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Low-molecular-weight xylanase from Trichoderma viride.

M Ujiie1, C Roy, M Yaguchi

  • 1Institute of Biological Sciences, National Research Council of Canada, Ottawa.

Applied and Environmental Microbiology
|June 1, 1991
PubMed
Summary
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Researchers isolated a Trichoderma viride endo-1,4-beta-xylanase, finding it homologous to other fungal and bacterial xylanases. This enzyme shows no cellulase activity, indicating its specific function in xylan degradation.

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Enzymes play crucial roles in biological processes.
  • Xylanases are important industrial enzymes for degrading plant biomass.

Purpose of the Study:

  • To isolate and characterize endo-1,4-beta-xylanase from Trichoderma viride.
  • To investigate the enzyme's properties and its homology to other xylanases.

Main Methods:

  • Isolation of endo-1,4-beta-xylanase from Trichoderma viride.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for molecular weight determination.
  • Isoelectric focusing (IEF) for pI value determination.
  • N-terminal amino acid sequencing and homology analysis.

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Main Results:

  • A true xylanase (EC 3.2.1.8) was isolated with no cellulase activity.
  • The enzyme exhibited a molecular weight of 22,000 Da and a pI of 9.3.
  • Significant homology was found between the N-terminal amino acid sequence of T. viride xylanase and xylanases from Schizophyllum commune and bacteria (>50% identity).

Conclusions:

  • The isolated enzyme is a specific endo-1,4-beta-xylanase.
  • The findings suggest a conserved N-terminal domain among fungal and bacterial xylanases.
  • This characterization provides insights into the structural and evolutionary relationships of xylanases.