XynX, a Possible Exo-xylanase of Aeromonas caviae ME-1 that Produces Exclusively Xylobiose and Xylotetraose from Xylan.

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  • USUI Kengo
    Department of Biotechnology, Faculty of Agriculture, Gifu University
  • IBATA Keiji
    Department of Biotechnology, Faculty of Agriculture, Gifu University
  • SUZUKI Tohru
    Department of Biotechnology, Faculty of Agriculture, Gifu University
  • KAWAI Keiichi
    Department of Biotechnology, Faculty of Agriculture, Gifu University Molecular Genetics Research Center, Gifu University

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  • XynX, a Possible Exo-xylanase of<i>Aeromonas caviae</i>ME-1 that Produces Exclusively Xylobiose and Xylotetraose from Xylan
  • XynX, a possible exo-xylanase ofAeromonas caviae ME-1 that produces exclusively xylobiose and xylotetraose from xylan. Biosci

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Abstract

  A gene, xynX, encoding a novel xylanase, was cloned from Aeromonas caviae ME-1. This gene encoded an enzyme that was constituted of 334 amino acid residues (38,580 Da) and was similar in sequence to Family 10 (Family F) β-1,4 endo-xylanases. XynX produced only xylobiose and xylotetraose from birch wood xylan, and xylotriose, xylopentaose, and higher oligosaccharides were not detected in the TLC analysis. We designated it as X2/X4-forming xylanase. This enzyme does not have transglycosylation activity. These data suggested that this enzyme is a possible exo-xylanase. According to homology modeling, the enzyme has a ring-shaped (α/β)8 barrel (TIM barrel) structure, typical of Family 10 endo-xylanases, with the extraordinary feature of a longer bottom-loop structure.<br>

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