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

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)408-413
    Number of pages6
    JournalBioscience, Biotechnology and Biochemistry
    Volume64
    Issue number2
    DOIs
    Publication statusPublished - 2000 Jan 1

    Keywords

    • Aeromonas caviae
    • Enzyme characteristics
    • Purification
    • Transxylosidase
    • Xylanase

    ASJC Scopus subject areas

    • Biotechnology
    • Analytical Chemistry
    • Biochemistry
    • Applied Microbiology and Biotechnology
    • Molecular Biology
    • Organic Chemistry

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