View in EDS

Heterologous expression, characterization and application of a new β-xylosidase identified in solventogenic Clostridium sp. strain BOH3.

Saved in:
Bibliographic Details
Title: Heterologous expression, characterization and application of a new β-xylosidase identified in solventogenic Clostridium sp. strain BOH3.
Authors: Li, Tinggang1, Wu, Yi-Rui1, He, Jianzhong1 jianzhong.he@nus.edu.sg
Source: Process Biochemistry. Apr2018, Vol. 67, p99-104. 6p.
Subjects: Xylosidases, Clostridium, Gene expression, Glycosidases, Hydrolysis, Escherichia coli
Abstract: A β-xylosidase gene (Bxyl BOH3 ) was identified in a solventogenic bacterium Clostridium sp. strain BOH3, which is a member of the glycoside hydrolase family 43 (GH43). The recombinant enzyme of Bxyl BOH3 was expressed in Escherichia coli with a high specific activity of 48.7 U/mg and a low K m value of 2.71 mM at an optimal temperature of 40 °C and pH of 5.0-6.0, indicating its high affinity for the substrate and enzymatic potency. Moreover, activity of β-xylosidase can be enhanced (>1.6 times) by addition of Zn 2+ . The concentration of reducing sugar (including xylose and xylooligosaccharides) with the synergism of xylanase and recombinant β-xylosidase was enhanced up to 129.8% (11.93 g/L) after hydrolysis of 30 g/L of xylan for 24 h when comparing with only xylanase (9.19 g/L). Application of this recombinant β-xylosidase together with xylanase improved xylan hydrolysis efficiency, thus leading to increased biofuels productivity from xylan fermented by Clostridium species. [ABSTRACT FROM AUTHOR]
Copyright of Process Biochemistry is the property of Elsevier B.V. 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 Text:
  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 128564086
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Heterologous expression, characterization and application of a new β-xylosidase identified in solventogenic Clostridium sp. strain BOH3.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Li%2C+Tinggang%22">Li, Tinggang</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Wu%2C+Yi-Rui%22">Wu, Yi-Rui</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22He%2C+Jianzhong%22">He, Jianzhong</searchLink><relatesTo>1</relatesTo><i> jianzhong.he@nus.edu.sg</i>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Process+Biochemistry%22">Process Biochemistry</searchLink>. Apr2018, Vol. 67, p99-104. 6p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Xylosidases%22">Xylosidases</searchLink><br /><searchLink fieldCode="DE" term="%22Clostridium%22">Clostridium</searchLink><br /><searchLink fieldCode="DE" term="%22Gene+expression%22">Gene expression</searchLink><br /><searchLink fieldCode="DE" term="%22Glycosidases%22">Glycosidases</searchLink><br /><searchLink fieldCode="DE" term="%22Hydrolysis%22">Hydrolysis</searchLink><br /><searchLink fieldCode="DE" term="%22Escherichia+coli%22">Escherichia coli</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: A β-xylosidase gene (Bxyl BOH3 ) was identified in a solventogenic bacterium Clostridium sp. strain BOH3, which is a member of the glycoside hydrolase family 43 (GH43). The recombinant enzyme of Bxyl BOH3 was expressed in Escherichia coli with a high specific activity of 48.7 U/mg and a low K m value of 2.71 mM at an optimal temperature of 40 °C and pH of 5.0-6.0, indicating its high affinity for the substrate and enzymatic potency. Moreover, activity of β-xylosidase can be enhanced (>1.6 times) by addition of Zn 2+ . The concentration of reducing sugar (including xylose and xylooligosaccharides) with the synergism of xylanase and recombinant β-xylosidase was enhanced up to 129.8% (11.93 g/L) after hydrolysis of 30 g/L of xylan for 24 h when comparing with only xylanase (9.19 g/L). Application of this recombinant β-xylosidase together with xylanase improved xylan hydrolysis efficiency, thus leading to increased biofuels productivity from xylan fermented by Clostridium species. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Process Biochemistry is the property of Elsevier B.V. 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=128564086
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.procbio.2018.02.003
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 6
        StartPage: 99
    Subjects:
      – SubjectFull: Xylosidases
        Type: general
      – SubjectFull: Clostridium
        Type: general
      – SubjectFull: Gene expression
        Type: general
      – SubjectFull: Glycosidases
        Type: general
      – SubjectFull: Hydrolysis
        Type: general
      – SubjectFull: Escherichia coli
        Type: general
    Titles:
      – TitleFull: Heterologous expression, characterization and application of a new β-xylosidase identified in solventogenic Clostridium sp. strain BOH3.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Li, Tinggang
      – PersonEntity:
          Name:
            NameFull: Wu, Yi-Rui
      – PersonEntity:
          Name:
            NameFull: He, Jianzhong
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 04
              Text: Apr2018
              Type: published
              Y: 2018
          Identifiers:
            – Type: issn-print
              Value: 13595113
          Numbering:
            – Type: volume
              Value: 67
          Titles:
            – TitleFull: Process Biochemistry
              Type: main
ResultId 1