Purification and Characterization of ${\alpha}$-L-Arabinosidase from Trichoderma sp. SY

  • Jung, Bo-Ra (Bio/Molecular Informatics Center, Department of Molecular Biotechnology, Konkuk University) ;
  • Kim, Bong-Gyu (Bio/Molecular Informatics Center, Department of Molecular Biotechnology, Konkuk University) ;
  • Lee, Yoon-Jung (Bio/Molecular Informatics Center, Department of Molecular Biotechnology, Konkuk University) ;
  • Ahn, Joong-Hoon (Bio/Molecular Informatics Center, Department of Molecular Biotechnology, Konkuk University)
  • Published : 2005.03.31

Abstract

Trichoderma sp. SY most effectively produces an extracellular ${\gamma}$-L-arabinofuranosidase (AF) using arabinose as a carbon source. AF grown on cellulose as a carbon source was purified 28-fold with 4.4% yield by DEAE exchange and HQ/20 cation exchange chromatographies The purified enzyme was found to be homogeneous on SDS-PAGE with molecular weight of 89 kDa. It exhibited a high level of activity with p-nitrophenyl ${\alpha}$-L-arabinofuranoside, showing $K_m$ and $V_{max}$ values of $0.15\;{\mu}M$ and $239.85U{\cdot}mg^{-1}$, respectively and did not require any metal ion for activity. It also released p-nitrophenol from p-nitrophenol conjugated ${\beta}$-D-xylopyranoside, and ${\beta}$-D-galactopyranoside not from ${\beta}$-D-glucopyranoside.

Keywords

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