Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Characterization of the Four GH12 Endoxylanases from the Plant Pathogen Fusarium graminearum

  • Habrylo, Olivier (Laboratoire d'Ingenierie des Polymeres pour les Hautes Technologies, Universite de Strasbourg) ;
  • Song, Xinghan (Laboratoire d'Ingenierie des Polymeres pour les Hautes Technologies, Universite de Strasbourg) ;
  • Forster, Anne (Laboratoire d'Ingenierie des Polymeres pour les Hautes Technologies, Universite de Strasbourg) ;
  • Jeltsch, Jean-Marc (Laboratoire d'Ingenierie des Polymeres pour les Hautes Technologies, Universite de Strasbourg) ;
  • Phalip, Vincent (Laboratoire d'Ingenierie des Polymeres pour les Hautes Technologies, Universite de Strasbourg)
  • Received : 2011.12.22
  • Accepted : 2012.03.11
  • Published : 2012.08.28
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Abstract

Four putative GH12 genes were found in the Fusarium graminearum genome. The corresponding proteins were expressed in Escherichia coli, purified, and evaluated. FGSG_05851 and FGSG_11037 displayed high activities towards xyloglucan ($V_{max}$ of 4 and $11{\mu}mol/min$, respectively), whereas FGSG_07892 and FGSG_16349 were much less active with this substrate (0.081 and $0.004{\mu}mol/min$, respectively). However, all four of these enzymes had a similar binding affinity for xyloglucan. Xyloglucan was the substrate preferred by FGSG_05851, in contrast to the three other enzymes, which preferred ${\beta}$-glucan or lichenan. Therefore, FGSG_05851 is a xyloglucan-specific glucanase (E.C. 3.2.1.151) rather than an endoglucanase (E.C. 3.2.1.4) with broad substrate specificity. FGSG_11037 displayed a peculiar behavior in that the xyloglucan binding was highly cooperative, with a Hill coefficient of 2.5. Finally, FGSG_05851 essentially degraded xyloglucan into hepta-, octa-, and nonasaccharides, whereas the three other enzymes yielded hepta- and octa-saccharides as well as larger molecules.

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References

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