Purification and Some Properties of High-molecular-weight Xylanases, the Xylanases 4 and 5 of Aeromonas caviae W-61

Narayan Roy, Naoko Okai, Toshio Tomita, Koji Muramoto, Yoshiyuki Kamio

    研究成果: Article査読

    10 被引用数 (Scopus)

    抄録

    Aeromonas caviae W-61 produces multiple extracellular xylanases, the xylanases 1, 2, 3, 4, and 5 [Nguyen, V. D. et al., Biosci. Biotechnol. Biochem., 56, 1708-1712 (1993)]. Here we purified and characterized high-molecular-weight xylanases, the xylanases 4 and 5 from the culture fluids of the bacterium. The purified xylanases 4 and 5, which had molecular masses of 120 and 140 kDa, respectively, were endo-β-1,4-xylanases with similar enzymatic properties except for transxylosidase activity. The xylanase 4 showed a prominent transxylosidase activity when xylotriose and xylotetraose were used as the substrates, while the xylanase 5 had little transxylosidase activity under the same conditions. Protein sequencing indicated that the xylanase 4 was a C-terminally-truncated xylanase 5, suggesting that the C-terminal truncation of the xylanase 5 may endow the enzyme with transxylosidase activity.

    本文言語English
    ページ(範囲)408-413
    ページ数6
    ジャーナルBioscience, Biotechnology and Biochemistry
    64
    2
    DOI
    出版ステータスPublished - 2000 1月 1

    ASJC Scopus subject areas

    • バイオテクノロジー
    • 分析化学
    • 生化学
    • 応用微生物学とバイオテクノロジー
    • 分子生物学
    • 有機化学

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