Purification and Characterization of β-1,3-Xylanase from a Marine Bacterium, Vibrio sp. XY-214

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概要

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• β-1,3-Xylanase was purified to gel electrophoretic homogeneity and 83-fold from a cell-free culture fluid of Vibrio sp. XY-214 by ammonium sulfate precipitation and successive chromatographies. The enzyme had a pl of 3.6 and a molecular mass of 52 kDa. The enzyme had the highest level of activity at pH 7.0 and 37℃. The enzyme activity was completely inhibited by Cu<2+>, Hg<2+>, and N-bromosuccinimide. The enzyme hydrolyzed β-1,3-xylan to produce mainly xylotriose and xylobiose but did not act xylobiose, ρ-nitrophenyl-β-D-xyloside, β-1,4-xylan, β-1,3-glucan, or carboxymethyl cellulose.

• 社団法人日本農芸化学会の論文
• 1999-11-23

著者

• Nakagawa Hiroki

  Faculty Of Agriculture Saga University

• ARAKI TOSHIYOSHI

  Faculty of Bioresources, Mie University

• MORISHITA TATSUO

  Faculty of Bioresources, Mie University

• Araki Toshiyoshi

  Faculty Of Bioresources Mie University

• Maeda Keiko

  Department Of Physics Engineering Mie University

• TANI Shuji

  Faculty of Bioresources, Mie University

• MAEDA Keiko

  Faculty of Bioresources, Mie University

• HASHIKAWA Shinnosuke

  Faculty of Bioresources, Mie University

• Tani Shuji

  Dep. Of Biological Mechanisms And Functions Graduate School Of Bioagricultural Sciences Nagoya Univ.

• Tani Shuji

  Department Of Biological Mechanisms And Functions Graduate School Of Bioagricultural Sciences Nagoya

• Morishita Tatsuo

  Faculty Of Bioresources Mie University

• Hashikawa Shinnosuke

  Faculty Of Bioresources Mie University

• Maeda Keiko

  Faculty Of Bioresources Mie University

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