Discovery and characterization of a thermostable and highly halotolerant GH5 cellulase from an icelandic hot spring isolate

  • Zarafeta D
  • Kissas D
  • Sayer C
 et al. 
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With the ultimate goal of identifying robust cellulases for industrial biocatalytic conversions, we have isolated and characterized a new thermostable and very halotolerant GH5 cellulase. This new enzyme, termed CelDZ1, was identified by bioinformatic analysis from the genome of a polysaccharide-enrichment culture isolate, initiated from material collected from an Icelandic hot spring. Biochemical characterization of CelDZ1 revealed that it is a glycoside hydrolase with optimal activity at 70°C and pH 5.0 that exhibits good thermostability, high halotolerance at near-saturating salt concentrations, and resistance towards metal ions and other denaturing agents. X-ray crystallography of the new enzyme showed that CelDZ1 is the first reported cellulase structure that lacks the defined sugar-binding 2 subsite and revealed structural features which provide potential explanations of its biochemical characteristics.

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  • Dimitra Zarafeta

  • Dimitrios Kissas

  • Christopher Sayer

  • Sóley R. Gudbergsdottir

  • Efthymios Ladoukakis

  • Michail N. Isupov

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