Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Purification and Characterization of a Thermostable Xylanase from Fomitopsis pinicola

  • Shin, Keum (Department of Forest Products, Kookmin University) ;
  • Jeya, Marimuthu (Department of Chemical Engineering, Konkuk University) ;
  • Lee, Jung-Kul (Department of Chemical Engineering, Konkuk University) ;
  • Kim, Yeong-Suk (Department of Forest Products, Kookmin University)
  • Received : 2010.03.18
  • Accepted : 2010.06.23
  • Published : 2010.10.28
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Abstract

An extracellular xylanase was purified to homogeneity by sequential chromatography of Fomitopsis pinicola culture supernatants on a DEAE-Sepharose column, a gel filtration column, and then on a MonoQ column with fast protein liquid chromatography. The relative molecular mass of the F. pinicola xylanase was determined to be 58 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis and by size-exclusion chromatography, indicating that the enzyme is a monomer. The hydrolytic activity of the xylanase had a pH optimum of 4.5 and a temperature optimum of $70^{\circ}C$. The enzyme showed a $t_{1/2}$ value of 33 h at $70^{\circ}C$ and catalytic efficiency ($k_{cat}=77.4\;s^{-1}$, $k_{cat}/K_m$=22.7 mg/ml/s) for oatspelt xylan. Its internal amino acid sequences showed a significant homology with hydrolases from glycoside hydrolase (GH) family 10, indicating that the F. pinicola xylanase is a member of GH family 10.

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References

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