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

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  • Purification and Characterization of .BETA.-1,3-Xylanase from a Marine Bacterium, Vibrio sp. XY-214.
  • Purification and Characterization of ベータ 1 3 Xylanase from a Marine Bacterium Vibrio sp.XY-214
  • Purification and Characterization of β-1,3-Xylanase from a Marine Bacterium,<i>Vibrio</i>sp. XY-214

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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°C. The enzyme activity was completely inhibited by Cu2+, Hg2+, and N-bromosuccinimide. The enzyme hydrolyzed β-1,3-xylan to produce mainly xylotriose and xylobiose but did not act on xylobiose, p-nitrophenyl-β-D-xyloside, β-1,4-xylan, β-1,3-glucan, or carboxymethyl cellulose.<br>

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