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Enzymology and Protein Engineering

Purification and Properties of β-1, 4-Xylanase from Aeromonas caviae W-61

Dung Nguyen Viet, Yoshiyuki Kamio, Naoki Abe, Jun Kaneko, Kazuo Izaki
Dung Nguyen Viet
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Yoshiyuki Kamio
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Naoki Abe
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Jun Kaneko
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Kazuo Izaki
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ABSTRACT

Aeromonas caviae W-61, which was isolated from water samples at the Faculty of Agriculture, Tohoku University, produced β-1, 4-xylanase (1,4-β-d-xylan xylanohydrolase; EC 3.2.1.8) extracellularly. The xylanase was purified to homogeneity by using DEAE-Sephadex A-50, CM-Sephadex C-50, and Sephadex G-100 column chromatographies. The molecular weight of the purified enzyme was estimated to be 22,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point of the enzyme was 9.2. The optimal pH and temperature for the activity of the enzyme were 7.0 and 55°C, respectively. The enzyme was stable at pH 7.0 at temperatures of up to 50°C. As enzymatic products, various xylo-oligosaccharides such as xylobiose, xylotriose, xylotetraose, and xylopentaose were formed, and only a small amount of xylose was detected. The purified enzyme did not hydrolyze starch, cellulose, carboxymethylcellulose, or β-1, 3-xylan.

FOOTNOTES

  • ↵* Corresponding author.

  • ↵† Present address: Department of Microbiology, Hanoi Polytechnical University, Hanoi, Vietnam.

  • Copyright © 1991, American Society for Microbiology
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Purification and Properties of β-1, 4-Xylanase from Aeromonas caviae W-61
Dung Nguyen Viet, Yoshiyuki Kamio, Naoki Abe, Jun Kaneko, Kazuo Izaki
Applied and Environmental Microbiology Feb 1991, 57 (2) 445-449; DOI:

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Purification and Properties of β-1, 4-Xylanase from Aeromonas caviae W-61
Dung Nguyen Viet, Yoshiyuki Kamio, Naoki Abe, Jun Kaneko, Kazuo Izaki
Applied and Environmental Microbiology Feb 1991, 57 (2) 445-449; DOI:
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