang</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Yongming+Bao%22">Yongming Bao</searchLink><relatesTo>1,3</relatesTo><i> biosci@dlut.edu.cn</i>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Electronic+Journal+of+Biotechnology%22">Electronic Journal of Biotechnology</searchLink>. Jan2021, Vol. 49, p56-63. 8p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Butanediol%22">Butanediol</searchLink><br /><searchLink fieldCode="DE" term="%22Diacetyl%22">Diacetyl</searchLink><br /><searchLink fieldCode="DE" term="%22NAD+%28Coenzyme%29%22">NAD (Coenzyme)</searchLink><br /><searchLink fieldCode="DE" term="%22Identification%22">Identification</searchLink><br /><searchLink fieldCode="DE" term="%22Bacillus+subtilis%22">Bacillus subtilis</searchLink><br /><searchLink fieldCode="DE" term="%22Hydroxyl+group%22">Hydroxyl group</searchLink><br /><searchLink fieldCode="DE" term="%22Acetoin%22">Acetoin</searchLink><br /><searchLink fieldCode="DE" term="%22NADH+dehydrogenase%22">NADH dehydrogenase</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Background: 2R,3R-butanediol dehydrogenase (R-BDH) and other BDHs contribute to metabolism of 3R/3S-Acetoin (3R/3S-AC) and 2,3-butanediol (2,3-BD), which are important bulk chemicals used in different industries. R-BDH is responsible for oxidizing the hydroxyl group at their (R) configuration. Bacillus species is a promising producer of 3R/3S-AC and 2,3-BD. In this study, R-bdh gene encoding R-BDH from Bacillus sp. DL01 was isolated, expressed and identified. Results: R-BDH exerted reducing activities towards Diacetyl (DA) and 3R/3S-AC using NADH, and oxidizing activities towards 2R,3R-BD and Meso-BD using NAD+, while no activity was detected with 2S,3S-BD. The R-BDH showed its activity at a wide range of temperature (25°C to 65°C) and pH (5.0-8.0). The R-BDH activity was increased significantly by Cd2+ when DA, 3R/3S-AC, and Meso-BD were used as substrates, while Fe2+ enhanced the activity remarkably at 2R,3R-BD oxidation. Kinetic parameters of the R-BDH from Bacillus sp. DL01 showed the lowest Km, the highest Vmax, and the highest Kcat towards the racemic 3R/3S-AC substrate, also displayed low Km towards 2R,3R-BD and Meso-BD when compared with other reported R-BDHs. Conclusions: The R-BDH from Bacillus sp. DL01 was characterized as a novel R-BDH with high enantioselectivity for R-configuration. It considered NAD+ and Zn2+ dependant enzyme, with a significant affinity towards 3R/3S-AC, 2R,3R-BD, and Meso-BD substrates. Thus, R-BDH is providing an approach to regulate the production of 3R/3S-AC or 2,3-BD from Bacillus sp. DL01. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Electronic Journal of Biotechnology is the property of Pontificia Universidad Catolica de Valparaiso 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.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=148177387
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.ejbt.2020.11.002
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 8
        StartPage: 56
    Subjects:
      – SubjectFull: Butanediol
        Type: general
      – SubjectFull: Diacetyl
        Type: general
      – SubjectFull: NAD (Coenzyme)
        Type: general
      – SubjectFull: Identification
        Type: general
      – SubjectFull: Bacillus subtilis
        Type: general
      – SubjectFull: Hydroxyl group
        Type: general
      – SubjectFull: Acetoin
        Type: general
      – SubjectFull: NADH dehydrogenase
        Type: general
    Titles:
      – TitleFull: Identification and characterization of a novel 2R,3R-Butanediol dehydrogenase from Bacillus sp. DL01.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Elmahmoudy, Mostafa
      – PersonEntity:
          Name:
            NameFull: Elfeky, Nora
      – PersonEntity:
          Name:
            NameFull: Pu Zhongji
      – PersonEntity:
          Name:
            NameFull: Yue Zhang
      – PersonEntity:
          Name:
            NameFull: Yongming Bao
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 01
              Text: Jan2021
              Type: published
              Y: 2021
          Identifiers:
            – Type: issn-print
              Value: 07173458
          Numbering:
            – Type: volume
              Value: 49
          Titles:
            – TitleFull: Electronic Journal of Biotechnology
              Type: main
ResultId 1