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ONLINEISSN:1347-6947
PRINTISSN:0916-8451
Bioscience, Biotechnology, and Biochemistry
Vol. 63 (1999) , No. 8 pp.1346-1352
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XynX, a Possible Exo-xylanase of Aeromonas caviae ME-1 that Produces Exclusively Xylobiose and Xylotetraose from Xylan
Kengo USUI1), Keiji IBATA1), Tohru SUZUKI1) and Keiichi KAWAI1)2)
1) Department of Biotechnology, Faculty of Agriculture, Gifu University
2) Molecular Genetics Research Center, Gifu University
(Received January 20, 1999)
(Accepted April 16, 1999)
  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.
Key words:exo-xylanase; Aeromonas caviae ME-1; Family 10; X2/X4-forming xylanase; gene cloning

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To cite this article:
Kengo USUI, Keiji IBATA, Tohru SUZUKI and Keiichi KAWAI, “XynX, a Possible Exo-xylanase of Aeromonas caviae ME-1 that Produces Exclusively Xylobiose and Xylotetraose from Xylan”, Biosci. Biotechnol. Biochem., Vol. 63, 1346-1352 (1999) .

doi:10.1271/bbb.63.1346
JOI  JST.JSTAGE/bbb/63.1346
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