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A xylan-degrading strain of Sulfolobus solfataricus: isolation and characterization of the xylanase activity

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Abstract

Two strains (Oα and X2) of the hyperthermophilic crenarchaeon Sulfolobus solfataricus strain MT4 were selected and isolated for their ability to grow on xylan. Oα and X2, grown on media containing oat spelt xylan and birchwood xylan as the sole nutrient source, respectively, produced the same thermostable xylanase that was demonstrated to be inducible in xylan cultures. In an oat spelt medium, S. solfataricus Oα underwent interesting morphological changes in the cell envelope, exhibiting mobile appendages not present in the typical coccal shape. The enzyme was prevalently membrane associated and showed a molecular mass of approximately 57.0 kDa. It was also highly thermostable, with a half-life of 47 min at 100°C, and exhibited an optimal temperature and pH of 90°C and 7.0, respectively. Xylo-oligosaccharides were the enzymatic products of xylan hydrolysis, and the smallest degradation product was xylobiose, thus indicating that the enzyme was an endoxylanase. The enzyme was able to bind weakly to crystalline cellulose (Avicel) and more strongly to insoluble xylan in a substrate amount-and temperature-dependent manner.

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Authors and Affiliations

  1. Istituto di Biochimica delle Proteine-CNR, Via P. Castellino 111, 80131 , Naples, Italy

    Raffaele Cannio, Mosè Rossi & Alessandra Morana

  2. Istituto Zooprofilattico Sperimentale delle Regioni Lazio e Toscana, Via Appia Nuova 1411, 00178 , Rome, Italy

    Natascia Di Prizito

Authors
  1. Raffaele Cannio
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  2. Natascia Di Prizito
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  3. Mosè Rossi
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  4. Alessandra Morana
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Correspondence to Alessandra Morana.

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Communicated by G. Antranikian

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Cannio, R., Di Prizito, N., Rossi, M. et al. A xylan-degrading strain of Sulfolobus solfataricus: isolation and characterization of the xylanase activity. Extremophiles 8, 117–124 (2004). https://doi.org/10.1007/s00792-003-0370-3

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  • DOI: https://doi.org/10.1007/s00792-003-0370-3

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