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

Publication: Research - peer-reviewJournal article – Annual report year: 2003

  • Author: Wainø, M.

  • Author: Ingvorsen, K.

    Technical University of Denmark

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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
Publication date2003
Volume7
Issue2
Pages87-93
ISSN1431-0651
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 39

Keywords

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