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Cloning, expression and characterization of a novel GH5 exo/endoglucanase of Thermobifida halotolerans YIM 90462T by genome mining.

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Title: Cloning, expression and characterization of a novel GH5 exo/endoglucanase of Thermobifida halotolerans YIM 90462T by genome mining.
Authors: Zhang, Feng1, Zhang, Xiao-Mei2, Yin, Yi-Rui2, Li, Wen-Jun2,3 liact@hotmail.com
Source: Journal of Bioscience & Bioengineering. Dec2015, Vol. 120 Issue 6, p644-649. 6p.
Subjects: Molecular cloning, Gene expression, Glycosidases, Glucanases, Genetic code
Abstract: The 1389-bp thcel5A gene, which encodes a family 5 of glycoside hydrolases (GH5), was screened from the draft genome of Thermobifida halotolerans YIM 90462 T . ThCel5A was most similar (77% identity) to a GH5 endoglucanase from Thermobifida fusca YX, followed by cellulases from Nocardiopsis dassonvillei subsp. dassonvillei DSM 43111, Nocardiopsis alba ATCC BAA-2165, and Kribbella flavida DSM 17836. The deduced amino acid sequence of ThCel5A, which consisted of 462 amino acid residues, encompassed a family 2 cellulose-binding module and a GH5 catalytic domain. Notably, ThCel5A hydrolysed soluble as well as insoluble cellulose substrates. The enzymatic hydrolysis assay showed that the activity of recombinant ThCel5A was optimized at pH 8.0 and 50°C. Moreover, it retained hydrolytic activity in the presence of various metal ions and >90% activity within the range of pH 8.0–9.0 after 30 min at 50°C. These results suggested that this enzyme has considerable potential in industrial applications. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Bioscience & Bioengineering 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
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DbLabel: Engineering Source
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  Data: Cloning, expression and characterization of a novel GH5 exo/endoglucanase of Thermobifida halotolerans YIM 90462T by genome mining.
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  Data: <searchLink fieldCode="AR" term="%22Zhang%2C+Feng%22">Zhang, Feng</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Zhang%2C+Xiao-Mei%22">Zhang, Xiao-Mei</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Yin%2C+Yi-Rui%22">Yin, Yi-Rui</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Li%2C+Wen-Jun%22">Li, Wen-Jun</searchLink><relatesTo>2,3</relatesTo><i> liact@hotmail.com</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Bioscience+%26+Bioengineering%22">Journal of Bioscience & Bioengineering</searchLink>. Dec2015, Vol. 120 Issue 6, p644-649. 6p.
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  Data: <searchLink fieldCode="DE" term="%22Molecular+cloning%22">Molecular cloning</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="%22Glucanases%22">Glucanases</searchLink><br /><searchLink fieldCode="DE" term="%22Genetic+code%22">Genetic code</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The 1389-bp thcel5A gene, which encodes a family 5 of glycoside hydrolases (GH5), was screened from the draft genome of Thermobifida halotolerans YIM 90462 T . ThCel5A was most similar (77% identity) to a GH5 endoglucanase from Thermobifida fusca YX, followed by cellulases from Nocardiopsis dassonvillei subsp. dassonvillei DSM 43111, Nocardiopsis alba ATCC BAA-2165, and Kribbella flavida DSM 17836. The deduced amino acid sequence of ThCel5A, which consisted of 462 amino acid residues, encompassed a family 2 cellulose-binding module and a GH5 catalytic domain. Notably, ThCel5A hydrolysed soluble as well as insoluble cellulose substrates. The enzymatic hydrolysis assay showed that the activity of recombinant ThCel5A was optimized at pH 8.0 and 50°C. Moreover, it retained hydrolytic activity in the presence of various metal ions and >90% activity within the range of pH 8.0–9.0 after 30 min at 50°C. These results suggested that this enzyme has considerable potential in industrial applications. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Bioscience & Bioengineering 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.)
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      – Type: doi
        Value: 10.1016/j.jbiosc.2015.04.012
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      – Code: eng
        Text: English
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        PageCount: 6
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      – SubjectFull: Molecular cloning
        Type: general
      – SubjectFull: Gene expression
        Type: general
      – SubjectFull: Glycosidases
        Type: general
      – SubjectFull: Glucanases
        Type: general
      – SubjectFull: Genetic code
        Type: general
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      – TitleFull: Cloning, expression and characterization of a novel GH5 exo/endoglucanase of Thermobifida halotolerans YIM 90462T by genome mining.
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            NameFull: Zhang, Feng
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            NameFull: Zhang, Xiao-Mei
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            NameFull: Yin, Yi-Rui
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            NameFull: Li, Wen-Jun
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            – D: 01
              M: 12
              Text: Dec2015
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              Y: 2015
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