Production of beta-xylanase and beta-xylosidase by the extremely halophilic archaeon Halorhabdus utahensis

M. Wainø, K. Ingvorsen

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    The extremely halophilic archaeon, Halorhabdus utahensis, isolated from the Great Salt Lake, Utah, produced beta-xylanase and beta-xylosidase activities. Both enzymes were active over a broad NaCl range from near zero to 30% NaCl when tested with culture broth. A broad NaCl optimum was observed for beta-xylanase activity between 5% and 15% NaCl, while beta-xylosidase activity was highest at 5% NaCl. Almost half of the maximum activities remained at 27%-30% NaCl for both enzyme activities. When dialyzed culture supernatant and culture broth were employed for determination of beta-xylanase and beta-xylosidase stabilities, approximately 55% and 83% of the initial beta-xylanase and beta-xylosidase activities, respectively, remained after 24 h incubation at 20% NaCl. The enzymes were also shown to be slightly thermophilic: P-xylanase activity exhibiting two optima at 55degrees and 70degreesC, while beta-xylosidase activity was optimal at 65degreesC. SDS-PAGE and zymogram techniques revealed the presence of two xylan-degrading proteins of approximately 45 and 67 kDa in culture supernatants. To our knowledge, this paper is the first report on hemicellulose-degrading enzymes produced by an extremely halophilic archaeon.
    Original languageEnglish
    JournalExtremophiles
    Volume7
    Issue number2
    Pages (from-to)87-93
    ISSN1431-0651
    DOIs
    Publication statusPublished - 2003

    Keywords

    • beta-xylosidase
    • beta-xylanase
    • Archaea
    • Halorhabdus utahensis
    • halostable
    • halophilic

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